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. 1995 Mar;59(1):94–123. doi: 10.1128/mr.59.1.94-123.1995

Protein-protein interactions: methods for detection and analysis.

E M Phizicky 1, S Fields 1
PMCID: PMC239356  PMID: 7708014

Abstract

The function and activity of a protein are often modulated by other proteins with which it interacts. This review is intended as a practical guide to the analysis of such protein-protein interactions. We discuss biochemical methods such as protein affinity chromatography, affinity blotting, coimmunoprecipitation, and cross-linking; molecular biological methods such as protein probing, the two-hybrid system, and phage display: and genetic methods such as the isolation of extragenic suppressors, synthetic mutants, and unlinked noncomplementing mutants. We next describe how binding affinities can be evaluated by techniques including protein affinity chromatography, sedimentation, gel filtration, fluorescence methods, solid-phase sampling of equilibrium solutions, and surface plasmon resonance. Finally, three examples of well-characterized domains involved in multiple protein-protein interactions are examined. The emphasis of the discussion is on variations in the approaches, concerns in evaluating the results, and advantages and disadvantages of the techniques.

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Selected References

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  1. Ackers G. K. Analytical gel chromatography of proteins. Adv Protein Chem. 1970;24:343–446. doi: 10.1016/s0065-3233(08)60245-4. [DOI] [PubMed] [Google Scholar]
  2. Adams A. E., Botstein D. Dominant suppressors of yeast actin mutations that are reciprocally suppressed. Genetics. 1989 Apr;121(4):675–683. doi: 10.1093/genetics/121.4.675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Alber T. Structure of the leucine zipper. Curr Opin Genet Dev. 1992 Apr;2(2):205–210. doi: 10.1016/s0959-437x(05)80275-8. [DOI] [PubMed] [Google Scholar]
  4. Alberts B., Miake-Lye R. Unscrambling the puzzle of biological machines: the importance of the details. Cell. 1992 Feb 7;68(3):415–420. doi: 10.1016/0092-8674(92)90179-g. [DOI] [PubMed] [Google Scholar]
  5. Ayer D. E., Kretzner L., Eisenman R. N. Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell. 1993 Jan 29;72(2):211–222. doi: 10.1016/0092-8674(93)90661-9. [DOI] [PubMed] [Google Scholar]
  6. Baird B. A., Hammes G. G. Chemical cross-linking studies of chloroplast coupling factor 1. J Biol Chem. 1976 Nov 25;251(22):6953–6962. [PubMed] [Google Scholar]
  7. Ballinger D. G., Xue N., Harshman K. D. A Drosophila photoreceptor cell-specific protein, calphotin, binds calcium and contains a leucine zipper. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1536–1540. doi: 10.1073/pnas.90.4.1536. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Banik U., Mandal N. C., Bhattacharyya B., Roy S. A fluorescence anisotropy study of tetramer-dimer equilibrium of lambda repressor and its implication for function. J Biol Chem. 1993 Feb 25;268(6):3938–3943. [PubMed] [Google Scholar]
  9. Barbas C. F., 3rd, Kang A. S., Lerner R. A., Benkovic S. J. Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):7978–7982. doi: 10.1073/pnas.88.18.7978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Bass S., Greene R., Wells J. A. Hormone phage: an enrichment method for variant proteins with altered binding properties. Proteins. 1990;8(4):309–314. doi: 10.1002/prot.340080405. [DOI] [PubMed] [Google Scholar]
  11. Basson M. E., Moore R. L., O'Rear J., Rine J. Identifying mutations in duplicated functions in Saccharomyces cerevisiae: recessive mutations in HMG-CoA reductase genes. Genetics. 1987 Dec;117(4):645–655. doi: 10.1093/genetics/117.4.645. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Beckett D., Koblan K. S., Ackers G. K. Quantitative study of protein association at picomolar concentrations: the lambda phage cl repressor. Anal Biochem. 1991 Jul;196(1):69–75. doi: 10.1016/0003-2697(91)90118-d. [DOI] [PubMed] [Google Scholar]
  13. Beeckmans S., Kanarek L. Demonstration of physical interactions between consecutive enzymes of the citric acid cycle and of the aspartate-malate shuttle. A study involving fumarase, malate dehydrogenase, citrate synthesis and aspartate aminotransferase. Eur J Biochem. 1981 Jul;117(3):527–535. doi: 10.1111/j.1432-1033.1981.tb06369.x. [DOI] [PubMed] [Google Scholar]
  14. Bender A., Pringle J. R. Use of a screen for synthetic lethal and multicopy suppressee mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae. Mol Cell Biol. 1991 Mar;11(3):1295–1305. doi: 10.1128/mcb.11.3.1295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Birge R. B., Fajardo J. E., Reichman C., Shoelson S. E., Songyang Z., Cantley L. C., Hanafusa H. Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol Cell Biol. 1993 Aug;13(8):4648–4656. doi: 10.1128/mcb.13.8.4648. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Blackwood E. M., Eisenman R. N. Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science. 1991 Mar 8;251(4998):1211–1217. doi: 10.1126/science.2006410. [DOI] [PubMed] [Google Scholar]
  17. Blanar M. A., Rutter W. J. Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-Fos. Science. 1992 May 15;256(5059):1014–1018. doi: 10.1126/science.1589769. [DOI] [PubMed] [Google Scholar]
  18. Bleil J. D., Wassarman P. M. Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking. Proc Natl Acad Sci U S A. 1990 Jul;87(14):5563–5567. doi: 10.1073/pnas.87.14.5563. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Booker G. W., Breeze A. L., Downing A. K., Panayotou G., Gout I., Waterfield M. D., Campbell I. D. Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase. Nature. 1992 Aug 20;358(6388):684–687. doi: 10.1038/358684a0. [DOI] [PubMed] [Google Scholar]
  20. Bragg P. D., Hou C. A cross-linking study of the Ca2+, Mg2+-activated adenosine triphosphatase of Escherichia coli. Eur J Biochem. 1980 May;106(2):495–503. doi: 10.1111/j.1432-1033.1980.tb04596.x. [DOI] [PubMed] [Google Scholar]
  21. Bragg P. D., Hou C. Chemical crosslinking of alpha subunits in the F1 adenosine triphosphatase of Escherichia coli. Arch Biochem Biophys. 1986 Jan;244(1):361–372. doi: 10.1016/0003-9861(86)90125-6. [DOI] [PubMed] [Google Scholar]
  22. Brent R., Ptashne M. A eukaryotic transcriptional activator bearing the DNA specificity of a prokaryotic repressor. Cell. 1985 Dec;43(3 Pt 2):729–736. doi: 10.1016/0092-8674(85)90246-6. [DOI] [PubMed] [Google Scholar]
  23. Bretscher A., Weber K. Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner. Cell. 1980 Jul;20(3):839–847. doi: 10.1016/0092-8674(80)90330-x. [DOI] [PubMed] [Google Scholar]
  24. Brown R. L. Functional regions of the inhibitory subunit of retinal rod cGMP phosphodiesterase identified by site-specific mutagenesis and fluorescence spectroscopy. Biochemistry. 1992 Jun 30;31(25):5918–5925. doi: 10.1021/bi00140a031. [DOI] [PubMed] [Google Scholar]
  25. Burton D. R., Barbas C. F., 3rd, Persson M. A., Koenig S., Chanock R. M., Lerner R. A. A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc Natl Acad Sci U S A. 1991 Nov 15;88(22):10134–10137. doi: 10.1073/pnas.88.22.10134. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Calakos N., Bennett M. K., Peterson K. E., Scheller R. H. Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking. Science. 1994 Feb 25;263(5150):1146–1149. doi: 10.1126/science.8108733. [DOI] [PubMed] [Google Scholar]
  27. Carr D. W., Scott J. D. Blotting and band-shifting: techniques for studying protein-protein interactions. Trends Biochem Sci. 1992 Jul;17(7):246–249. doi: 10.1016/0968-0004(92)90402-u. [DOI] [PubMed] [Google Scholar]
  28. Chardin P., Camonis J. H., Gale N. W., van Aelst L., Schlessinger J., Wigler M. H., Bar-Sagi D. Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2. Science. 1993 May 28;260(5112):1338–1343. doi: 10.1126/science.8493579. [DOI] [PubMed] [Google Scholar]
  29. Chellappan S. P., Hiebert S., Mudryj M., Horowitz J. M., Nevins J. R. The E2F transcription factor is a cellular target for the RB protein. Cell. 1991 Jun 14;65(6):1053–1061. doi: 10.1016/0092-8674(91)90557-f. [DOI] [PubMed] [Google Scholar]
  30. Chellappan S., Kraus V. B., Kroger B., Munger K., Howley P. M., Phelps W. C., Nevins J. R. Adenovirus E1A, simian virus 40 tumor antigen, and human papillomavirus E7 protein share the capacity to disrupt the interaction between transcription factor E2F and the retinoblastoma gene product. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4549–4553. doi: 10.1073/pnas.89.10.4549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Chen Y., Ebright Y. W., Ebright R. H. Identification of the target of a transcription activator protein by protein-protein photocrosslinking. Science. 1994 Jul 1;265(5168):90–92. doi: 10.1126/science.8016656. [DOI] [PubMed] [Google Scholar]
  32. Chevray P. M., Nathans D. Protein interaction cloning in yeast: identification of mammalian proteins that react with the leucine zipper of Jun. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):5789–5793. doi: 10.1073/pnas.89.13.5789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Chien C. T., Bartel P. L., Sternglanz R., Fields S. The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9578–9582. doi: 10.1073/pnas.88.21.9578. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Cicchetti P., Mayer B. J., Thiel G., Baltimore D. Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. Science. 1992 Aug 7;257(5071):803–806. doi: 10.1126/science.1379745. [DOI] [PubMed] [Google Scholar]
  35. Clackson T., Hoogenboom H. R., Griffiths A. D., Winter G. Making antibody fragments using phage display libraries. Nature. 1991 Aug 15;352(6336):624–628. doi: 10.1038/352624a0. [DOI] [PubMed] [Google Scholar]
  36. Cohen B. D., Lowy D. R., Schiller J. T. The conserved C-terminal domain of the bovine papillomavirus E5 oncoprotein can associate with an alpha-adaptin-like molecule: a possible link between growth factor receptors and viral transformation. Mol Cell Biol. 1993 Oct;13(10):6462–6468. doi: 10.1128/mcb.13.10.6462. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Cornish V. W., Benson D. R., Altenbach C. A., Hideg K., Hubbell W. L., Schultz P. G. Site-specific incorporation of biophysical probes into proteins. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2910–2914. doi: 10.1073/pnas.91.8.2910. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Costigan C., Gehrung S., Snyder M. A synthetic lethal screen identifies SLK1, a novel protein kinase homolog implicated in yeast cell morphogenesis and cell growth. Mol Cell Biol. 1992 Mar;12(3):1162–1178. doi: 10.1128/mcb.12.3.1162. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Cover J. A., Lambert J. M., Norman C. M., Traut R. R. Identification of proteins at the subunit interface of the Escherichia coli ribosome by cross-linking with dimethyl 3,3'-dithiobis(propionimidate). Biochemistry. 1981 May 12;20(10):2843–2852. doi: 10.1021/bi00513a021. [DOI] [PubMed] [Google Scholar]
  40. Cull M. G., Miller J. F., Schatz P. J. Screening for receptor ligands using large libraries of peptides linked to the C terminus of the lac repressor. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1865–1869. doi: 10.1073/pnas.89.5.1865. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Cwirla S. E., Peters E. A., Barrett R. W., Dower W. J. Peptides on phage: a vast library of peptides for identifying ligands. Proc Natl Acad Sci U S A. 1990 Aug;87(16):6378–6382. doi: 10.1073/pnas.87.16.6378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Dalton S., Treisman R. Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell. 1992 Feb 7;68(3):597–612. doi: 10.1016/0092-8674(92)90194-h. [DOI] [PubMed] [Google Scholar]
  43. Dang C. V., Barrett J., Villa-Garcia M., Resar L. M., Kato G. J., Fearon E. R. Intracellular leucine zipper interactions suggest c-Myc hetero-oligomerization. Mol Cell Biol. 1991 Feb;11(2):954–962. doi: 10.1128/mcb.11.2.954. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Darawshe S., Rivas G., Minton A. P. Sedimentation equilibrium-quantitative polyacrylamide gel electrophoresis (SE-QPAGE): a new technique for the detection of associations in multicomponent solutions. Anal Biochem. 1993 Dec;215(2):236–242. doi: 10.1006/abio.1993.1581. [DOI] [PubMed] [Google Scholar]
  45. Denny J. B., Blobel G. 125I-labeled crosslinking reagent that is hydrophilic, photoactivatable, and cleavable through an azo linkage. Proc Natl Acad Sci U S A. 1984 Sep;81(17):5286–5290. doi: 10.1073/pnas.81.17.5286. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Devlin J. J., Panganiban L. C., Devlin P. E. Random peptide libraries: a source of specific protein binding molecules. Science. 1990 Jul 27;249(4967):404–406. doi: 10.1126/science.2143033. [DOI] [PubMed] [Google Scholar]
  47. Diamond M. I., Miner J. N., Yoshinaga S. K., Yamamoto K. R. Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science. 1990 Sep 14;249(4974):1266–1272. doi: 10.1126/science.2119054. [DOI] [PubMed] [Google Scholar]
  48. Drubin D. G., Miller K. G., Botstein D. Yeast actin-binding proteins: evidence for a role in morphogenesis. J Cell Biol. 1988 Dec;107(6 Pt 2):2551–2561. doi: 10.1083/jcb.107.6.2551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Dumont M. E., Corin A. F., Campbell G. A. Noncovalent binding of heme induces a compact apocytochrome c structure. Biochemistry. 1994 Jun 14;33(23):7368–7378. doi: 10.1021/bi00189a043. [DOI] [PubMed] [Google Scholar]
  50. Durfee T., Becherer K., Chen P. L., Yeh S. H., Yang Y., Kilburn A. E., Lee W. H., Elledge S. J. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 1993 Apr;7(4):555–569. doi: 10.1101/gad.7.4.555. [DOI] [PubMed] [Google Scholar]
  51. Ellenberger T. E., Brandl C. J., Struhl K., Harrison S. C. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex. Cell. 1992 Dec 24;71(7):1223–1237. doi: 10.1016/s0092-8674(05)80070-4. [DOI] [PubMed] [Google Scholar]
  52. Evans P. R., Farrants G. W., Hudson P. J. Phosphofructokinase: structure and control. Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):53–62. doi: 10.1098/rstb.1981.0059. [DOI] [PubMed] [Google Scholar]
  53. Ewen M. E., Faha B., Harlow E., Livingston D. M. Interaction of p107 with cyclin A independent of complex formation with viral oncoproteins. Science. 1992 Jan 3;255(5040):85–87. doi: 10.1126/science.1532457. [DOI] [PubMed] [Google Scholar]
  54. Faha B., Ewen M. E., Tsai L. H., Livingston D. M., Harlow E. Interaction between human cyclin A and adenovirus E1A-associated p107 protein. Science. 1992 Jan 3;255(5040):87–90. doi: 10.1126/science.1532458. [DOI] [PubMed] [Google Scholar]
  55. Fahien L. A., Smith S. E. The enzyme-enzyme complex of transaminase and glutamate dehydrogenase. J Biol Chem. 1974 May 10;249(9):2696–2703. [PubMed] [Google Scholar]
  56. Felder S., Zhou M., Hu P., Ureña J., Ullrich A., Chaudhuri M., White M., Shoelson S. E., Schlessinger J. SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol Cell Biol. 1993 Mar;13(3):1449–1455. doi: 10.1128/mcb.13.3.1449. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Fields S., Song O. A novel genetic system to detect protein-protein interactions. Nature. 1989 Jul 20;340(6230):245–246. doi: 10.1038/340245a0. [DOI] [PubMed] [Google Scholar]
  58. Fields S., Sternglanz R. The two-hybrid system: an assay for protein-protein interactions. Trends Genet. 1994 Aug;10(8):286–292. doi: 10.1016/0168-9525(90)90012-u. [DOI] [PubMed] [Google Scholar]
  59. Finlay C. A., Hinds P. W., Levine A. J. The p53 proto-oncogene can act as a suppressor of transformation. Cell. 1989 Jun 30;57(7):1083–1093. doi: 10.1016/0092-8674(89)90045-7. [DOI] [PubMed] [Google Scholar]
  60. Flynn D. C., Leu T. H., Reynolds A. B., Parsons J. T. Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate. Mol Cell Biol. 1993 Dec;13(12):7892–7900. doi: 10.1128/mcb.13.12.7892. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Formosa T., Barry J., Alberts B. M., Greenblatt J. Using protein affinity chromatography to probe structure of protein machines. Methods Enzymol. 1991;208:24–45. doi: 10.1016/0076-6879(91)08005-3. [DOI] [PubMed] [Google Scholar]
  62. Friguet B., Chaffotte A. F., Djavadi-Ohaniance L., Goldberg M. E. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J Immunol Methods. 1985 Mar 18;77(2):305–319. doi: 10.1016/0022-1759(85)90044-4. [DOI] [PubMed] [Google Scholar]
  63. Gegner J. A., Dahlquist F. W. Signal transduction in bacteria: CheW forms a reversible complex with the protein kinase CheA. Proc Natl Acad Sci U S A. 1991 Feb 1;88(3):750–754. doi: 10.1073/pnas.88.3.750. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Geiser J. R., Sundberg H. A., Chang B. H., Muller E. G., Davis T. N. The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae. Mol Cell Biol. 1993 Dec;13(12):7913–7924. doi: 10.1128/mcb.13.12.7913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Germino F. J., Wang Z. X., Weissman S. M. Screening for in vivo protein-protein interactions. Proc Natl Acad Sci U S A. 1993 Feb 1;90(3):933–937. doi: 10.1073/pnas.90.3.933. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Gilbert G. A., Kellett G. L. Interacting systems of the type A + B = C. J Biol Chem. 1971 Oct 10;246(19):6079–6086. [PubMed] [Google Scholar]
  67. Gill S. C., Weitzel S. E., von Hippel P. H. Escherichia coli sigma 70 and NusA proteins. I. Binding interactions with core RNA polymerase in solution and within the transcription complex. J Mol Biol. 1991 Jul 20;220(2):307–324. doi: 10.1016/0022-2836(91)90015-x. [DOI] [PubMed] [Google Scholar]
  68. Glenney J. R., Jr, Weber K. Detection of calmodulin-binding polypeptides separated in SDS-polyacrylamide gels by a sensitive [125I]calmodulin gel overlay assay. Methods Enzymol. 1983;102:204–210. doi: 10.1016/s0076-6879(83)02021-2. [DOI] [PubMed] [Google Scholar]
  69. Goodsell D. S., Olson A. J. Soluble proteins: size, shape and function. Trends Biochem Sci. 1993 Mar;18(3):65–68. doi: 10.1016/0968-0004(93)90153-e. [DOI] [PubMed] [Google Scholar]
  70. Greenblatt J., Li J. The nusA gene protein of Escherichia coli. Its identification and a demonstration that it interacts with the gene N transcription anti-termination protein of bacteriophage lambda. J Mol Biol. 1981 Mar 25;147(1):11–23. doi: 10.1016/0022-2836(81)90076-0. [DOI] [PubMed] [Google Scholar]
  71. Gross M., Wallimann T. Kinetics of assembly and dissociation of the mitochondrial creatine kinase octamer. A fluorescence study. Biochemistry. 1993 Dec 21;32(50):13933–13940. doi: 10.1021/bi00213a024. [DOI] [PubMed] [Google Scholar]
  72. Görlich D., Hartmann E., Prehn S., Rapoport T. A. A protein of the endoplasmic reticulum involved early in polypeptide translocation. Nature. 1992 May 7;357(6373):47–52. doi: 10.1038/357047a0. [DOI] [PubMed] [Google Scholar]
  73. HUMMEL J. P., DREYER W. J. Measurement of protein-binding phenomena by gel filtration. Biochim Biophys Acta. 1962 Oct 8;63:530–532. doi: 10.1016/0006-3002(62)90124-5. [DOI] [PubMed] [Google Scholar]
  74. Hadwiger J. A., Wittenberg C., Richardson H. E., de Barros Lopes M., Reed S. I. A family of cyclin homologs that control the G1 phase in yeast. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6255–6259. doi: 10.1073/pnas.86.16.6255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Hannon G. J., Demetrick D., Beach D. Isolation of the Rb-related p130 through its interaction with CDK2 and cyclins. Genes Dev. 1993 Dec;7(12A):2378–2391. doi: 10.1101/gad.7.12a.2378. [DOI] [PubMed] [Google Scholar]
  76. Harlow E., Whyte P., Franza B. R., Jr, Schley C. Association of adenovirus early-region 1A proteins with cellular polypeptides. Mol Cell Biol. 1986 May;6(5):1579–1589. doi: 10.1128/mcb.6.5.1579. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Harper J. W., Adami G. R., Wei N., Keyomarsi K., Elledge S. J. The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell. 1993 Nov 19;75(4):805–816. doi: 10.1016/0092-8674(93)90499-g. [DOI] [PubMed] [Google Scholar]
  78. Hartman P. E., Roth J. R. Mechanisms of suppression. Adv Genet. 1973;17:1–105. doi: 10.1016/s0065-2660(08)60170-4. [DOI] [PubMed] [Google Scholar]
  79. Hartmann E., Wiedmann M., Rapoport T. A. A membrane component of the endoplasmic reticulum that may be essential for protein translocation. EMBO J. 1989 Aug;8(8):2225–2229. doi: 10.1002/j.1460-2075.1989.tb08346.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Herberg F. W., Dostmann W. R., Zorn M., Davis S. J., Taylor S. S. Crosstalk between domains in the regulatory subunit of cAMP-dependent protein kinase: influence of amino terminus on cAMP binding and holoenzyme formation. Biochemistry. 1994 Jun 14;33(23):7485–7494. doi: 10.1021/bi00189a057. [DOI] [PubMed] [Google Scholar]
  81. Herberg F. W., Taylor S. S. Physiological inhibitors of the catalytic subunit of cAMP-dependent protein kinase: effect of MgATP on protein-protein interactions. Biochemistry. 1993 Dec 21;32(50):14015–14022. doi: 10.1021/bi00213a035. [DOI] [PubMed] [Google Scholar]
  82. Herskowitz I. Functional inactivation of genes by dominant negative mutations. Nature. 1987 Sep 17;329(6136):219–222. doi: 10.1038/329219a0. [DOI] [PubMed] [Google Scholar]
  83. Heyduk T., Lee J. C., Ebright Y. W., Blatter E. E., Zhou Y., Ebright R. H. CAP interacts with RNA polymerase in solution in the absence of promoter DNA. Nature. 1993 Aug 5;364(6437):548–549. doi: 10.1038/364548a0. [DOI] [PubMed] [Google Scholar]
  84. Hiebert S. W., Chellappan S. P., Horowitz J. M., Nevins J. R. The interaction of RB with E2F coincides with an inhibition of the transcriptional activity of E2F. Genes Dev. 1992 Feb;6(2):177–185. doi: 10.1101/gad.6.2.177. [DOI] [PubMed] [Google Scholar]
  85. Hieter P., Mann C., Snyder M., Davis R. W. Mitotic stability of yeast chromosomes: a colony color assay that measures nondisjunction and chromosome loss. Cell. 1985 Feb;40(2):381–392. doi: 10.1016/0092-8674(85)90152-7. [DOI] [PubMed] [Google Scholar]
  86. Hill R. L., Brew K. Lactose synthetase. Adv Enzymol Relat Areas Mol Biol. 1975;43:411–490. doi: 10.1002/9780470122884.ch5. [DOI] [PubMed] [Google Scholar]
  87. Hope I. A., Struhl K. Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast. Cell. 1986 Sep 12;46(6):885–894. doi: 10.1016/0092-8674(86)90070-x. [DOI] [PubMed] [Google Scholar]
  88. Hu J. C., O'Shea E. K., Kim P. S., Sauer R. T. Sequence requirements for coiled-coils: analysis with lambda repressor-GCN4 leucine zipper fusions. Science. 1990 Dec 7;250(4986):1400–1403. doi: 10.1126/science.2147779. [DOI] [PubMed] [Google Scholar]
  89. Hu P., Margolis B., Skolnik E. Y., Lammers R., Ullrich A., Schlessinger J. Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors. Mol Cell Biol. 1992 Mar;12(3):981–990. doi: 10.1128/mcb.12.3.981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Huang S., Lee W. H., Lee E. Y. A cellular protein that competes with SV40 T antigen for binding to the retinoblastoma gene product. Nature. 1991 Mar 14;350(6314):160–162. doi: 10.1038/350160a0. [DOI] [PubMed] [Google Scholar]
  91. Huffaker T. C., Hoyt M. A., Botstein D. Genetic analysis of the yeast cytoskeleton. Annu Rev Genet. 1987;21:259–284. doi: 10.1146/annurev.ge.21.120187.001355. [DOI] [PubMed] [Google Scholar]
  92. Hurley J. B., Stryer L. Purification and characterization of the gamma regulatory subunit of the cyclic GMP phosphodiesterase from retinal rod outer segments. J Biol Chem. 1982 Sep 25;257(18):11094–11099. [PubMed] [Google Scholar]
  93. Iwabuchi K., Li B., Bartel P., Fields S. Use of the two-hybrid system to identify the domain of p53 involved in oligomerization. Oncogene. 1993 Jun;8(6):1693–1696. [PubMed] [Google Scholar]
  94. James P., Inui M., Tada M., Chiesi M., Carafoli E. Nature and site of phospholamban regulation of the Ca2+ pump of sarcoplasmic reticulum. Nature. 1989 Nov 2;342(6245):90–92. doi: 10.1038/342090a0. [DOI] [PubMed] [Google Scholar]
  95. Jarvik J., Botstein D. Conditional-lethal mutations that suppress genetic defects in morphogenesis by altering structural proteins. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2738–2742. doi: 10.1073/pnas.72.7.2738. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Jarvis T. C., Ring D. M., Daube S. S., von Hippel P. H. "Macromolecular crowding": thermodynamic consequences for protein-protein interactions within the T4 DNA replication complex. J Biol Chem. 1990 Sep 5;265(25):15160–15167. [PubMed] [Google Scholar]
  97. Jönsson U., Fägerstam L., Ivarsson B., Johnsson B., Karlsson R., Lundh K., Löfås S., Persson B., Roos H., Rönnberg I. Real-time biospecific interaction analysis using surface plasmon resonance and a sensor chip technology. Biotechniques. 1991 Nov;11(5):620–627. [PubMed] [Google Scholar]
  98. Kang A. S., Barbas C. F., Janda K. D., Benkovic S. J., Lerner R. A. Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces. Proc Natl Acad Sci U S A. 1991 May 15;88(10):4363–4366. doi: 10.1073/pnas.88.10.4363. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Karlsson R., Michaelsson A., Mattsson L. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J Immunol Methods. 1991 Dec 15;145(1-2):229–240. doi: 10.1016/0022-1759(91)90331-9. [DOI] [PubMed] [Google Scholar]
  100. Keegan L., Gill G., Ptashne M. Separation of DNA binding from the transcription-activating function of a eukaryotic regulatory protein. Science. 1986 Feb 14;231(4739):699–704. doi: 10.1126/science.3080805. [DOI] [PubMed] [Google Scholar]
  101. Kellogg D. R., Field C. M., Alberts B. M. Identification of microtubule-associated proteins in the centrosome, spindle, and kinetochore of the early Drosophila embryo. J Cell Biol. 1989 Dec;109(6 Pt 1):2977–2991. doi: 10.1083/jcb.109.6.2977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Kerppola T. K., Curran T. Fos-Jun heterodimers and Jun homodimers bend DNA in opposite orientations: implications for transcription factor cooperativity. Cell. 1991 Jul 26;66(2):317–326. doi: 10.1016/0092-8674(91)90621-5. [DOI] [PubMed] [Google Scholar]
  103. Kim Y. T., Tabor S., Churchich J. E., Richardson C. C. Interactions of gene 2.5 protein and DNA polymerase of bacteriophage T7. J Biol Chem. 1992 Jul 25;267(21):15032–15040. [PubMed] [Google Scholar]
  104. Koch C. A., Anderson D., Moran M. F., Ellis C., Pawson T. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science. 1991 May 3;252(5006):668–674. doi: 10.1126/science.1708916. [DOI] [PubMed] [Google Scholar]
  105. Kohda D., Hatanaka H., Odaka M., Mandiyan V., Ullrich A., Schlessinger J., Inagaki F. Solution structure of the SH3 domain of phospholipase C-gamma. Cell. 1993 Mar 26;72(6):953–960. doi: 10.1016/0092-8674(93)90583-c. [DOI] [PubMed] [Google Scholar]
  106. Koshland D., Kent J. C., Hartwell L. H. Genetic analysis of the mitotic transmission of minichromosomes. Cell. 1985 Feb;40(2):393–403. doi: 10.1016/0092-8674(85)90153-9. [DOI] [PubMed] [Google Scholar]
  107. Koyama S., Yu H., Dalgarno D. C., Shin T. B., Zydowsky L. D., Schreiber S. L. Structure of the PI3K SH3 domain and analysis of the SH3 family. Cell. 1993 Mar 26;72(6):945–952. doi: 10.1016/0092-8674(93)90582-b. [DOI] [PubMed] [Google Scholar]
  108. Krieg U. C., Johnson A. E., Walter P. Protein translocation across the endoplasmic reticulum membrane: identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel. J Cell Biol. 1989 Nov;109(5):2033–2043. doi: 10.1083/jcb.109.5.2033. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Kukuruzinska M. A., Turner B. W., Ackers G. K., Roseman S. Subunit association of enzyme I of the Salmonella typhimurium phosphoenolpyruvate: glycose phosphotransferase system. Temperature dependence and thermodynamic properties. J Biol Chem. 1984 Oct 10;259(19):11679–11681. [PubMed] [Google Scholar]
  110. Kwon O. S., Churchich J. E. Interaction of 70-kDA heat shock cognate protein with peptides and myo-inositol monophosphatase. J Biol Chem. 1994 Jan 7;269(1):266–271. [PubMed] [Google Scholar]
  111. Landschulz W. H., Johnson P. F., McKnight S. L. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science. 1988 Jun 24;240(4860):1759–1764. doi: 10.1126/science.3289117. [DOI] [PubMed] [Google Scholar]
  112. Lazarides E., Lindberg U. Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4742–4746. doi: 10.1073/pnas.71.12.4742. [DOI] [PMC free article] [PubMed] [Google Scholar]
  113. Lee F. S., Auld D. S., Vallee B. L. Tryptophan fluorescence as a probe of placental ribonuclease inhibitor binding to angiogenin. Biochemistry. 1989 Jan 10;28(1):219–224. doi: 10.1021/bi00427a030. [DOI] [PubMed] [Google Scholar]
  114. Lee F. S., Shapiro R., Vallee B. L. Tight-binding inhibition of angiogenin and ribonuclease A by placental ribonuclease inhibitor. Biochemistry. 1989 Jan 10;28(1):225–230. doi: 10.1021/bi00427a031. [DOI] [PubMed] [Google Scholar]
  115. Li B., Fields S. Identification of mutations in p53 that affect its binding to SV40 large T antigen by using the yeast two-hybrid system. FASEB J. 1993 Jul;7(10):957–963. doi: 10.1096/fasebj.7.10.8344494. [DOI] [PubMed] [Google Scholar]
  116. Li N., Batzer A., Daly R., Yajnik V., Skolnik E., Chardin P., Bar-Sagi D., Margolis B., Schlessinger J. Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling. Nature. 1993 May 6;363(6424):85–88. doi: 10.1038/363085a0. [DOI] [PubMed] [Google Scholar]
  117. Li S., Sedivy J. M. Raf-1 protein kinase activates the NF-kappa B transcription factor by dissociating the cytoplasmic NF-kappa B-I kappa B complex. Proc Natl Acad Sci U S A. 1993 Oct 15;90(20):9247–9251. doi: 10.1073/pnas.90.20.9247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  118. Liu X., Marengere L. E., Koch C. A., Pawson T. The v-Src SH3 domain binds phosphatidylinositol 3'-kinase. Mol Cell Biol. 1993 Sep;13(9):5225–5232. doi: 10.1128/mcb.13.9.5225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  119. Lowman H. B., Bass S. H., Simpson N., Wells J. A. Selecting high-affinity binding proteins by monovalent phage display. Biochemistry. 1991 Nov 12;30(45):10832–10838. doi: 10.1021/bi00109a004. [DOI] [PubMed] [Google Scholar]
  120. Ludlow J. W., DeCaprio J. A., Huang C. M., Lee W. H., Paucha E., Livingston D. M. SV40 large T antigen binds preferentially to an underphosphorylated member of the retinoblastoma susceptibility gene product family. Cell. 1989 Jan 13;56(1):57–65. doi: 10.1016/0092-8674(89)90983-5. [DOI] [PubMed] [Google Scholar]
  121. Ludlow J. W., Glendening C. L., Livingston D. M., DeCarprio J. A. Specific enzymatic dephosphorylation of the retinoblastoma protein. Mol Cell Biol. 1993 Jan;13(1):367–372. doi: 10.1128/mcb.13.1.367. [DOI] [PMC free article] [PubMed] [Google Scholar]
  122. MONOD J., WYMAN J., CHANGEUX J. P. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965 May;12:88–118. doi: 10.1016/s0022-2836(65)80285-6. [DOI] [PubMed] [Google Scholar]
  123. Ma J., Ptashne M. A new class of yeast transcriptional activators. Cell. 1987 Oct 9;51(1):113–119. doi: 10.1016/0092-8674(87)90015-8. [DOI] [PubMed] [Google Scholar]
  124. Macgregor P. F., Abate C., Curran T. Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1. Oncogene. 1990 Apr;5(4):451–458. [PubMed] [Google Scholar]
  125. Malmqvist M. Biospecific interaction analysis using biosensor technology. Nature. 1993 Jan 14;361(6408):186–187. doi: 10.1038/361186a0. [DOI] [PubMed] [Google Scholar]
  126. Marengere L. E., Songyang Z., Gish G. D., Schaller M. D., Parsons J. T., Stern M. J., Cantley L. C., Pawson T. SH2 domain specificity and activity modified by a single residue. Nature. 1994 Jun 9;369(6480):502–505. doi: 10.1038/369502a0. [DOI] [PubMed] [Google Scholar]
  127. Mason S. W., Li J., Greenblatt J. Direct interaction between two Escherichia coli transcription antitermination factors, NusB and ribosomal protein S10. J Mol Biol. 1992 Jan 5;223(1):55–66. doi: 10.1016/0022-2836(92)90715-v. [DOI] [PubMed] [Google Scholar]
  128. Mayer B. J., Jackson P. K., Baltimore D. The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):627–631. doi: 10.1073/pnas.88.2.627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  129. Mayer B. J., Jackson P. K., Van Etten R. A., Baltimore D. Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo. Mol Cell Biol. 1992 Feb;12(2):609–618. doi: 10.1128/mcb.12.2.609. [DOI] [PMC free article] [PubMed] [Google Scholar]
  130. McCafferty J., Griffiths A. D., Winter G., Chiswell D. J. Phage antibodies: filamentous phage displaying antibody variable domains. Nature. 1990 Dec 6;348(6301):552–554. doi: 10.1038/348552a0. [DOI] [PubMed] [Google Scholar]
  131. Meeks-Wagner D., Hartwell L. H. Normal stoichiometry of histone dimer sets is necessary for high fidelity of mitotic chromosome transmission. Cell. 1986 Jan 17;44(1):43–52. doi: 10.1016/0092-8674(86)90483-6. [DOI] [PubMed] [Google Scholar]
  132. Miller K. G., Alberts B. M. F-actin affinity chromatography: technique for isolating previously unidentified actin-binding proteins. Proc Natl Acad Sci U S A. 1989 Jul;86(13):4808–4812. doi: 10.1073/pnas.86.13.4808. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. Miller K. G., Field C. M., Alberts B. M., Kellogg D. R. Use of actin filament and microtubule affinity chromatography to identify proteins that bind to the cytoskeleton. Methods Enzymol. 1991;196:303–319. doi: 10.1016/0076-6879(91)96028-p. [DOI] [PubMed] [Google Scholar]
  134. Mills J. S., Walsh M. P., Nemcek K., Johnson J. D. Biologically active fluorescent derivatives of spinach calmodulin that report calmodulin target protein binding. Biochemistry. 1988 Feb 9;27(3):991–996. doi: 10.1021/bi00403a023. [DOI] [PubMed] [Google Scholar]
  135. Mita S., Tominaga A., Hitoshi Y., Sakamoto K., Honjo T., Akagi M., Kikuchi Y., Yamaguchi N., Takatsu K. Characterization of high-affinity receptors for interleukin 5 on interleukin 5-dependent cell lines. Proc Natl Acad Sci U S A. 1989 Apr;86(7):2311–2315. doi: 10.1073/pnas.86.7.2311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  136. Mitchell D. A., Marshall T. K., Deschenes R. J. Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast. Yeast. 1993 Jul;9(7):715–722. doi: 10.1002/yea.320090705. [DOI] [PubMed] [Google Scholar]
  137. Mitsuzawa H., Uno I., Oshima T., Ishikawa T. Isolation and characterization of temperature-sensitive mutations in the RAS2 and CYR1 genes of Saccharomyces cerevisiae. Genetics. 1989 Dec;123(4):739–748. doi: 10.1093/genetics/123.4.739. [DOI] [PMC free article] [PubMed] [Google Scholar]
  138. Moerman D. G., Benian G. M., Barstead R. J., Schriefer L. A., Waterston R. H. Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans. Genes Dev. 1988 Jan;2(1):93–105. doi: 10.1101/gad.2.1.93. [DOI] [PubMed] [Google Scholar]
  139. Moerman D. G., Plurad S., Waterston R. H., Baillie D. L. Mutations in the unc-54 myosin heavy chain gene of Caenorhabditis elegans that alter contractility but not muscle structure. Cell. 1982 Jul;29(3):773–781. doi: 10.1016/0092-8674(82)90439-1. [DOI] [PubMed] [Google Scholar]
  140. Moir D., Stewart S. E., Osmond B. C., Botstein D. Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies. Genetics. 1982 Apr;100(4):547–563. doi: 10.1093/genetics/100.4.547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  141. Musacchio A., Noble M., Pauptit R., Wierenga R., Saraste M. Crystal structure of a Src-homology 3 (SH3) domain. Nature. 1992 Oct 29;359(6398):851–855. doi: 10.1038/359851a0. [DOI] [PubMed] [Google Scholar]
  142. Müsch A., Wiedmann M., Rapoport T. A. Yeast Sec proteins interact with polypeptides traversing the endoplasmic reticulum membrane. Cell. 1992 Apr 17;69(2):343–352. doi: 10.1016/0092-8674(92)90414-8. [DOI] [PubMed] [Google Scholar]
  143. Nakai H., Richardson C. C. The gene 1.2 protein of bacteriophage T7 interacts with the Escherichia coli dGTP triphosphohydrolase to form a GTP-binding protein. J Biol Chem. 1990 Mar 15;265(8):4411–4419. [PubMed] [Google Scholar]
  144. Nefsky B., Bretscher A. Yeast actin is relatively well behaved. Eur J Biochem. 1992 Jun 15;206(3):949–955. doi: 10.1111/j.1432-1033.1992.tb17005.x. [DOI] [PubMed] [Google Scholar]
  145. Nelson R. M., Long G. L. Solution-phase equilibrium binding interaction of human protein S with C4b-binding protein. Biochemistry. 1991 Mar 5;30(9):2384–2390. doi: 10.1021/bi00223a013. [DOI] [PubMed] [Google Scholar]
  146. Nogi Y., Shimada H., Matsuzaki Y., Hashimoto H., Fukasawa T. Regulation of expression of the galactose gene cluster in Saccharomyces cerevisiae. II. The isolation and dosage effect of the regulatory gene GAL80. Mol Gen Genet. 1984;195(1-2):29–34. doi: 10.1007/BF00332719. [DOI] [PubMed] [Google Scholar]
  147. Novick P., Osmond B. C., Botstein D. Suppressors of yeast actin mutations. Genetics. 1989 Apr;121(4):659–674. doi: 10.1093/genetics/121.4.659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. O'Shea E. K., Klemm J. D., Kim P. S., Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science. 1991 Oct 25;254(5031):539–544. doi: 10.1126/science.1948029. [DOI] [PubMed] [Google Scholar]
  149. O'Shea E. K., Rutkowski R., Kim P. S. Mechanism of specificity in the Fos-Jun oncoprotein heterodimer. Cell. 1992 Feb 21;68(4):699–708. doi: 10.1016/0092-8674(92)90145-3. [DOI] [PubMed] [Google Scholar]
  150. O'Shea E. K., Rutkowski R., Stafford W. F., 3rd, Kim P. S. Preferential heterodimer formation by isolated leucine zippers from fos and jun. Science. 1989 Aug 11;245(4918):646–648. doi: 10.1126/science.2503872. [DOI] [PubMed] [Google Scholar]
  151. Otto-Bruc A., Antonny B., Vuong T. M., Chardin P., Chabre M. Interaction between the retinal cyclic GMP phosphodiesterase inhibitor and transducin. Kinetics and affinity studies. Biochemistry. 1993 Aug 24;32(33):8636–8645. doi: 10.1021/bi00084a035. [DOI] [PubMed] [Google Scholar]
  152. Overduin M., Rios C. B., Mayer B. J., Baltimore D., Cowburn D. Three-dimensional solution structure of the src homology 2 domain of c-abl. Cell. 1992 Aug 21;70(4):697–704. doi: 10.1016/0092-8674(92)90437-h. [DOI] [PubMed] [Google Scholar]
  153. Panayotou G., Gish G., End P., Truong O., Gout I., Dhand R., Fry M. J., Hiles I., Pawson T., Waterfield M. D. Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach. Mol Cell Biol. 1993 Jun;13(6):3567–3576. doi: 10.1128/mcb.13.6.3567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. Pannekoek H., van Meijer M., Schleef R. R., Loskutoff D. J., Barbas C. F., 3rd Functional display of human plasminogen-activator inhibitor 1 (PAI-1) on phages: novel perspectives for structure-function analysis by error-prone DNA synthesis. Gene. 1993 Jun 15;128(1):135–140. doi: 10.1016/0378-1119(93)90164-x. [DOI] [PubMed] [Google Scholar]
  155. Pawson T., Gish G. D. SH2 and SH3 domains: from structure to function. Cell. 1992 Oct 30;71(3):359–362. doi: 10.1016/0092-8674(92)90504-6. [DOI] [PubMed] [Google Scholar]
  156. Phizicky E. M., Schwartz R. C., Abelson J. Saccharomyces cerevisiae tRNA ligase. Purification of the protein and isolation of the structural gene. J Biol Chem. 1986 Feb 25;261(6):2978–2986. [PubMed] [Google Scholar]
  157. Pinkney M., Hoggett J. G. Binding of the cyclic AMP receptor protein of Escherichia coli to RNA polymerase. Biochem J. 1988 Mar 15;250(3):897–902. doi: 10.1042/bj2500897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  158. Porpáczy Z., Sümegi B., Alkonyi I. Association between the alpha-ketoglutarate dehydrogenase complex and succinate thiokinase. Biochim Biophys Acta. 1983 Dec 12;749(2):172–179. doi: 10.1016/0167-4838(83)90249-2. [DOI] [PubMed] [Google Scholar]
  159. Prasad K. V., Janssen O., Kapeller R., Raab M., Cantley L. C., Rudd C. E. Src-homology 3 domain of protein kinase p59fyn mediates binding to phosphatidylinositol 3-kinase in T cells. Proc Natl Acad Sci U S A. 1993 Aug 1;90(15):7366–7370. doi: 10.1073/pnas.90.15.7366. [DOI] [PMC free article] [PubMed] [Google Scholar]
  160. Prasad K. V., Kapeller R., Janssen O., Repke H., Duke-Cohan J. S., Cantley L. C., Rudd C. E. Phosphatidylinositol (PI) 3-kinase and PI 4-kinase binding to the CD4-p56lck complex: the p56lck SH3 domain binds to PI 3-kinase but not PI 4-kinase. Mol Cell Biol. 1993 Dec;13(12):7708–7717. doi: 10.1128/mcb.13.12.7708. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. Prelich G., Tan C. K., Kostura M., Mathews M. B., So A. G., Downey K. M., Stillman B. Functional identity of proliferating cell nuclear antigen and a DNA polymerase-delta auxiliary protein. Nature. 1987 Apr 2;326(6112):517–520. doi: 10.1038/326517a0. [DOI] [PubMed] [Google Scholar]
  162. Rabindran S. K., Haroun R. I., Clos J., Wisniewski J., Wu C. Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science. 1993 Jan 8;259(5092):230–234. doi: 10.1126/science.8421783. [DOI] [PubMed] [Google Scholar]
  163. Ratner D. The interaction bacterial and phage proteins with immobilized Escherichia coli RNA polymerase. J Mol Biol. 1974 Sep 15;88(2):373–383. doi: 10.1016/0022-2836(74)90488-4. [DOI] [PubMed] [Google Scholar]
  164. Rauhut R., Green P. R., Abelson J. Yeast tRNA-splicing endonuclease is a heterotrimeric enzyme. J Biol Chem. 1990 Oct 25;265(30):18180–18184. [PubMed] [Google Scholar]
  165. Ray S. K., Arroyo M., Bagchi S., Raychaudhuri P. Identification of a 60-kilodalton Rb-binding protein, RBP60, that allows the Rb-E2F complex to bind DNA. Mol Cell Biol. 1992 Oct;12(10):4327–4333. doi: 10.1128/mcb.12.10.4327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  166. Redl B., Walleczek J., Stöffler-Meilicke M., Stöffler G. Immunoblotting analysis of protein-protein crosslinks within the 50S ribosomal subunit of Escherichia coli. A study using dimethylsuberimidate as crosslinking reagent. Eur J Biochem. 1989 May 1;181(2):351–356. doi: 10.1111/j.1432-1033.1989.tb14731.x. [DOI] [PubMed] [Google Scholar]
  167. Ren R., Mayer B. J., Cicchetti P., Baltimore D. Identification of a ten-amino acid proline-rich SH3 binding site. Science. 1993 Feb 19;259(5098):1157–1161. doi: 10.1126/science.8438166. [DOI] [PubMed] [Google Scholar]
  168. Rine J. Gene overexpression in studies of Saccharomyces cerevisiae. Methods Enzymol. 1991;194:239–251. doi: 10.1016/0076-6879(91)94019-9. [DOI] [PubMed] [Google Scholar]
  169. Rivas G., Ingham K. C., Minton A. P. Ca(2+)-linked association of human complement C1s and C1r. Biochemistry. 1994 Mar 1;33(8):2341–2348. doi: 10.1021/bi00174a048. [DOI] [PubMed] [Google Scholar]
  170. Rivas G., Ingham K. C., Minton A. P. Calcium-linked self-association of human complement C1s. Biochemistry. 1992 Dec 1;31(47):11707–11712. doi: 10.1021/bi00162a006. [DOI] [PubMed] [Google Scholar]
  171. Rivas G., Minton A. P. New developments in the study of biomolecular associations via sedimentation equilibrium. Trends Biochem Sci. 1993 Aug;18(8):284–287. doi: 10.1016/0968-0004(93)90035-l. [DOI] [PubMed] [Google Scholar]
  172. Roberts B. L., Markland W., Ley A. C., Kent R. B., White D. W., Guterman S. K., Ladner R. C. Directed evolution of a protein: selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2429–2433. doi: 10.1073/pnas.89.6.2429. [DOI] [PMC free article] [PubMed] [Google Scholar]
  173. Rozakis-Adcock M., Fernley R., Wade J., Pawson T., Bowtell D. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature. 1993 May 6;363(6424):83–85. doi: 10.1038/363083a0. [DOI] [PubMed] [Google Scholar]
  174. Russell R. B., Breed J., Barton G. J. Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains. FEBS Lett. 1992 Jun 8;304(1):15–20. doi: 10.1016/0014-5793(92)80579-6. [DOI] [PubMed] [Google Scholar]
  175. Sadowski I., Stone J. C., Pawson T. A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. Mol Cell Biol. 1986 Dec;6(12):4396–4408. doi: 10.1128/mcb.6.12.4396. [DOI] [PMC free article] [PubMed] [Google Scholar]
  176. Salminen A., Novick P. J. A ras-like protein is required for a post-Golgi event in yeast secretion. Cell. 1987 May 22;49(4):527–538. doi: 10.1016/0092-8674(87)90455-7. [DOI] [PubMed] [Google Scholar]
  177. Sanders S. L., Whitfield K. M., Vogel J. P., Rose M. D., Schekman R. W. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell. 1992 Apr 17;69(2):353–365. doi: 10.1016/0092-8674(92)90415-9. [DOI] [PubMed] [Google Scholar]
  178. Sarkar F. H., Gupta S. L. Receptors for human gamma interferon: binding and crosslinking of 125I-labeled recombinant human gamma interferon to receptors on WISH cells. Proc Natl Acad Sci U S A. 1984 Aug;81(16):5160–5164. doi: 10.1073/pnas.81.16.5160. [DOI] [PMC free article] [PubMed] [Google Scholar]
  179. Sawyers C. L., Callahan W., Witte O. N. Dominant negative MYC blocks transformation by ABL oncogenes. Cell. 1992 Sep 18;70(6):901–910. doi: 10.1016/0092-8674(92)90241-4. [DOI] [PubMed] [Google Scholar]
  180. Scherer P. E., Manning-Krieg U. C., Jenö P., Schatz G., Horst M. Identification of a 45-kDa protein at the protein import site of the yeast mitochondrial inner membrane. Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11930–11934. doi: 10.1073/pnas.89.24.11930. [DOI] [PMC free article] [PubMed] [Google Scholar]
  181. Schmidt-Dörr T., Oertel-Buchheit P., Pernelle C., Bracco L., Schnarr M., Granger-Schnarr M. Construction, purification, and characterization of a hybrid protein comprising the DNA binding domain of the LexA repressor and the Jun leucine zipper: a circular dichroism and mutagenesis study. Biochemistry. 1991 Oct 8;30(40):9657–9664. doi: 10.1021/bi00104a013. [DOI] [PubMed] [Google Scholar]
  182. Schuster S. C., Swanson R. V., Alex L. A., Bourret R. B., Simon M. I. Assembly and function of a quaternary signal transduction complex monitored by surface plasmon resonance. Nature. 1993 Sep 23;365(6444):343–347. doi: 10.1038/365343a0. [DOI] [PubMed] [Google Scholar]
  183. Scott J. K., Smith G. P. Searching for peptide ligands with an epitope library. Science. 1990 Jul 27;249(4967):386–390. doi: 10.1126/science.1696028. [DOI] [PubMed] [Google Scholar]
  184. Shapiro R., Vallee B. L. Interaction of human placental ribonuclease with placental ribonuclease inhibitor. Biochemistry. 1991 Feb 26;30(8):2246–2255. doi: 10.1021/bi00222a030. [DOI] [PubMed] [Google Scholar]
  185. Sikela J. M., Hahn W. E. Screening an expression library with a ligand probe: isolation and sequence of a cDNA corresponding to a brain calmodulin-binding protein. Proc Natl Acad Sci U S A. 1987 May;84(9):3038–3042. doi: 10.1073/pnas.84.9.3038. [DOI] [PMC free article] [PubMed] [Google Scholar]
  186. Skolnik E. Y., Margolis B., Mohammadi M., Lowenstein E., Fischer R., Drepps A., Ullrich A., Schlessinger J. Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases. Cell. 1991 Apr 5;65(1):83–90. doi: 10.1016/0092-8674(91)90410-z. [DOI] [PubMed] [Google Scholar]
  187. Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 1988 Jul 15;67(1):31–40. doi: 10.1016/0378-1119(88)90005-4. [DOI] [PubMed] [Google Scholar]
  188. Smith G. P. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science. 1985 Jun 14;228(4705):1315–1317. doi: 10.1126/science.4001944. [DOI] [PubMed] [Google Scholar]
  189. Songyang Z., Shoelson S. E., Chaudhuri M., Gish G., Pawson T., Haser W. G., King F., Roberts T., Ratnofsky S., Lechleider R. J. SH2 domains recognize specific phosphopeptide sequences. Cell. 1993 Mar 12;72(5):767–778. doi: 10.1016/0092-8674(93)90404-e. [DOI] [PubMed] [Google Scholar]
  190. Sopta M., Carthew R. W., Greenblatt J. Isolation of three proteins that bind to mammalian RNA polymerase II. J Biol Chem. 1985 Aug 25;260(18):10353–10360. [PubMed] [Google Scholar]
  191. Srere P. A. Complexes of sequential metabolic enzymes. Annu Rev Biochem. 1987;56:89–124. doi: 10.1146/annurev.bi.56.070187.000513. [DOI] [PubMed] [Google Scholar]
  192. Steitz T. A., Anderson W. F., Fletterick R. J., Anderson C. M. High resolution crystal structures of yeast hexokinase complexes with substrates, activators, and inhibitors. Evidence for an allosteric control site. J Biol Chem. 1977 Jul 10;252(13):4494–4500. [PubMed] [Google Scholar]
  193. Stephen C. W., Lane D. P. Mutant conformation of p53. Precise epitope mapping using a filamentous phage epitope library. J Mol Biol. 1992 Jun 5;225(3):577–583. doi: 10.1016/0022-2836(92)90386-x. [DOI] [PubMed] [Google Scholar]
  194. Stevens F. J. Analysis of protein-protein interaction by simulation of small-zone size-exclusion chromatography: application to an antibody-antigen association. Biochemistry. 1986 Mar 11;25(5):981–993. doi: 10.1021/bi00353a006. [DOI] [PubMed] [Google Scholar]
  195. Stöffler G., Redl B., Walleczek J., Stöffler-Meilicke M. Identification of protein-protein cross-links within the Escherichia coli ribosome by immunoblotting techniques. Methods Enzymol. 1988;164:64–76. doi: 10.1016/s0076-6879(88)64035-3. [DOI] [PubMed] [Google Scholar]
  196. Söllner T., Rassow J., Wiedmann M., Schlossmann J., Keil P., Neupert W., Pfanner N. Mapping of the protein import machinery in the mitochondrial outer membrane by crosslinking of translocation intermediates. Nature. 1992 Jan 2;355(6355):84–87. doi: 10.1038/355084a0. [DOI] [PubMed] [Google Scholar]
  197. Tompa P., Batke J., Ovadi J., Welch G. R., Srere P. A. Quantitation of the interaction between citrate synthase and malate dehydrogenase. J Biol Chem. 1987 May 5;262(13):6089–6092. [PubMed] [Google Scholar]
  198. Truant R., Xiao H., Ingles C. J., Greenblatt J. Direct interaction between the transcriptional activation domain of human p53 and the TATA box-binding protein. J Biol Chem. 1993 Feb 5;268(4):2284–2287. [PubMed] [Google Scholar]
  199. Uchiumi T., Wahba A. J., Traut R. R. Topography and stoichiometry of acidic proteins in large ribosomal subunits from Artemia salina as determined by crosslinking. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5580–5584. doi: 10.1073/pnas.84.16.5580. [DOI] [PMC free article] [PubMed] [Google Scholar]
  200. Vallee R. B., Collins C. A. Purification of microtubules and microtubule-associated proteins from sea urchin eggs and cultured mammalian cells using taxol, and use of exogenous taxol-stabilized brain microtubules for purifying microtubule-associated proteins. Methods Enzymol. 1986;134:116–127. doi: 10.1016/0076-6879(86)34080-1. [DOI] [PubMed] [Google Scholar]
  201. Van Aelst L., Barr M., Marcus S., Polverino A., Wigler M. Complex formation between RAS and RAF and other protein kinases. Proc Natl Acad Sci U S A. 1993 Jul 1;90(13):6213–6217. doi: 10.1073/pnas.90.13.6213. [DOI] [PMC free article] [PubMed] [Google Scholar]
  202. Vincent J. P., Lazdunski M. Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges. Biochemistry. 1972 Aug 1;11(16):2967–2977. doi: 10.1021/bi00766a007. [DOI] [PubMed] [Google Scholar]
  203. Vinson C. R., Hai T., Boyd S. M. Dimerization specificity of the leucine zipper-containing bZIP motif on DNA binding: prediction and rational design. Genes Dev. 1993 Jun;7(6):1047–1058. doi: 10.1101/gad.7.6.1047. [DOI] [PubMed] [Google Scholar]
  204. Vinson C. R., LaMarco K. L., Johnson P. F., Landschulz W. H., McKnight S. L. In situ detection of sequence-specific DNA binding activity specified by a recombinant bacteriophage. Genes Dev. 1988 Jul;2(7):801–806. doi: 10.1101/gad.2.7.801. [DOI] [PubMed] [Google Scholar]
  205. Vojtek A. B., Hollenberg S. M., Cooper J. A. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell. 1993 Jul 16;74(1):205–214. doi: 10.1016/0092-8674(93)90307-c. [DOI] [PubMed] [Google Scholar]
  206. Waksman G., Kominos D., Robertson S. C., Pant N., Baltimore D., Birge R. B., Cowburn D., Hanafusa H., Mayer B. J., Overduin M. Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature. 1992 Aug 20;358(6388):646–653. doi: 10.1038/358646a0. [DOI] [PubMed] [Google Scholar]
  207. Waksman G., Shoelson S. E., Pant N., Cowburn D., Kuriyan J. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell. 1993 Mar 12;72(5):779–790. doi: 10.1016/0092-8674(93)90405-f. [DOI] [PubMed] [Google Scholar]
  208. Waldron C., Lacroute F. Effect of growth rate on the amounts of ribosomal and transfer ribonucleic acids in yeast. J Bacteriol. 1975 Jun;122(3):855–865. doi: 10.1128/jb.122.3.855-865.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  209. Warne P. H., Viciana P. R., Downward J. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature. 1993 Jul 22;364(6435):352–355. doi: 10.1038/364352a0. [DOI] [PubMed] [Google Scholar]
  210. Weber J., Lee R. S., Wilke-Mounts S., Grell E., Senior A. E. Combined application of site-directed mutagenesis, 2-azido-ATP labeling, and lin-benzo-ATP binding to study the noncatalytic sites of Escherichia coli F1-ATPase. J Biol Chem. 1993 Mar 25;268(9):6241–6247. [PubMed] [Google Scholar]
  211. Weiel J., Hershey J. W. Fluorescence polarization studies of the interaction of Escherichia coli protein synthesis initiation factor 3 with 30S ribosomal subunits. Biochemistry. 1981 Sep 29;20(20):5859–5865. doi: 10.1021/bi00523a032. [DOI] [PubMed] [Google Scholar]
  212. Weiel J., Hershey J. W. The binding of fluorescein-labeled protein synthesis initiation factor 2 to Escherichia coli 30 S ribosomal subunits determined by fluorescence polarization. J Biol Chem. 1982 Feb 10;257(3):1215–1220. [PubMed] [Google Scholar]
  213. Wells J. A., Lowman H. B. Rapid evolution of peptide and protein binding properties in vitro. Curr Opin Biotechnol. 1992 Aug;3(4):355–362. doi: 10.1016/0958-1669(92)90163-d. [DOI] [PubMed] [Google Scholar]
  214. Weng Z., Taylor J. A., Turner C. E., Brugge J. S., Seidel-Dugan C. Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells. J Biol Chem. 1993 Jul 15;268(20):14956–14963. [PubMed] [Google Scholar]
  215. Wensel T. G., Stryer L. Activation mechanism of retinal rod cyclic GMP phosphodiesterase probed by fluorescein-labeled inhibitory subunit. Biochemistry. 1990 Feb 27;29(8):2155–2161. doi: 10.1021/bi00460a028. [DOI] [PubMed] [Google Scholar]
  216. Wensel T. G., Stryer L. Reciprocal control of retinal rod cyclic GMP phosphodiesterase by its gamma subunit and transducin. Proteins. 1986 Sep;1(1):90–99. doi: 10.1002/prot.340010114. [DOI] [PubMed] [Google Scholar]
  217. White R. J., Jackson S. P. The TATA-binding protein: a central role in transcription by RNA polymerases I, II and III. Trends Genet. 1992 Aug;8(8):284–288. doi: 10.1016/0168-9525(92)90255-3. [DOI] [PubMed] [Google Scholar]
  218. Whyte P., Buchkovich K. J., Horowitz J. M., Friend S. H., Raybuck M., Weinberg R. A., Harlow E. Association between an oncogene and an anti-oncogene: the adenovirus E1A proteins bind to the retinoblastoma gene product. Nature. 1988 Jul 14;334(6178):124–129. doi: 10.1038/334124a0. [DOI] [PubMed] [Google Scholar]
  219. Whyte P., Williamson N. M., Harlow E. Cellular targets for transformation by the adenovirus E1A proteins. Cell. 1989 Jan 13;56(1):67–75. doi: 10.1016/0092-8674(89)90984-7. [DOI] [PubMed] [Google Scholar]
  220. Wiedmann M., Goerlich D., Hartmann E., Kurzchalia T. V., Rapoport T. A. Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum. FEBS Lett. 1989 Nov 6;257(2):263–268. doi: 10.1016/0014-5793(89)81549-2. [DOI] [PubMed] [Google Scholar]
  221. Wiedmann M., Kurzchalia T. V., Hartmann E., Rapoport T. A. A signal sequence receptor in the endoplasmic reticulum membrane. 1987 Aug 27-Sep 2Nature. 328(6133):830–833. doi: 10.1038/328830a0. [DOI] [PubMed] [Google Scholar]
  222. Wiman K. G. The retinoblastoma gene: role in cell cycle control and cell differentiation. FASEB J. 1993 Jul;7(10):841–845. doi: 10.1096/fasebj.7.10.8393817. [DOI] [PubMed] [Google Scholar]
  223. YANOFSKY C., RACHMELER M. The exclusion of free indole as an intermediate in the biosynthesis of tryptophan in Neurospora crassa. Biochim Biophys Acta. 1958 Jun;28(3):640–641. doi: 10.1016/0006-3002(58)90533-x. [DOI] [PubMed] [Google Scholar]
  224. Yee S. P., Branton P. E. Detection of cellular proteins associated with human adenovirus type 5 early region 1A polypeptides. Virology. 1985 Nov;147(1):142–153. doi: 10.1016/0042-6822(85)90234-x. [DOI] [PubMed] [Google Scholar]
  225. Yong H., Thomas G. A., Peticolas W. L. Metabolite-modulated complex formation between alpha-glycerophosphate dehydrogenase and lactate dehydrogenase. Biochemistry. 1993 Oct 19;32(41):11124–11131. doi: 10.1021/bi00092a023. [DOI] [PubMed] [Google Scholar]
  226. Young R. A., Davis R. W. Yeast RNA polymerase II genes: isolation with antibody probes. Science. 1983 Nov 18;222(4625):778–782. doi: 10.1126/science.6356359. [DOI] [PubMed] [Google Scholar]
  227. Yu H., Rosen M. K., Shin T. B., Seidel-Dugan C., Brugge J. S., Schreiber S. L. Solution structure of the SH3 domain of Src and identification of its ligand-binding site. Science. 1992 Dec 4;258(5088):1665–1668. doi: 10.1126/science.1280858. [DOI] [PubMed] [Google Scholar]
  228. Zebedee S. L., Barbas C. F., 3rd, Hom Y. L., Caothien R. H., Graff R., DeGraw J., Pyati J., LaPolla R., Burton D. R., Lerner R. A. Human combinatorial antibody libraries to hepatitis B surface antigen. Proc Natl Acad Sci U S A. 1992 Apr 15;89(8):3175–3179. doi: 10.1073/pnas.89.8.3175. [DOI] [PMC free article] [PubMed] [Google Scholar]
  229. Zervos A. S., Gyuris J., Brent R. Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites. Cell. 1993 Jan 29;72(2):223–232. doi: 10.1016/0092-8674(93)90662-a. [DOI] [PubMed] [Google Scholar]
  230. Zhang X. F., Settleman J., Kyriakis J. M., Takeuchi-Suzuki E., Elledge S. J., Marshall M. S., Bruder J. T., Rapp U. R., Avruch J. Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1. Nature. 1993 Jul 22;364(6435):308–313. doi: 10.1038/364308a0. [DOI] [PubMed] [Google Scholar]
  231. Zhou M., Felder S., Rubinstein M., Hurwitz D. R., Ullrich A., Lax I., Schlessinger J. Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activation. Biochemistry. 1993 Aug 17;32(32):8193–8198. doi: 10.1021/bi00083a020. [DOI] [PubMed] [Google Scholar]
  232. Zimmerman J. K., Ackers G. K. Molecular sieve studies of interacting protein systems. X. Behavior of small zone profiles for reversibly self-associating solutes. J Biol Chem. 1971 Dec 10;246(23):7289–7292. [PubMed] [Google Scholar]
  233. de Gunzburg J., Riehl R., Weinberg R. A. Identification of a protein associated with p21ras by chemical crosslinking. Proc Natl Acad Sci U S A. 1989 Jun;86(11):4007–4011. doi: 10.1073/pnas.86.11.4007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  234. el-Deiry W. S., Tokino T., Velculescu V. E., Levy D. B., Parsons R., Trent J. M., Lin D., Mercer W. E., Kinzler K. W., Vogelstein B. WAF1, a potential mediator of p53 tumor suppression. Cell. 1993 Nov 19;75(4):817–825. doi: 10.1016/0092-8674(93)90500-p. [DOI] [PubMed] [Google Scholar]

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