The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Open accessOverview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Citations
Cites
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 16,688
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS *
Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 16,129
Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
Shapiro, A. L., Viñuela, E., & Maizel, J. V. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(67)90391-9 · Cited by 3,775
Fundamental techniques in virology.
Habel, K., & Salzman, N. P. (1969) · Medical Entomology and Zoology · Cited by 1,762
Physiological Studies of Conditional Lethal Mutants of Bacteriophage T4DPreprint
Epstein, R. H., Bolle, A., Steinberg, C. M., Kellenberger, E., de la Tour, E. B., Chevalley, R., Edgar, R. S., Susman, M., Denhardt, G. H., & Lielausis, A. (1963) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1963.028.01.053 · Cited by 803
Analysis of C14-labeled proteins by disc electrophoresis
Fairbanks, G., Levinthal, C., & Reeder, R. H. (1965) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(65)90589-9 · Cited by 467
A factor preventing the major head protein of bacteriophage T4 from random aggregation
Laemmli, U. K., Béguin, F., & Gujer-Kellenberger, G. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90402-x · Cited by 387
Self-citationStructure of crystalline α-chymotrypsin
Steitz, T. A., Hendekson, R., & Blow, D. M. (1969) · Journal of Molecular Biology · doi:10.1016/0022-2836(69)90426-4 · Cited by 378
Co-Linearity of the Gene with the Polypeptide Chain
Sarabhai, A., Stretton, A. O. W., Brenner, S., & Bolle, A. (1964) · Nature · doi:10.1038/201013a0 · Cited by 362
Form-determining function of the genes required for the assembly of the head of bacteriophage T4
Laemmll, U. K., Mölbert, E., Showe, M. K., & Kellenberger, E. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90379-7 · Cited by 264
Flagged first, then by citations
Research works printed but not linked: 3
- Maizel, J. V., Fundamental Techniques of Virology (edit. by Habel, K., and Salzman, N. P.), chap. 32, 334 (Academic Press, New York, 1969).
- King, J., FEBS Symp. (edit. by Ochoa, S., Nachmansohn, D., Asensio, C., and Heredia, C. F.), 21, 156 (Academic Press, London, 1970).
- Sternberg, N., and Champe, S. P., J. Mol. Biol., 46, 337 (1970).
Cited by
Sorted by citations
Items 501–600 of 2,058
Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum
Letourneur, F., Gaynor, E. C., Hennecke, S., Démollière, C., Duden, R., Emr, S. D., Riezman, H., & Cosson, P. (1994) · Cell · doi:10.1016/0092-8674(94)90011-6 · Cited by 796
Amann, E. P., Brosius, J., & Ptashne, M. (1983) · Gene · doi:10.1016/0378-1119(83)90222-6 · Cited by 788
Isolation of Monoclonal Antibodies Specific for Human c-myc Proto-Oncogene Product
Evan, G. I., Lewis, G. K., Ramsay, G. M., & Bishop, J. M. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.12.3610-3616.1985 · Cited by 795
DNA Repair Helicase: a Component of BTF2 (TFIIH) Basic Transcription Factor
Schaeffer, L., Roy, R., Humbert, S., Moncollin, V., Vermeulen, W., Hoeijmakers, J. H. J., Chambon, P., & Egly, J. (1993) · Science · doi:10.1126/science.8465201 · Cited by 794
A very small porcine virus with circular single-stranded DNA
Tischer, I., Gelderblom, H., Vettermann, W., & Koch, M. A. (1982) · Nature · doi:10.1038/295064a0 · Cited by 788
Cell adhesion events mediated by α4 integrins are essential in placental and cardiac development
Yang, J. T., Rayburn, H., & Hynes, R. O. (1995) · Development · doi:10.1242/dev.121.2.549 · Cited by 785
Flier, J. S., Mueckler, M., Usher, P., & Lodish, H. F. (1987) · Science · doi:10.1126/science.3103217 · Cited by 783
Subbaramaiah, K., Chung, W. J., Michaluart, P., TELANG, N. T., Tanabe, T., Inoue, H., Jang, M., Pezzuto, J. M., & Dannenberg, A. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.21875 · Cited by 786
Zsebo, K. M., Wypych, J., McNiece, I., Lu, H. S., Smith, K. A., Karkare, S. B., Sachdev, R. K., Yuschenkoff, V. N., Birkett, N. C., Williams, L. R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90300-4 · Cited by 786
Thorens, B., Sarkar, H. K., Kaback, H. R., & Lodish, H. F. (1988) · Cell · doi:10.1016/0092-8674(88)90051-7 · Cited by 785
Sugino, A., Peebles, C. L., Kreuzer, K. N., & Cozzarelli, N. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.11.4767 · Cited by 784
Interactions among three distinct CesA proteins essential for cellulose synthesis
Taylor, N. G., Howells, R. M., Huttly, A. K., Vickers, K., & Turner, S. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0337628100 · Cited by 784
Wayner, E. A., Garcı́a-Pardo, A., Humphries, M. J., McDonald, J. A., & Carter, W. G. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.3.1321 · Cited by 784
Greenberg, A. S., Avila, D. W., Hughes, M. K., Hughes, A. L., McKinney, E. C., & Flajnik, M. F. (1995) · Nature · doi:10.1038/374168a0 · Cited by 783
DNA binding activities of three murine Jun proteins: Stimulation by Fos
Nakabeppu, Y., Ryder, K., & Nathans, D. (1988) · Cell · doi:10.1016/0092-8674(88)90146-8 · Cited by 781
A novel secretory pathway for interleukin‐1 beta, a protein lacking a signal sequence.
Rubartelli, A., Cozzolino, F., Talio, M., & Sitia, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08268.x · Cited by 780
The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
Walker, J. E. (1992) · Quarterly Reviews of Biophysics · doi:10.1017/s003358350000425x · Cited by 777
Lee, G. J., Roseman, A. M., Saibil, H. R., & Vierling, E. (1997) · The EMBO Journal · doi:10.1093/emboj/16.3.659 · Cited by 780
Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779
Debray, H., DECOUT, D., Strecker, G., Spik, G., & Montreuil, J. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb06300.x · Cited by 779
Yin, H. L., & Stossel, T. P. (1979) · Nature · doi:10.1038/281583a0 · Cited by 779
Tsukita, S., Oishi, K., Sato, N., Sagara, J., Kawai, A., & Tsukita, S. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.2.391 · Cited by 779
Huber, R., Langworthy, T. A., K�nig, H., Thomm, M., Woese, C. R., Sleytr, U. B., & STETTER, K. O. (1986) · Archives of Microbiology · doi:10.1007/bf00409880 · Cited by 778
Jenkins, C. M., Mancuso, D. J., Yan, W., Sims, H. F., Gibson, B., & Gross, R. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407841200 · Cited by 778
Klee, C. B., & VANAMAN, T. C. (1982) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60470-2 · Cited by 778
A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli.Preprint
Almirón, M. A., Link, A. J., Furlong, D., & Kolter, R. (1992) · Genes & Development · doi:10.1101/gad.6.12b.2646 · Cited by 768
Rahmoune, H., Thompson, P. W., Ward, J. M., Smith, C. D., Hong, G., & Brown, J. (2005) · Diabetes · doi:10.2337/diabetes.54.12.3427 · Cited by 787
de Boer, P. A. J., Crossley, R. E., & Rothfield, L. I. (1989) · Cell · doi:10.1016/0092-8674(89)90586-2 · Cited by 776
A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles.
Cohen, S., Ushiro, H., Stoscheck, C. M., & Chinkers, M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68224-4 · Cited by 776
Hébert, T. E., Moffett, S., Morello, J.-P., Loisel, T. P., Bichet, D. G., Barret, C., & Bouvier, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.27.16384 · Cited by 775
Draetta, G. F., & Beach, D. (1988) · Cell · doi:10.1016/0092-8674(88)90175-4 · Cited by 775
Elder, J. H., Pickett, R. A., Hampton, J., & Lerner, R. A. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39987-8 · Cited by 774
Diamond, M., Staunton, D. E., Marlin, S. D., & Springer, T. A. (1991) · Cell · doi:10.1016/0092-8674(91)90548-d · Cited by 778
A conditional tissue-specific transgene expression system using inducible GAL4
Osterwalder, T., Yoon, K. S., White, B. H., & Keshishian, H. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221303298 · Cited by 804
Labeling of proteins by reductive methylation using sodium cyanoborohydride.
Jentoft, N., & Dearborn, D. G. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30016-9 · Cited by 771
Hershko, A., Ciechanover, A. J., Heller, H., Haas, A. L., & Rose, I. A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.4.1783 · Cited by 769
Wu, T., Malinverni, J. C., Ruiz, N., Kim, S., Silhavy, T. J., & Kahne, D. E. (2005) · Cell · doi:10.1016/j.cell.2005.02.015 · Cited by 769
A Temperature-Dependent Switch from Chaperone to Protease in a Widely Conserved Heat Shock Protein
Spiess, C., Beil, A., & Ehrmann, M. (1999) · Cell · doi:10.1016/s0092-8674(00)80743-6 · Cited by 768
Dynamin-mediated Internalization of Caveolae
Henley, J. R., Krueger, E. W. A., Oswald, B. J., & McNiven, M. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.1.85 · Cited by 767
Nephrin is specifically located at the slit diaphragm of glomerular podocytes
Ruotsalainen, V., Ljungberg, P., Wartiovaara, J., Lenkkeri, U., Kestilä, M., Jalanko, H., Holmberg, C., & Tryggvason, K. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.14.7962 · Cited by 766
Yang, Y., Ciarletta, A. B., Temple, P. A., Chung, M. P., Kovacic, S., Witek-Giannotti, J. S., Leary, A. C., Kriz, R., Donahue, R. E., Wong, G. G., et al. (1986) · Cell · doi:10.1016/0092-8674(86)90360-0 · Cited by 766
Shanklin, J., Whittle, E. J., & Fox, B. G. (1994) · Biochemistry · doi:10.1021/bi00209a009 · Cited by 764
A one-step purification of membrane proteins using a high efficiency immunomatrix.
Schneider, C., Newman, R., Sutherland, D. R., Asser, U., & Greaves, M. F. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33889-4 · Cited by 764
Ahmad, A., Senapati, S., Khan, M. I., Kumar, R., & Sastry, M. (2003) · Langmuir · doi:10.1021/la026772l · Cited by 762
Connolly, E. L., Fett, J. P., & Guerinot, M. L. (2002) · The Plant Cell · doi:10.1105/tpc.001263 · Cited by 760
Dynamic O-Glycosylation of Nuclear and Cytosolic Proteins
Gao, Y., Wells, L., Comer, F. I., Parker, G. J., & Hart, G. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010420200 · Cited by 757
Immunolocalization of keratin polypeptides in human epidermis using monoclonal antibodies
Woodcock‐Mitchell, J. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.2.580 · Cited by 761
Hell, J. W., Westenbroek, R. E., Warner, C., Ahlijanian, M. K., Prystay, W., Gilbert, M., Snutch, T. P., & Catterall, W. A. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.123.4.949 · Cited by 760
Maines, M. D., Trakshel, G. M., & Kutty, R. K. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42488-4 · Cited by 759
Lugtenberg, B. J. J., & van Alphen, L. (1983) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(83)90014-x · Cited by 742
Piperno, G., & Fuller, M. T. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.6.2085 · Cited by 758
Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes
Carter, W. G., Ryan, M. C., & Gahr, P. J. (1991) · Cell · doi:10.1016/0092-8674(91)90092-d · Cited by 758
Mutations in GPC3, a glypican gene, cause the Simpson-Golabi-Behmel overgrowth syndrome
Pilia, G., Hughes-Benzie, R., MacKenzie, A., Baybayan, P. A., Chen, E. Y., Huber, R., Neri, G., Cao, A., Forabosco, A., & Schlessinger, D. (1996) · Nature Genetics · doi:10.1038/ng0396-241 · Cited by 750
Frazier, K. S., Williams, S. J., Kothapalli, D., Klapper, H., & Grotendorst, G. R. (1996) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12363389 · Cited by 750
Pear, J. R., Kawagoe, Y., Schreckengost, W. E., Delmer, D. P., & Stalker, D. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12637 · Cited by 748
Processing of Adenovirus 2-Induced Proteins
Anderson, C. W., Baum, P. R., & Gesteland, R. F. (1973) · Journal of Virology · doi:10.1128/jvi.12.2.241-252.1973 · Cited by 755
Snake venom variability: methods of study, results and interpretation
Chippaux, J., Williams, V. K., & White, J. (1991) · Toxicon · doi:10.1016/0041-0101(91)90116-9 · Cited by 754
Sondell, M., Lundborg, G., & Kanje, M. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-14-05731.1999 · Cited by 750
“The samples were electrophoresed according to Laemmli (1970).”
Method[2] Preparation and characterization of the different types of collagen
Miller, E. J., & Rhodes, R. K. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(82)82059-4 · Cited by 753
Peptide Binding and Release by Proteins Implicated as Catalysts of Protein Assembly
Flynn, G. C., Chappell, T. G., & Rothman, J. E. (1989) · Science · doi:10.1126/science.2756425 · Cited by 753
Resolution of Bacterial Proteins by Polyacrylamide Gel Electrophoresis on Slabs
Ames, G. F. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43074-3 · Cited by 753
Dynamic Glycosylation of Nuclear and Cytosolic Proteins
Kreppel, L. K., Blomberg, M. A., & Hart, G. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.14.9308 · Cited by 747
Willey, R. L., Smith, D. H., Lasky, L. A., Theodore, T. S., Earl, P. L., Moss, B., Capon, D. J., & Martin, M. A. (1988) · Journal of Virology · doi:10.1128/jvi.62.1.139-147.1988 · Cited by 751
Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning.
Soubrier, F., Alhenc‐Gelas, F., Hübert, C., Allegrini, J., John, M., Tregear, G. W., & Corvol, P. L. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.24.9386 · Cited by 750
Gheysen, D., Jacobs, E. J., de Foresta, F., Thiriart, C., Francotte, M., Thines, D., & Wilde, M. D. (1989) · Cell · doi:10.1016/0092-8674(89)90873-8 · Cited by 743
Manner of Interaction of Heterogeneous Claudin Species within and between Tight Junction Strands
Furuse, M., Sasaki, H., & Tsukita, S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.4.891 · Cited by 746
Coller, B. S., Peerschke, E. I. B., Scudder, L. E., & Sullivan, C. A. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110973 · Cited by 746
Giancotti, F. G., & Ruoslahtl, E. (1990) · Cell · doi:10.1016/0092-8674(90)90098-y · Cited by 739
Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis
Farrell, P. J., Balkow, K., Hunt, T., Jackson, R. J., & Trachsel, H. (1977) · Cell · doi:10.1016/0092-8674(77)90330-0 · Cited by 745
Direct stimulation of Jak/STAT pathway by the angiotensin II AT1 receptor
Marrero, M. B., Schieffer, B., Paxton, W. G., Heerdt, L., Berk, B. C., Delafontaine, P., & Bernstein, K. E. (1995) · Nature · doi:10.1038/375247a0 · Cited by 744
Killing of gram-negative bacteria by lactoferrin and lysozyme.
Ellison, R. T., & Giehl, T. J. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115407 · Cited by 744
de Waegh, S. M., Lee, V. M. ‐., & Brady, S. T. (1992) · Cell · doi:10.1016/0092-8674(92)90183-d · Cited by 743
Rathjen, F. G., & Schachner, M. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb01753.x · Cited by 741
Hodivala‐Dilke, K., McHugh, K. P., Tsakiris, D. Α., Rayburn, H., Crowley, D. G., Ullman-Culleré, M., Ross, F. P., Coller, B. S., Teitelbaum, S. L., & Hynes, R. O. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5487 · Cited by 741
Human hepatitis B vaccine from recombinant yeast
McAleer, W. J., Buynak, E. B., Maigetter, R. Z., Wampler, D. E., Miller, W. J. W., & Hilleman, M. R. (1984) · Nature · doi:10.1038/307178a0 · Cited by 740
Matrix Metalloproteinase Expression Increases After Cerebral Focal Ischemia in Rats
Romanic, A. M., White, R. F., Arleth, A. J., Ohlstein, E. H., & Barone, F. C. (1998) · Stroke · doi:10.1161/01.str.29.5.1020 · Cited by 740
Stanley, E. R., & Heard, P. M. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40265-1 · Cited by 738
Calcineurin: a calcium- and calmodulin-binding protein of the nervous system.
Klee, C. B., Crouch, T. H., & Krinks, M. H. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.12.6270 · Cited by 579
Flow of information in the light-triggered cyclic nucleotide cascade of vision.
Fung, B. K.-K., Hurley, J. B., & Stryer, L. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.1.152 · Cited by 738
Theta, a new class of glutathione transferases purified from rat and man
Meyer, D. J., Coles, B., Pemble, S. E., Gilmore, K. S., FRASER, G. M., & KETTERER, B. (1991) · Biochemical Journal · doi:10.1042/bj2740409 · Cited by 737
Expression cloning of the murine erythropoietin receptor
D’Andrea, A. D., Lodish, H. F., & Wong, G. G. (1989) · Cell · doi:10.1016/0092-8674(89)90965-3 · Cited by 737
Mechanism of activation of latent recombinant transforming growth factor beta 1 by plasmin.
Lyons, R. M., Gentry, L. E., Purchio, A. F., & Moses, H. L. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.4.1361 · Cited by 737
Wound Fluid from Chronic Leg Ulcers Contains Elevated Levels of Metalloproteinases MMP-2 and MMP-9
Wysocki, A. B., Staiano-Coico, L., & Grinnell, F. (1993) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12359590 · Cited by 732
Vesa, J., Hellsten, E., Verkruyse, L. A., Camp, L. A., Rapola, J., Santavuori, P., Hofmann, S. L., & Peltonen, L. (1995) · Nature · doi:10.1038/376584a0 · Cited by 736
Skehel, J. J., Bayley, P. M., Brown, E. B., Martin, S. R., Waterfield, M. D., White, J. M., Wilson, I. A., & Wiley, D. C. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.4.968 · Cited by 726
Li, G. C., & Werb, Z. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.10.3218 · Cited by 735
Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
Mayeda, A., & Krainer, A. R. (1992) · Cell · doi:10.1016/0092-8674(92)90477-t · Cited by 735
Proteomic Identification of S -Nitrosylated Proteins in Arabidopsis
Lindermayr, C., Saalbach, G., & Durner, J. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.104.058719 · Cited by 737
Zheng, L., Nukuna, B. N., Brennan, M., Sun, M., Goormastic, M., Settle, M., Schmitt, D., Fu, X., Thomson, L., Fox, P. L., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21109 · Cited by 735
Shevkani, K., Singh, N., Kaur, A., & Rana, J. C. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.07.024 · Cited by 764
Parathyroid hormone-related protein purified from a human lung cancer cell line.
Moseley, J. M., Kubota, M., Diefenbach-Jagger, H., Wettenhall, R. E. H., Kemp, B. E., Suva, L. J., Rodda, C. P., Ebeling, P. R., Hudson, P. J., & Zajac, J. D. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.14.5048 · Cited by 734
Monoclonal Antibodies for Analysis of the HLA System
Brodsky, F. M., Parham, P., Barnstable, C. J., Crumpton, M. J., & Bodmer, W. F. (1979) · Immunological Reviews · doi:10.1111/j.1600-065x.1979.tb00288.x · Cited by 734
Baar, K., & Esser, K. (1999) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1999.276.1.c120 · Cited by 726
Leptospiral lipopolysaccharide activates cells through a TLR2-dependent mechanism
Werts, C., Tapping, R. I., Mathison, J. C., Chuang, T., Kravchenko, V. V., Girons, I. S., Haake, D. A., Godowski, P. J., Hayashi, F., Ozinsky, A., et al. (2001) · Nature Immunology · doi:10.1038/86354 · Cited by 732
Haskill, S., Beg, A. A., Tompkins, S. M., Morris, J. S., Yurochko, A. D., Sampson-Johannes, A., Mondal, K., Ralph, P., & Baldwin, A. S. (1991) · Cell · doi:10.1016/0092-8674(91)90022-q · Cited by 732
Greenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 735
Association of dystrophin and an integral membrane glycoprotein
Campbell, K. P., & Kahl, S. D. (1989) · Nature · doi:10.1038/338259a0 · Cited by 732
Vandekerckhove, J. S., & Weber, K. K. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90020-7 · Cited by 731
Cooperation between gene encoding p53 tumour antigen and ras in cellular transformation
Parada, L. F., Land, H., Weinberg, R. A., Wolf, D., & Rotter, V. (1984) · Nature · doi:10.1038/312649a0 · Cited by 734
Renart, J., Reiser, J., & Stark, G. R. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.7.3116 · Cited by 730
Metadata
- Authors
- LAEMMLI, U. K.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- LAEMMLI, U. K.
- Venue
- Nature
- Published
- 1970-08
- Volume
- 227
- Issue
- 5259
- Pages
- 680-685
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2100837269
- Cited by
- 249,961
- References
- 21
- Citations by year
- 2026: 1249 · 2025: 1666 · 2024: 1888 · 2023: 2073 · 2022: 2397 · 2021: 2628 · 2020: 2933 · 2019: 2771 · 2018: 2930 · 2017: 3226 · 2016: 3362 · 2015: 3679 · 2014: 4166 · 2013: 4392 · 2012: 4509
- FWCI
- 333.16
- Type
- journal article
- Language
- en
- Open access
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- bacteriophage T4, structural proteins, proteolytic cleavage, precursor protein, gene products, assembly intermediates
- MeSH terms
- Autoradiography, Carbon Isotopes, Coliphages, Electrophoresis, Disc, Genes, Genetics, Microbial, Kinetics, Viral Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review