The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A simple method for displaying the hydropathic character of a protein
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
PARSEGIAN, A. (1969) · Nature · doi:10.1038/221844a0 · Cited by 854
Hermann, R. B. (1972) · The Journal of Physical Chemistry · doi:10.1021/j100663a023 · Cited by 700
Research works printed but not linked: 63
- Allen, 1980, Biochem. J, 187, 591, 10.1042/bj1870591 · DOI
- Anderson, 1981, Nature (London), 290, 457, 10.1038/290457a0 · DOI
- Bayley, 1981, 78, 2225
- Bigelow, 1967, J. Theoret. Biol, 16, 187, 10.1016/0022-5193(67)90004-5 · DOI
- Bonitz, 1980, J. Biol. Chem, 255, 11927, 10.1016/S0021-9258(19)70224-5 · DOI · Paper page
- Bull, 1974, Arch. Biochem. Biophys, 161, 665, 10.1016/0003-9861(74)90352-X · DOI · Paper page
- Buse, 1978, Hoppe-Seyler's Z. Physiol. Chem, 359, 1005, 10.1515/bchm2.1978.359.2.1005 · DOI
- Capaldi, 1972, 69, 930
- Chothia, 1976, J. Mol. Biol, 105, 1, 10.1016/0022-2836(76)90191-1 · DOI · Paper page
- Chothia, 1981, 78, 4146
- Chou, 1973, J. Mol. Biol, 74, 263, 10.1016/0022-2836(73)90372-0 · DOI
- Cohn, 1934, J. Amer. Chem. Soc, 56, 784, 10.1021/ja01319a006 · DOI
- Coruzzi, 1979, J. Biol. Chem, 254, 9324, 10.1016/S0021-9258(19)86848-5 · DOI
- Dayhoff, 1978, vol. 5
- Deno, 1963, J. Org. Chem, 28, 2143, 10.1021/jo01043a503 · DOI
- Doolittle, 1981, Science, 214, 149, 10.1126/science.7280687 · DOI
- Drickamer, 1977, J. Biol. Chem, 252, 6909, 10.1016/S0021-9258(17)39935-0 · DOI
- Engelman, 1980, 77, 2023
- Eventhoff, 1977, 74, 2677
- Fisher, 1964, 51, 1285
- Fleming, 1979, Biochemistry, 18, 5458, 10.1021/bi00591a031 · DOI
- Freer, 1970, Biochemistry, 9, 1997, 10.1021/bi00811a022 · DOI
- Fuller, 1979, J. Mol. Biol, 134, 305, 10.1016/0022-2836(79)90037-8 · DOI
- Garnier, 1978, J. Mol. Biol, 120, 97, 10.1016/0022-2836(78)90297-8 · DOI · Paper page
- Heller, 1968, Biochemistry, 7, 2906, 10.1021/bi00848a030 · DOI · Paper page
- Henderson, 1975, Nature (London), 257, 28, 10.1038/257028a0 · DOI
- Hine, 1975, J. Org. Chem, 40, 292, 10.1021/jo00891a006 · DOI
- Ho, 1975, J. Biol. Chem, 250, 675, 10.1016/S0021-9258(19)41949-2 · DOI · Paper page
- Janin, 1980, J. Mol. Biol, 143, 95, 10.1016/0022-2836(80)90126-6 · DOI
- Kauzmann, 1959, Advan. Protein Chem, 14, 1, 10.1016/S0065-3233(08)60608-7 · DOI · Paper page
- Khorana, 1979, 76, 5046
- King, 1980, 77, 4726
- Klotz, 1968, Biochemistry, 7, 3879, 10.1021/bi00851a013 · DOI
- Klotz, 1962, J. Amer. Chem. Soc, 84, 3461, 10.1021/ja00877a009 · DOI
- Kristof, 1980, Biophys. Struct. Mech, 6, 209, 10.1007/BF00537294 · DOI
- Kyte, 1972, J. Biol. Chem, 247, 7642, 10.1016/S0021-9258(19)44573-0 · DOI · Paper page
- Lifson, 1979, Nature (London), 282, 109, 10.1038/282109a0 · DOI
- Nakashima, 1974, J. Mol. Biol, 88, 598, 10.1016/0022-2836(74)90410-0 · DOI
- Nobraga, 1980, J. Biol. Chem, 255, 9828, 10.1016/S0021-9258(18)43467-9 · DOI
- Nozaki, 1971, J. Biol. Chem, 246, 2211, 10.1016/S0021-9258(19)77210-X · DOI · Paper page
- Pober, 1975, J. Mol. Biol, 95, 477, 10.1016/0022-2836(75)90204-1 · DOI
- Rose, 1978, Nature (London), 272, 586, 10.1038/272586a0 · DOI · Paper page
- Rose, 1980, 77, 4643
- Rose, 1980, 77, 3884
- Sacher, 1979, Hoppe-Seyler's Z. Physiol. Chem, 360, 1385, 10.1515/bchm2.1979.360.2.1385 · DOI
- Segrest, 1974, J. Mol. Biol, 87, 853, 10.1016/0022-2836(74)90090-4 · DOI
- Sogin, 1978, J. Supramol. Struct, 8, 447, 10.1002/jss.400080407 · DOI
- Steck, 1978, Biochemistry, 17, 1216, 10.1021/bi00600a013 · DOI
- Steffens, 1979, Hoppe-Seyler's Z. Physiol. Chem, 360, 613
- Strittmatter, 1972, J. Biol. Chem, 247, 7188, 10.1016/S0021-9258(19)44612-7 · DOI · Paper page
- Tanaka, 1979, J. Biol. Chem, 254, 3879, 10.1016/S0021-9258(18)50669-4 · DOI
- Tanford, 1968, Advan. Protein Chem, 23, 121, 10.1016/S0065-3233(08)60401-5 · DOI
- Thalenfeld, 1980, J. Biol. Chem, 255, 6173, 10.1016/S0021-9258(18)43718-0 · DOI
- Tomita, 1975, 72, 2964
- Tomita, 1978, Biochemistry, 17, 4756, 10.1021/bi00615a025 · DOI
- Traube, 1899, Samml. Chem. Chem.-Tech. Vortr, 4, 19
- Vandlen, 1979, Biochemistry, 18, 1845, 10.1021/bi00577a001 · DOI
- von Heijne, 1979, Eur. J. Biochem, 97, 175, 10.1111/j.1432-1033.1979.tb13100.x · DOI
- Wang, 1968, Science, 161, 328, 10.1126/science.161.3839.328 · DOI
- Wolfenden, 1979, Science, 206, 575, 10.1126/science.493962 · DOI
- Wolfenden, 1981, Biochemistry, 20, 849, 10.1021/bi00507a030 · DOI
- Wu, 1973, J. Mol. Biol, 75, 13, 10.1016/0022-2836(73)90526-3 · DOI
- Zimmerman, 1968, J. Theoret. Biol, 21, 170, 10.1016/0022-5193(68)90069-6 · DOI · Paper page
Cited by
Identification of the Cystic Fibrosis Gene: Cloning and Characterization of Complementary DNA
Riordan, J. R., Rommens, J. M., Kerem, B.-S., Alon, N., Rozmahel, R., Grzelczak, Z., Zielenski, J., Lok, S., Plavsic, N., Chou, J.-L., et al. (1989) · Science · doi:10.1126/science.2475911 · Cited by 7,418
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
Cloning of adiponectin receptors that mediate antidiabetic metabolic effects
Yamauchi, T., Kamon, J., Ito, Y., Tsuchida, A., Yokomizo, T., Kita, S., Sugiyama, T., Miyagishi, M., Hara, K., Tsunoda, M., et al. (2003) · Nature · doi:10.1038/nature01705 · Cited by 3,176
The Minimal Gene Complement of Mycoplasma genitalium
Fraser, C. M., Gocayne, J. D., White, O., Adams, M. D., Clayton, R. A., Fleischmann, R. D., Bult, C. J., Kerlavage, A. R., Sutton, G., Kelley, J. M., et al. (1995) · Science · doi:10.1126/science.270.5235.397 · Cited by 2,545
Pao, S. S., Paulsen, I. T., & Saier, M. H. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.1.1-34.1998 · Cited by 2,297
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Rogaev, E. I., Sherrington, R., Rogaeva, E. A., Levesque, G., Ikeda, M., Liang, Y., Chi, H., Lin, C., Holman, K., Tsuda, T., et al. (1995) · Nature · doi:10.1038/376775a0 · Cited by 2,052
Chen, C.-J., Chin, J. E., Ueda, K., Clark, D. P., Pastan, I., Gottesman, M. M., & Roninson, I. B. (1986) · Cell · doi:10.1016/0092-8674(86)90595-7 · Cited by 1,898
Convergent Antibody Responses to SARS-CoV-2 in Convalescent Individuals
Robbiani, D. F., Gaebler, C., Muecksch, F., Lorenzi, J. C. C., Wang, Z., Cho, A., Agudelo, M., Barnes, C. O., Gazumyan, A., Finkin, S., et al. (2020) · Nature · doi:10.1038/s41586-020-2456-9 · Cited by 1,853
Molecular cloning and characterization of the rat NMDA receptor
Moriyoshi, K., Masu, M., Ishii, T., Shigemoto, R., Mizuno, N., & Nakanishi, S. (1991) · Nature · doi:10.1038/354031a0 · Cited by 1,771
Evolution of antibody immunity to SARS-CoV-2
Gaebler, C., Wang, Z., Lorenzi, J. C. C., Muecksch, F., Finkin, S., Tokuyama, M., Cho, A., Jankovic, M., Schaefer-Babajew, D., Oliveira, T. Y., et al. (2021) · Nature · doi:10.1038/s41586-021-03207-w · Cited by 1,674
Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese
Enerbäck, S., Jacobsson, A., Simpson, E. M., Guerra, C., Yamashita, H., Harper, M.-E., & Kozak, L. P. (1997) · Nature · doi:10.1038/387090a0 · Cited by 1,379
mRNA vaccine-elicited antibodies to SARS-CoV-2 and circulating variants
Wang, Z., Schmidt, F., Weisblum, Y., Muecksch, F., Barnes, C. O., Finkin, S., Schaefer-Babajew, D., Cipolla, M., Gaebler, C., Lieberman, J. A., et al. (2021) · Nature · doi:10.1038/s41586-021-03324-6 · Cited by 1,343
Cooper, G. J., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., & Reid, K. B. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8628 · Cited by 1,299
Syntaxin: A Synaptic Protein Implicated in Docking of Synaptic Vesicles at Presynaptic Active Zones
Bennett, M. K., Calakos, N., & Scheller, R. H. (1992) · Science · doi:10.1126/science.1321498 · Cited by 1,263
Structural basis of water-specific transport through the AQP1 water channel
Sui, H., Han, B.-G., Lee, J. K., Walian, P., & Jap, B. K. (2001) · Nature · doi:10.1038/414872a · Cited by 1,166
A Novel Family of Divergent Seven-Transmembrane Proteins
Clyne, P. J., Warr, C. G., Freeman, M. R., Lessing, D., Kim, J., & Carlson, J. R. (1999) · Neuron · doi:10.1016/s0896-6273(00)81093-4 · Cited by 1,155
Multiblock Polymers: Panacea or Pandora’s Box?
Bates, F. S., Hillmyer, M. A., Lodge, T. P., Bates, C. M., Delaney, K. T., & Fredrickson, G. H. (2012) · Science · doi:10.1126/science.1215368 · Cited by 1,147
Primary structure and expression from complementary DNA of skeletal muscle ryanodine receptor
Takeshima, H., Nishimura, S., Matsumoto, T., Ishida, H., Kangawa, K., Minamino, N., Matsuo, H., Ueda, M., Hanaoka, M., Hirose, T., et al. (1989) · Nature · doi:10.1038/339439a0 · Cited by 1,146
Lu, P., Vogel, C., Wang, R., Yao, X., & Marcotte, E. M. (2007) · Nature Biotechnology · doi:10.1038/nbt1270 · Cited by 1,139
A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
Brown, M. S., & Goldstein, J. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11041 · Cited by 1,134
The neurofibromatosis type 1 gene encodes a protein related to GAP
Xu, G., O'Connell, P., Viskochil, D., Cawthon, R., Robertson, M., Culver, M., Dunn, D., Stevens, J., Gesteland, R., White, R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90024-9 · Cited by 1,095
Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg
Vidal, S. M., Malo, D., Vogan, K., Skamene, E., & Gros, P. (1993) · Cell · doi:10.1016/0092-8674(93)90135-d · Cited by 1,104
The basics of thiols and cysteines in redox biology and chemistry
Poole, L. B. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.013 · Cited by 1,031
Crucial Step in Cholesterol Homeostasis
Yang, T., Espenshade, P. J., Wright, M. E., Yabe, D., Gong, Y., Aebersold, R., Goldstein, J. L., & Brown, M. S. (2002) · Cell · doi:10.1016/s0092-8674(02)00872-3 · Cited by 987
Melanopsin: An opsin in melanophores, brain, and eye
Provencio, I., Jiang, G., De Grip, W. J., Hayes, W. P., & Rollag, M. D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.1.340 · Cited by 975
A family of metabotropic glutamate receptors
Tanabe, Y., Masu, M., Ishii, T., Shigemoto, R., & Nakanishi, S. (1992) · Neuron · doi:10.1016/0896-6273(92)90118-w · Cited by 940
Gene transfer and molecular cloning of the rat nerve growth factor receptor
Radeke, M. J., Misko, T. P., Hsu, C., Herzenberg, L. A., & Shooter, E. M. (1987) · Nature · doi:10.1038/325593a0 · Cited by 938
Expression cloning of a cocaine-and antidepressant-sensitive human noradrenaline transporter
Pacholczyk, T., Blakely, R. D., & Amara, S. G. (1991) · Nature · doi:10.1038/350350a0 · Cited by 933
Meta-analysis of tumor- and T cell-intrinsic mechanisms of sensitization to checkpoint inhibition
Litchfield, K., Reading, J. L., Puttick, C., Thakkar, K., Abbosh, C., Bentham, R., Watkins, T. B. K., Rosenthal, R., Biswas, D., Rowan, A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.002 · Cited by 893
The Human Gene Mutation Database: 2008 update
Stenson, P. D., Mort, M., Ball, E. V., Howells, K., Phillips, A. D., Thomas, N. S., & Cooper, D. N. (2009) · Genome Medicine · doi:10.1186/gm13 · Cited by 873
Franco, B., Guioli, S., Pragliola, A., Incerti, B., Bardoni, B., Tonlorenzi, R., Carrozzo, R., Maestrini, E., Pieretti, M., Taillon-Miller, P., et al. (1991) · Nature · doi:10.1038/353529a0 · Cited by 846
Molecular code for transmembrane-helix recognition by the Sec61 translocon.
Hessa, T., Meindl-Beinker, N. M., Bernsel, A., Kim, H., Sato, Y., Lerch-Bader, M., Nilsson, I., White, S. H., & von Heijne, G. (2007) · Nature · doi:10.1038/nature06387 · Cited by 708
Identification of a Specialized Adenylyl Cyclase That May Mediate Odorant Detection
Bakalyar, H. A., & Reed, R. R. (1990) · Science · doi:10.1126/science.2255909 · Cited by 694
Ishiguro, S., & Nakamura, K. (1994) · Molecular and General Genetics MGG · doi:10.1007/bf00282746 · Cited by 664
Bettler, B., Boulter, J., Hermans-Borgmeyer, I., O'Shea-Greenfield, A., Deneris, E. S., Moll, C., Borgmeyer, U., Hollmann, M., & Heinemann, S. (1990) · Neuron · doi:10.1016/0896-6273(90)90213-y · Cited by 649
Lee, J. J., von Kessler, D. P., Parks, S., & Beachy, P. A. (1992) · Cell · doi:10.1016/0092-8674(92)90264-d · Cited by 581
Chang, C.-P., Pearse, R. V., O'Connell, S., & Rosenfeld, M. G. (1993) · Neuron · doi:10.1016/0896-6273(93)90230-o · Cited by 537
Wilks, A. F., Harpur, A. G., Kurban, R. R., Ralph, S. J., Zürcher, G., & Ziemiecki, A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.2057 · Cited by 528
The Drosophila learning and memory gene rutabaga encodes a - adenylyl cyclase
Levin, L. R., Han, P.-L., Hwang, P. M., Feinstein, P. G., Davis, R. L., & Reed, R. R. (1992) · Cell · doi:10.1016/0092-8674(92)90185-f · Cited by 517
KAR3, a kinesin-related gene required for yeast nuclear fusion
Meluh, P. (1990) · Cell · doi:10.1016/0092-8674(90)90351-e · Cited by 503
Andersson, S., & Russell, D. W. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3640 · Cited by 501
Kibar, Z., Vogan, K. J., Groulx, N., Justice, M. J., Underhill, D. A., & Gros, P. (2001) · Nature Genetics · doi:10.1038/90081 · Cited by 504
CAMP: a useful resource for research on antimicrobial peptides.
Thomas, S., Karnik, S., Barai, R. S., Jayaraman, V. K., & Idicula-Thomas, S. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp1021 · Cited by 462
Humphries, M. J., Akiyama, S. K., Komoriya, A., Olden, K., & Yamada, K. M. (1986) · The Journal of cell biology · doi:10.1083/jcb.103.6.2637 · Cited by 438
Hashimoto, T., Horikawa, D. D., Saito, Y., Kuwahara, H., Kozuka-Hata, H., Shin-I, T., Minakuchi, Y., Ohishi, K., Motoyama, A., Aizu, T., et al. (2016) · Nature Communications · doi:10.1038/ncomms12808 · Cited by 394
Sterol Resistance in CHO Cells Traced to Point Mutation in SREBP Cleavage–Activating Protein
Hua, X., Nohturfft, A., Goldstein, J. L., & Brown, M. S. (1996) · Cell · doi:10.1016/s0092-8674(00)81362-8 · Cited by 426
Genestier, A.-L., Michallet, M.-C., Prévost, G., Bellot, G., Chalabreysse, L., Peyrol, S., Thivolet, F., Etienne, J., Lina, G., Vallette, F. M., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci22684 · Cited by 416
PICADO-LEONARD, J., & MILLER, W. L. (1987) · DNA · doi:10.1089/dna.1987.6.439 · Cited by 415
The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
Hulko, M., Berndt, F., Gruber, M., Linder, J. U., Truffault, V., Schultz, A., Martin, J., Schultz, J. E., Lupas, A. N., & Coles, M. (2006) · Cell · doi:10.1016/j.cell.2006.06.058 · Cited by 416
Kamijo, K., Taketani, S., Yokota, S., Osumi, T., & Hashimoto, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39595-x · Cited by 391
Kikkert, M., Doolman, R., Dai, M., Avner, R., Hassink, G., van Voorden, S., Thanedar, S., Roitelman, J., Chau, V., & Wiertz, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307453200 · Cited by 384
PRICE, T. N., JACKSON, N. V., & HALESTRAP, P. A. (1998) · Biochemical Journal · doi:10.1042/bj3290321 · Cited by 361
Current insights into protein solubility: A review of its importance for alternative proteins
Grossmann, L., & McClements, D. J. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108416 · Cited by 367
Ross, J. I., Eady, E. A., Cove, J. H., Cunliffe, W. J., Baumberg, S., & Wootton, J. C. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb00696.x · Cited by 358
Abello, N., Kerstjens, H. A. M., Postma, D. S., & Bischoff, R. (2009) · Journal of Proteome Research · doi:10.1021/pr900039c · Cited by 359
A quantitative measure of error minimization in the genetic code
Haig, D., & Hurst, L. D. (1991) · Journal of Molecular Evolution · doi:10.1007/bf02103132 · Cited by 337
Henderson, I. R., Czeczulin, J., Eslava, C., Noriega, F., & Nataro, J. P. (1999) · Infection and Immunity · doi:10.1128/iai.67.11.5587-5596.1999 · Cited by 357
Five computational developability guidelines for therapeutic antibody profiling
Raybould, M. I. J., Marks, C., Krawczyk, K., Taddese, B., Nowak, J., Lewis, A. P., Bujotzek, A., Shi, J., & Deane, C. M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810576116 · Cited by 357
A receptor for subgroup A Rous sarcoma virus is related to the low density lipoprotein receptor
Bates, P., Young, J. A. T., & Varmus, H. E. (1993) · Cell · doi:10.1016/0092-8674(93)90726-7 · Cited by 355
Sundstrom, P. (2002) · Cellular Microbiology · doi:10.1046/j.1462-5822.2002.00206.x · Cited by 336
Proteomics of Integral Membrane ProteinsTheory and Application
Speers, A. E., & Wu, C. C. (2007) · Chemical Reviews · doi:10.1021/cr068286z · Cited by 325
Klionsky, D. J., & Emr, S. D. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08348.x · Cited by 325
Protein design and variant prediction using autoregressive generative models
Shin, J.-E., Riesselman, A. J., Kollasch, A. W., McMahon, C., Simon, E., Sander, C., Manglik, A., Kruse, A. C., & Marks, D. S. (2021) · Nature Communications · doi:10.1038/s41467-021-22732-w · Cited by 320
Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase.
Chen, J.-M., Dando, P. M., Rawlings, N. D., Brown, M. A., Young, N. E., Stevens, R. A., Hewitt, E., Watts, C., & Barrett, A. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.8090 · Cited by 320
Francois, V, Solloway, M., O'Neill, J. W., Emery, J., & Bier, E. (1994) · Genes & Development · doi:10.1101/gad.8.21.2602 · Cited by 308
Boulter, J., O'Shea-Greenfield, A., Duvoisin, R. M., Connolly, J. G., Wada, E., Jensen, A., Gardner, P. D., Ballivet, M., Deneris, E. S., & McKinnon, D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39588-2 · Cited by 302
INPS-MD: a web server to predict stability of protein variants from sequence and structure
Savojardo, C., Fariselli, P., Martelli, P. L., & Casadio, R. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw192 · Cited by 290
Ebola Virus VP40-Induced Particle Formation and Association with the Lipid Bilayer
Jasenosky, L. D., Neumann, G., Lukashevich, I., & Kawaoka, Y. (2001) · Journal of Virology · doi:10.1128/jvi.75.11.5205-5214.2001 · Cited by 286
Tyrosine biosynthesis, metabolism, and catabolism in plants
Schenck, C. A., & Maeda, H. A. (2018) · Phytochemistry · doi:10.1016/j.phytochem.2018.02.003 · Cited by 286
Sogo, L. F., & Yaffe, M. P. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.6.1361 · Cited by 284
Amaya, Y., Yamazaki, K., Sato, M., Noda, K., Nishino, T., & Nishino, T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77283-9 · Cited by 275
Rutledge, B. J., Zhang, K., Bier, E., Jan, Y. N., & Perrimon, N. (1992) · Genes & Development · doi:10.1101/gad.6.8.1503 · Cited by 274
Role of molecular charge and hydrophilicity in regulating the kinetics of crystal growth
Elhadj, S., De Yoreo, J. J., Hoyer, J. R., & Dove, P. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605748103 · Cited by 270
Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from NCB-20 cells.
Yoshimura, M., & Cooper, D. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.15.6716 · Cited by 268
Conformational states dynamically populated by a kinase determine its function
Xie, T., Saleh, T., Rossi, P., & Kalodimos, C. G. (2020) · Science · doi:10.1126/science.abc2754 · Cited by 266
CHLOROPLAST UNUSUAL POSITIONING1 Is Essential for Proper Chloroplast Positioning
Oikawa, K., Kasahara, M., Kiyosue, T., Kagawa, T., Suetsugu, N., Takahashi, F., Kanegae, T., Niwa, Y., Kadota, A., & Wada, M. (2003) · The Plant Cell · doi:10.1105/tpc.016428 · Cited by 258
Chung, C.-S., Chen, C.-H., Ho, M.-Y., Huang, C.-Y., Liao, C.-L., & Chang, W. (2006) · Journal of Virology · doi:10.1128/jvi.80.5.2127-2140.2006 · Cited by 253
Heckmann, D., Lloyd, C. J., Mih, N., Ha, Y., Zielinski, D. C., Haiman, Z. B., Desouki, A. A., Lercher, M. J., & Palsson, B. O. (2018) · Nature Communications · doi:10.1038/s41467-018-07652-6 · Cited by 218
Burgess, S. M., Delannoy, M., & Jensen, R. E. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.6.1375 · Cited by 249
A novel CPx‐ATPase from the cadmium hyperaccumulator Thlaspi caerulescens
Bernard, C., Roosens, N., Czernic, P., Lebrun, M., & Verbruggen, N. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.05.036 · Cited by 248
Numata, M., & Orlowski, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101319200 · Cited by 244
Leidich, S. D., Ibrahim, A. S., Fu, Y., Koul, A., Jessup, C., Vitullo, J., Fonzi, W., Mirbod, F., Nakashima, S., Nozawa, Y., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.26078 · Cited by 241
TCR contact residue hydrophobicity is a hallmark of immunogenic CD8 + T cell epitopes
Chowell, D., Krishna, S., Becker, P. D., Cocita, C., Shu, J., Tan, X., Greenberg, P. D., Klavinskis, L. S., Blattman, J. N., & Anderson, K. S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500973112 · Cited by 239
Genetic and biochemical characterization of the oligopeptide transport system of Lactococcus lactis
Tynkkynen, S., Buist, G., Kunji, E., Kok, J., Poolman, B., Venema, G., & Haandrikman, A. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.23.7523-7532.1993 · Cited by 231
Discovering highly potent antimicrobial peptides with deep generative model HydrAMP
Szymczak, P., Możejko, M., Grzegorzek, T., Jurczak, R., Bauer, M., Neubauer, D., Sikora, K., Michalski, M., Sroka, J., Setny, P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36994-z · Cited by 231
Yu, C. Y., Belt, K. T., Giles, C. M., Campbell, R. D., & Porter, R. R. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04582.x · Cited by 221
Optimization of Mass Spectrometry-Compatible Surfactants for Shotgun Proteomics
Chen, E. I., Cociorva, D., Norris, J. L., & Yates, J. R. (2007) · Journal of Proteome Research · doi:10.1021/pr060682a · Cited by 218
modlAMP: Python for antimicrobial peptides
Müller, A. T., Gabernet, G., Hiss, J. A., & Schneider, G. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx285 · Cited by 215
Scott, I., Webster, B. R., Li, J. H., & Sack, M. N. (2012) · Biochemical Journal · doi:10.1042/bj20120118 · Cited by 214
Finegold, A. A., Shatwell, K. P., Segal, A. W., Klausner, R. D., & Dancis, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31021 · Cited by 213
Hung, L. W., Ciccotosto, G. D., Giannakis, E., Tew, D. J., Perez, K., Masters, C. L., Cappai, R., Wade, J. D., & Barnham, K. J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.3916-08.2008 · Cited by 210
Katsushika, S., Chen, L., Kawabe, J., Nilakantan, R., Halnon, N. J., Homcy, C. J., & Ishikawa, Y. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.18.8774 · Cited by 209
Cloning and characterization of the human V3 pituitary vasopressin receptor
de Keyzer, Y., Auzan, C., Lenne, F., Beldjord, C., Thibonnier, M., Bertagna, X., & Clauser, E. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01268-7 · Cited by 209
Protein synthesis rates and ribosome occupancies reveal determinants of translation elongation rates
Riba, A., Di Nanni, N., Mittal, N., Arhné, E., Schmidt, A., & Zavolan, M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1817299116 · Cited by 209
Blaudez, D., Kohler, A., Martin, F., Sanders, D., & Chalot, M. (2003) · The Plant Cell · doi:10.1105/tpc.017541 · Cited by 200
Geber, A., Hitchcock, C. A., Swartz, J. E., Pullen, F. S., Marsden, K. E., Kwon-Chung, K. J., & Bennett, J. E. (1995) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.39.12.2708 · Cited by 203
Moran, G. P., Sanglard, D., Donnelly, S. M., Shanley, D. B., Sullivan, D. J., & Coleman, D. C. (1998) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.42.7.1819 · Cited by 197
The SREBP Pathway in Drosophila
Seegmiller, A. C., Dobrosotskaya, I., Goldstein, J. L., Ho, Y. K., Brown, M. S., & Rawson, R. B. (2002) · Developmental Cell · doi:10.1016/s1534-5807(01)00119-8 · Cited by 194
Metadata
- Authors
- Kyte, J., & Doolittle, R. F.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1982-05
- Volume
- 157
- Issue
- 1
- Pages
- 105-132
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1975304761
- Cited by
- 22,843
- References
- 3
- FWCI
- 77.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.