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
Items 101–200 of 249
Paidhungat, M., & Garrett, S. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6339 · Cited by 191
Temperature-dependent solvation modulates the dimensions of disordered proteins
Wuttke, R., Hofmann, H., Nettels, D., Borgia, M. B., Mittal, J., Best, R. B., & Schuler, B. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313006111 · Cited by 192
Identification of the key structural motifs involved in HspB8/HspB6–Bag3 interaction
Fuchs, M., Poirier, D. J., Seguin, S. J., Lambert, H., Carra, S., Charette, S. J., & Landry, J. (2010) · Biochemical Journal · doi:10.1042/bj20090907 · Cited by 190
Emanuelli, M., Carnevali, F., Saccucci, F., Pierella, F., Amici, A., Raffaelli, N., & Magni, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008700200 · Cited by 189
Guimera, J., Casas, C., Estivill, X., & Pritchard, M. (1999) · Genomics · doi:10.1006/geno.1999.5775 · Cited by 186
Point Mutations (Thr240Arg and Ala311Stop) in theParkinGene
Hattori, N., Matsumine, H., Asakawa, S., Kitada, T., Yoshino, H., Elibol, B., Brookes, A. J., Yamamura, Y., Kobayashi, T., Wang, M., et al. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9134 · Cited by 181
Where Have All the Interactions Gone? Estimating the Coverage of Two-Hybrid Protein Interaction Maps
Huang, H., Jedynak, B. M., & Bader, J. S. (2007) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0030214 · Cited by 182
PIG‐S and PIG‐T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8
Ohishi, K., Inoue, N., & Kinoshita, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4088 · Cited by 177
Pimenta, A. F., Zhukareva, V., Barbe, M. F., Reinoso, B. S., Grimley, C., Henzel, W., Fischer, I., & Levitt, P. (1995) · Neuron · doi:10.1016/0896-6273(95)90034-9 · Cited by 172
Rajan, D. P., Huang, W., Dutta, B., Devoe, L. D., Leibach, F. H., Ganapathy, V., & Prasad, P. D. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1272 · Cited by 162
The Hydrophobic Temperature Dependence of Amino Acids Directly Calculated from Protein Structures
van Dijk, E., Hoogeveen, A., & Abeln, S. (2015) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004277 · Cited by 162
“More specifically, hydrophobicity scales for the different amino acid types may be obtained using physicochemical properties [18], or by calculating how often we find each residue type exposed to the solvent at the surface of a protein [18–21].”
Localization of adipocyte long-chain fatty acyl-CoA synthetase at the plasma membrane
Gargiulo, C. E., Stuhlsatz-Krouper, S. M., & Schaffer, J. E. (1999) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32123-4 · Cited by 156
Higgs, P. G. (2009) · Biology Direct · doi:10.1186/1745-6150-4-16 · Cited by 137
Furin mediates enhanced production of fibrillogenic ABri peptides in familial British dementia
Kim, S.-H., Wang, R., Gordon, D. J., Bass, J., Steiner, D. F., Lynn, D. G., Thinakaran, G., Meredith, S. C., & Sisodia, S. S. (1999) · Nature Neuroscience · doi:10.1038/14783 · Cited by 154
Identification and Characterization of a Novel Human Collectin CL-K1
Keshi, H., Sakamoto, T., Kawai, T., Ohtani, K., Katoh, T., Jang, S., Motomura, W., Yoshizaki, T., Fukuda, M., Koyama, S., et al. (2006) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2006.tb03868.x · Cited by 150
Toward the molecular structure of the mitochondrial channel, VDAC
Mannella, C. A., Forte, M., & Colombini, M. (1992) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00769525 · Cited by 150
Structure of the STRA6 receptor for retinol uptake
Chen, Y., Clarke, O. B., Kim, J., Stowe, S., Kim, Y.-K., Assur, Z., Cavalier, M., Godoy-Ruiz, R., von Alpen, D. C., Manzini, C., et al. (2016) · Science · doi:10.1126/science.aad8266 · Cited by 148
Buurman, E. T., Westwater, C., Hube, B., Brown, A. J. P., Odds, F. C., & Gow, N. A. R. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7670 · Cited by 146
Carnitine transport: Pathophysiology and metabolism of known molecular defects
Tein, I. (2003) · Journal of Inherited Metabolic Disease · doi:10.1023/a:1024481016187 · Cited by 140
Tailor, C. S., Willett, B. J., & Kabat, D. (1999) · Journal of Virology · doi:10.1128/jvi.73.8.6500-6505.1999 · Cited by 137
Rodrigues, V., Cheah, P. Y., Ray, K., & Chia, W. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07303.x · Cited by 136
Rexroth, S., Mullineaux, C. W., Ellinger, D., Sendtko, E., Rögner, M., & Koenig, F. (2011) · The Plant Cell · doi:10.1105/tpc.111.085779 · Cited by 136
Hong, W., Jiao, W., Hu, J., Zhang, J., Liu, C., Fu, X., Shen, D., Xia, B., & Chang, Z. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503934200 · Cited by 132
Li, Y., Champion, M. M., Sun, L., Champion, P. A. D., Wojcik, R., & Dovichi, N. J. (2012) · Analytical Chemistry · doi:10.1021/ac202899p · Cited by 128
Tanaka, S., Tanaka, J., Miwa, Y., Horikawa, D. D., Katayama, T., Arakawa, K., Toyoda, A., Kubo, T., & Kunieda, T. (2015) · PLOS ONE · doi:10.1371/journal.pone.0118272 · Cited by 128
Smith, R. L., Thompson, L. J., & Maguire, M. E. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.5.1233-1238.1995 · Cited by 127
Sougakoff, W., Papadopoulou, B., Nordmann, P., & Courvalin, P. (1987) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1987.tb02260.x · Cited by 124
Single-chain heteropolymers transport protons selectively and rapidly
Jiang, T., Hall, A., Eres, M., Hemmatian, Z., Qiao, B., Zhou, Y., Ruan, Z., Couse, A. D., Heller, W. T., Huang, H., et al. (2020) · Nature · doi:10.1038/s41586-019-1881-0 · Cited by 122
Hong, Y., Ohishi, K., Kang, J. Y., Tanaka, S., Inoue, N., Nishimura, J.-I., Maeda, Y., & Kinoshita, T. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-12-0794 · Cited by 121
Evers, M. R., Xia, G., Kang, H.-G., Schachner, M., & Baenziger, J. U. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105848200 · Cited by 117
The origin of the biologically coded amino acids
Cleaves II, H. J. (2010) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2009.12.014 · Cited by 108
Gough, W. H., VanOoteghem, S., Sint, T., & Kedishvili, N. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.31.19778 · Cited by 114
Solubility-Weighted Index: fast and accurate prediction of protein solubility
Bhandari, B. K., Gardner, P. P., & Lim, C. S. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa578 · Cited by 97
Understanding Retinol Metabolism: Structure and Function of Retinol Dehydrogenases
Lidén, M., & Eriksson, U. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.r500027200 · Cited by 109
Fertala, A. (2020) · Bioengineering · doi:10.3390/bioengineering7040155 · Cited by 109
Lelias, J. M., Adra, C. N., Wulf, G. M., Guillemot, J. C., Khagad, M., Caput, D., & Lim, B. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.4.1479 · Cited by 109
Secretion of islet amyloid polypeptide in response to glucose
Kanatsuka, A., Makino, H., Ohsawa, H., Tokuyama, Y., Yamaguchi, T., Yoshida, S., & Adachi, M. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81527-3 · Cited by 107
Identification of a Sialidase Encoded in the Human Major Histocompatibility Complex
Milner, C. M., Smith, S. V., Carrillo, M. B., Taylor, G. L., Hollinshead, M., & Campbell, R. D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4549 · Cited by 106
Pox proteomics: mass spectrometry analysis and identification of Vaccinia virion proteins
Yoder, J. D., Chen, T. S., Gagnier, C. R., Vemulapalli, S., Maier, C. S., & Hruby, D. E. (2006) · Virology Journal · doi:10.1186/1743-422x-3-10 · Cited by 104
Feinstein, Y., Borrell, V., Garcia, C., Burstyn-Cohen, T., Tzarfaty, V., Frumkin, A., Nose, A., Okamoto, H., Higashijima, S.-I., Soriano, E., et al. (1999) · Development · doi:10.1242/dev.126.16.3637 · Cited by 105
Systematic discovery of protein interaction interfaces using AlphaFold and experimental validation
Lee, C. Y., Hubrich, D., Varga, J. K., Schäfer, C., Welzel, M., Schumbera, E., Djokic, M., Strom, J. M., Schönfeld, J., Geist, J. L., et al. (2024) · Molecular Systems Biology · doi:10.1038/s44320-023-00005-6 · Cited by 105
“In cases where the motif adopts partial secondary structure, such as loop-helix-loop or loop-strand-loop, they are treated as helical or strand, respectively.”
Systematic discovery of protein interaction interfaces using AlphaFold and experimental validation
Lee, C. Y., Hubrich, D., Varga, J. K., Schäfer, C., Welzel, M., Schumbera, E., Đokić, M., Strom, J. M., Schönfeld, J., Geist, J. L., et al. (2023) · doi:10.1101/2023.08.07.552219 · Cited by 105
Putrescine N-methyltransferase – The start for alkaloids
Biastoff, S., Brandt, W., & Dräger, B. (2009) · Phytochemistry · doi:10.1016/j.phytochem.2009.06.012 · Cited by 87
Zolfaghari, R., & Ross, A. C. (2000) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)32364-6 · Cited by 96
Li, L., Gupta, E., Spaeth, J., Shing, L., Jaimes, R., Engelhart, E., Lopez, R., Caceres, R. S., Bepler, T., & Walsh, M. E. (2023) · Nature Communications · doi:10.1038/s41467-023-39022-2 · Cited by 96
Casein and casein micelle structures, functions and diversity in 20 species.
Holt, C. (2016) · International Dairy Journal · doi:10.1016/j.idairyj.2016.01.004 · Cited by 95
Mirror-image T7 transcription of chirally inverted ribosomal and functional RNAs
Xu, Y., & Zhu, T. F. (2022) · Science · doi:10.1126/science.abm0646 · Cited by 94
Welte, T., Kudva, R., Kuhn, P., Sturm, L., Braig, D., Müller, M., Warscheid, B., Drepper, F., & Koch, H.-G. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-07-0590 · Cited by 87
Weissman, Z., Shemer, R., & Kornitzer, D. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02976.x · Cited by 88
An overview of the prediction of protein DNA-binding sites
Si, J., Zhao, R., & Wu, R. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16035194 · Cited by 91
Perchlorate Reductase Is Distinguished by Active Site Aromatic Gate Residues
Youngblut, M. D., Tsai, C.-L., Clark, I. C., Carlson, H. K., Maglaqui, A. P., Gau-Pan, P. S., Redford, S. A., Wong, A., Tainer, J. A., & Coates, J. D. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.714618 · Cited by 88
Miclo, L., Roux, É., Genay, M., Brusseaux, É., Poirson, C., Jameh, N., Perrin, C., & Dary, A. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf202176d · Cited by 87
Cloning and Characterization of Cyclooxygenase-1b (Putative Cyclooxygenase-3) in Rat
Snipes, J. A., Kis, B., Shelness, G. S., Hewett, J. A., & Busija, D. W. (2005) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.079533 · Cited by 82
Identification of a novel growth factor-responsive gene in vascular smooth muscle cells
Wax, S. D., Rosenfield, C. L., & Taubman, M. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99981-3 · Cited by 82
Ozaki, K., Doi, H., Mitsui, J., Sato, N., Iikuni, Y., Majima, T., Yamane, K., Irioka, T., Ishiura, H., Doi, K., et al. (2015) · JAMA Neurology · doi:10.1001/jamaneurol.2015.0610 · Cited by 81
Baron, S. F., Franklund, C. V., & Hylemon, P. B. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.15.4558-4569.1991 · Cited by 80
Chromosome‐Determined Zinc‐Responsible Operon czr in Staphylococcus aureus Strain 912
Kuroda, M., Hayashi, H., & Ohta, T. (1999) · Microbiology and Immunology · doi:10.1111/j.1348-0421.1999.tb02382.x · Cited by 78
FTDP-17 Tau Mutations Induce Distinct Effects on Aggregation and Microtubule Interactions
Combs, B., & Gamblin, T. C. (2012) · Biochemistry · doi:10.1021/bi3010818 · Cited by 79
Grevesse, C., Lepoivre, P., & Jijakli, M. H. (2003) · Phytopathology® · doi:10.1094/phyto.2003.93.9.1145 · Cited by 78
Zhai, Y., Heijne, W. H. M., Smith, D. W., & Saier, M. H. (2001) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(00)00389-8 · Cited by 75
Cch1 Mediates Calcium Entry in Cryptococcus neoformans and Is Essential in Low-Calcium Environments
Liu, M., Du, P., Heinrich, G., Cox, G. M., & Gelli, A. (2006) · Eukaryotic Cell · doi:10.1128/ec.00158-06 · Cited by 76
Song, Z., Krishna, S., Thanos, D., Strominger, J. L., & Ono, S. J. (1994) · The Journal of experimental medicine · doi:10.1084/jem.180.5.1763 · Cited by 72
McCaffrey, G., Seelbach, M. J., Staatz, W. D., Nametz, N., Quigley, C., Campos, C. R., Brooks, T. A., & Davis, T. P. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05582.x · Cited by 71
Sequence-to-conformation relationships of disordered regions tethered to folded domains of proteins
Mittal, A., Holehouse, A. S., Cohan, M. C., & Pappu, R. V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.05.012 · Cited by 72
Hammacott, J. E., Williams, P. H., & Cashmore, A. M. (2000) · Microbiology · doi:10.1099/00221287-146-4-869 · Cited by 69
Bassoon contributes to tau-seed propagation and neurotoxicity
Martinez, P., Patel, H., You, Y., Jury, N., Perkins, A., Lee-Gosselin, A., Taylor, X., You, Y., Viana Di Prisco, G., Huang, X., et al. (2022) · Nature Neuroscience · doi:10.1038/s41593-022-01191-6 · Cited by 68
Prediction of antimicrobial peptides based on the adaptive neuro‐fuzzy inference system application
Fernandes, F. C., Rigden, D. J., & Franco, O. L. (2012) · Peptide Science · doi:10.1002/bip.22066 · Cited by 67
The hydrophobic moment and its use in the classification of amphiphilic structures (Review)
Phoenix, D. A., & Harris, F. (2002) · Molecular Membrane Biology · doi:10.1080/09687680110103631 · Cited by 66
Molecular Cloning and Functional Expression of Alternative Oxidase from Candida albicans
Huh, W.-K., & Kang, S.-O. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.13.4098-4102.1999 · Cited by 66
Human ABC Transporter ABCG2 in Xenobiotic Protection and Redox Biology
Wakabayashi, K., Tamura, A., Saito, H., Onishi, Y., & Ishikawa, T. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600727947 · Cited by 66
Roure, B., & Philippe, H. (2011) · BMC Evolutionary Biology · doi:10.1186/1471-2148-11-17 · Cited by 64
Martins, V. P., Dinamarco, T. M., Soriani, F. M., Tudella, V. G., Oliveira, S. C., Goldman, G. H., Curti, C., & Uyemura, S. A. (2011) · Eukaryotic Cell · doi:10.1128/ec.00194-10 · Cited by 64
Treml, K., Meimaroglou, D., Hentges, A., & Bause, E. (2000) · Glycobiology · doi:10.1093/glycob/10.5.493 · Cited by 63
Structural features of nucleosomes in interphase and metaphase chromosomes
Arimura, Y., Shih, R. M., Froom, R., & Funabiki, H. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.08.010 · Cited by 59
Neyrolles, O., Mintz, E., & Catty, P. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00089 · Cited by 56
REYES, F., GAVIRA, M., CASTILLO, F., & MORENO-VIVIÁN, C. (1998) · Biochemical Journal · doi:10.1042/bj3310897 · Cited by 56
Sequence and genetic analysis of the hemin storage (hms) system of Yersinia pestis
Lillard, J. W., Fetherston, J. D., Pedersen, L., Pendrak, M. L., & Perry, R. D. (1997) · Gene · doi:10.1016/s0378-1119(97)00071-1 · Cited by 54
The N-terminal Domain of Tomato 3-Hydroxy-3-methylglutaryl-CoA Reductases
Denbow, C. J., Lång, S., & Cramer, C. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9710 · Cited by 52
Qian, Y., Baisden, J. M., Zot, H. G., Van Winkle, W. B., & Flynn, D. C. (2000) · Experimental Cell Research · doi:10.1006/excr.1999.4795 · Cited by 51
Intermediate conformations of CD4-bound HIV-1 Env heterotrimers
Dam, K.-M. A., Fan, C., Yang, Z., & Bjorkman, P. J. (2023) · Nature · doi:10.1038/s41586-023-06639-8 · Cited by 50
Fan, J., & Papadopoulos, V. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076701 · Cited by 48
Burger, M., Woods, R. G., McCarthy, C., & Beacham, I. R. (2000) · Microbiology · doi:10.1099/00221287-146-12-3149 · Cited by 48
Bae, J. M., & Liu, J. R. (1997) · Molecular and General Genetics MGG · doi:10.1007/s004380050406 · Cited by 47
Olmo-Mira, M. F., Gavira, M., Richardson, D. J., Castillo, F., Moreno-Vivián, C., & Roldán, M. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406502200 · Cited by 44
Orti, G., & Meyer, A. (1996) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a025616 · Cited by 44
Greven, J. A., Wydra, J. R., Greer, R. A., Zhi, C., Price, D. A., Svoboda, J. D., Camitta, C. L. M., Washington, M., Leung, D. W., Song, Y., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00795-9 · Cited by 42
Kell, B., Jewers, R. J., Cason, J., Pakarian, F., Kaye, J. N., & Best, J. M. (1994) · Journal of General Virology · doi:10.1099/0022-1317-75-9-2451 · Cited by 42
Signals for protein targeting into and across membranes.
von Heijne, G. (1994) · Subcellular Biochemistry · doi:10.1007/978-1-4615-2401-4_1 · Cited by 40
Dudley, E. G., Husgen, A. C., He, W., & Steele, J. L. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.3.701-704.1996 · Cited by 40
Endothelialization of polyurethanes: Surface silanization and immobilization of REDV peptide
Butruk-Raszeja, B. A., Dresler, M. S., Kuźmińska, A., & Ciach, T. (2016) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2016.04.017 · Cited by 38
Cross-phyla protein annotation by structural prediction and alignment
Ruperti, F., Papadopoulos, N., Musser, J. M., Mirdita, M., Steinegger, M., & Arendt, D. (2023) · Genome Biology · doi:10.1186/s13059-023-02942-9 · Cited by 38
The benefits (and misfortunes) of SDS in top-down proteomics
Kachuk, C., & Doucette, A. A. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2017.03.002 · Cited by 39
Tandem metalloenzymes gate plant cell entry by pathogenic fungi
Bissaro, B., Kodama, S., Nishiuchi, T., Díaz-Rovira, A. M., Hage, H., Ribeaucourt, D., Haon, M., Grisel, S., Simaan, A. J., Beisson, F., et al. (2022) · Science Advances · doi:10.1126/sciadv.ade9982 · Cited by 37
Human Sialidase Neu3 is S-Acylated and Behaves Like an Integral Membrane Protein
Rodriguez-Walker, M., & Daniotti, J. L. (2017) · Scientific Reports · doi:10.1038/s41598-017-04488-w · Cited by 36
Membrane targeting and insertion of the C-tail protein SciP.
Pross, E., Soussoula, L., Seitl, I., Lupo, D., & Kuhn, A. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.09.001 · Cited by 35
Kuntumalla, S., Braisted, J. C., Huang, S.-T., Parmar, P. P., Clark, D. J., Alami, H., Zhang, Q., Donohue-Rolfe, A., Tzipori, S., Fleischmann, R. D., et al. (2009) · Proteome Science · doi:10.1186/1477-5956-7-22 · Cited by 35
DEGRONOPEDIA: a web server for proteome-wide inspection of degrons
Szulc, N. A., Stefaniak, F., Piechota, M., Soszyńska, A., Piórkowska, G., Cappannini, A., Bujnicki, J. M., Maniaci, C., & Pokrzywa, W. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae238 · Cited by 35
Does Intrinsic Disorder in Proteins Favor Their Interaction with Lipids?
Deryusheva, E., Nemashkalova, E., Galloux, M., Richard, C., Eléouët, J., Kovacs, D., Van Belle, K., Tompa, P., Uversky, V., & Permyakov, S. (2019) · PROTEOMICS · doi:10.1002/pmic.201800098 · Cited by 34
Wang, S.-S., & Brandriss, M. C. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.12.4431-4440.1987 · Cited by 32
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.