The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Sequence Variations within Protein Families are Linearly Related to Structural Variations
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Proteins with 50% identity and higher have been reported to have less than 1-Å difference between their backbones (60).”
From Electron bifurcation and fluoride efflux systems implicated in defluorination of perfluorinated unsaturated carboxylic acids by Acetobacterium spp (2024) · cites this paper as [60]
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
Evolutionary divergence and convergence in proteins.
ZUCKERKANDL, E., & PAULING, L. (1965) · Evolving Genes and Proteins · doi:10.1016/b978-1-4832-2734-4.50017-6 · Cited by 3,020
The relation between the divergence of sequence and structure in proteins.
Chothia, C., & Lesk, A. M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04288.x · Cited by 2,458
A new approach to protein fold recognition
Jones, D. T., Taylort, W. R., & Thornton, J. M. (1992) · Nature · doi:10.1038/358086a0 · Cited by 1,221
Research works printed but not linked: 38
- Chothia, 1992, One thousand fold families for the molecular biologist?, Nature (London), 357, 543, 10.1038/357543a0 · DOI
- Orengo, 1994, Protein superfamilies and domain superfolds, Nature (London), 372, 631, 10.1038/372631a0 · DOI
- Govindarajan, 1999, Estimating the total number of protein folds, J. Mol. Biol., 35, 408
- Wang, 1998, A re-estimation of the total numbers of protein folds and superfamilies, Protein Eng., 11, 621, 10.1093/protein/11.8.621 · DOI
- Gerstein, 1998, Comprehensive assessment of automatic structural alignment against a manual standard; the scop classification of proteins, Protein Sci., 7, 445, 10.1002/pro.5560070226 · DOI
- Chung, 1996, A structural explanation for the twilight zone of protein sequence homology, Structure, 4, 1123, 10.1016/S0969-2126(96)00119-0 · DOI
- Rost, 1999, Twilight zone of protein sequence alignments, Protein Eng., 12, 85, 10.1093/protein/12.2.85 · DOI · Paper page
- Brenner, 1998, Assessing sequence comparison methods with reliable structurally identified distant evolutionary relationships, Proc. Natl Acad. Sci. USA, 95, 6073, 10.1073/pnas.95.11.6073 · DOI
- Rost, 1997, Protein structures sustain evolutionary drift, Fold. Des., 2, 519, 10.1016/S1359-0278(97)00059-X · DOI
- Flores, 1993, Comparison of conformation characteristics in structurally similar protein pairs, Protein Sci., 2, 1811, 10.1002/pro.5560021104 · DOI
- Russell, 1997, Recognition of analogous and homologous protein folds: analysis of sequence and structure conservation, J. Mol. Biol., 269, 423, 10.1006/jmbi.1997.1019 · DOI
- Sauder, 2000, Large-scale comparison of protein sequence alignment algorithms with structure alignments, Proteins: Struct. Funct. Genet., 40, 6, 10.1002/(SICI)1097-0134(20000701)40:1<6::AID-PROT30>3.0.CO;2-7 · DOI
- Wood, 1999, Evolution of protein sequence and structures, J. Mol. Biol., 291, 977, 10.1006/jmbi.1999.2972 · DOI
- Gronenborn, 1991, A Novel: highly stable fold of the immunoglobulin binding domain of streptococcal protein-G, Science, 253, 657, 10.1126/science.1871600 · DOI
- Gallagher, 1994, Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR, Biochemistry, 33, 4721, 10.1021/bi00181a032 · DOI
- Wikstrom, 1994, 3-Dimensional solution structure of an immunoglobulin light chain-binding domain of protein L: comparison with the IGG binding domains of protein G, Biochemistry, 33, 14011, 10.1021/bi00251a008 · DOI
- Banner, 1987, Structure of the COL-E1 ROP protein at 1.7Å resolution, J. Mol. Biol., 196, 657, 10.1016/0022-2836(87)90039-8 · DOI
- Dalal, 1997, Protein alchemy: changing beta-sheet into alpha-helix, Nature Struct. Biol., 4, 548, 10.1038/nsb0797-548 · DOI
- Murzin, 1995, Scop: a structural classification of proteins database for the investigation of sequences and structures, J. Mol. Biol., 247, 536, 10.1016/S0022-2836(05)80134-2 · DOI
- Subbiah, 1993, Structural similarity of DNA-binding domains of bacteriophage repressors and the globin core, Curr. Biol., 3, 141, 10.1016/0960-9822(93)90255-M · DOI
- Doolittle, 1981, Similar amino acid sequences: chances or common ancestry, Science, 214, 149, 10.1126/science.7280687 · DOI
- Bernstein, 1977, The protein databank: a computer-based archival file for macromolecular structures, J. Mol. Biol., 112, 535, 10.1016/S0022-2836(77)80200-3 · DOI
- Koehl, 2002, Protein structure similarities, Curr. Opin. Struct. Biol., 11, 348, 10.1016/S0959-440X(00)00214-1 · DOI
- Lattman, 1993, Protein folding—what's the question?, Proc. Natl Acad. Sci. USA, 90, 439, 10.1073/pnas.90.2.439 · DOI
- Koehl, 1999, De novo protein design. I. In search of stability and specificity, J. Mol. Biol., 293, 1161, 10.1006/jmbi.1999.3211 · DOI
- Koehl, 1999, De novo protein design. II. Plasticity in sequence space, J. Mol. Biol., 293, 1183, 10.1006/jmbi.1999.3212 · DOI
- Altschul, 1997, Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucl. Acids Res., 25, 3389, 10.1093/nar/25.17.3389 · DOI · Paper page
- Eddy, 1996, Hidden Markov models, Curr. Opin. Struct. Biol., 6, 361, 10.1016/S0959-440X(96)80056-X · DOI
- Koehl, 2002, Protein topology and stability define the space of allowed sequences, Proc. Natl Acad. Sci. USA, 95, 1280, 10.1073/pnas.032405199 · DOI
- Lee, 1997, New optimization method for conformational energy calculations on polypeptides: conformational space annealing, J. Comp. Chem., 18, 1222, 10.1002/(SICI)1096-987X(19970715)18:9<1222::AID-JCC10>3.0.CO;2-7 · DOI
- Lee, 1999, Energy-based de novo protein folding by conformational space annealing and an off-lattice united-residue force field: application to the 10–55 fragment of staphylococcal protein A and to apo calbindin D9K, Proc. Natl Acad. Sci. USA, 96, 2025, 10.1073/pnas.96.5.2025 · DOI
- Koehl, 1994, Application of a self-consistent mean field theory to predict protein side-chains conformation and estimate their conformational entropy, J. Mol. Biol., 239, 249, 10.1006/jmbi.1994.1366 · DOI
- Koehl, 1994, Polar and non-polar atomic environment in the protein core: implications for folding and binding, Proteins: Struct. Funct. Genet., 20, 264, 10.1002/prot.340200307 · DOI
- Pande, 1997, Statistical mechanics of simple models of protein folding and design, Biophys. J., 73, 3192, 10.1016/S0006-3495(97)78345-0 · DOI
- Shakhnovich, 1993, A new approach to the design of stable proteins, Protein Eng., 6, 793, 10.1093/protein/6.8.793 · DOI
- Shakhnovich, 1993, Engineering of stable and fast-folding sequences of model proteins, Proc. Natl Acad. Sci. USA, 90, 7195, 10.1073/pnas.90.15.7195 · DOI
- Henikoff, 1992, Amino-acid substitution matrices from protein blocks, Proc. Natl Acad. Sci. USA, 89, 10915, 10.1073/pnas.89.22.10915 · DOI · Paper page
- Kraulis, 1991, MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallog., 24, 946, 10.1107/S0021889891004399 · DOI
Cited by
Sorted by citations
Yu, Y., Xu, F., Zhao, W., Thoma, C., Che, S., Richman, J. E., Jin, B., Zhu, Y., Xing, Y., Wackett, L., et al. (2024) · Science Advances · doi:10.1126/sciadv.ado2957 · Cited by 63
Metadata
- Authors
- Koehl, P., & Levitt, M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2002-10
- Volume
- 323
- Issue
- 3
- Pages
- 551-562
- ISSN
- 0022-2836
- Cited by
- 67
- References
- 3
- Language
- en
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