The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Evolution of Amino Acid Frequencies in Proteins Over Deep Time: Inferred Order of Introduction of Amino Acids into the Genetic Code
Open accessAbstract
To understand more fully how amino acid composition of proteins has changed over the course of evolution, a method has been developed for estimating the composition of proteins in an ancestral genome. Estimates are based upon the composition of conserved residues in descendant sequences and empirical knowledge of the relative probability of conservation of various amino acids. Simulations are used to model and correct for errors in the estimates. The method was used to infer the amino acid composition of a large protein set in the Last Universal Ancestor (LUA) of all extant species. Relative to the modern protein set, LUA proteins were found to be generally richer in those amino acids that are believed to have been most abundant in the prebiotic environment and poorer in those amino acids that are believed to have been unavailable or scarce. It is proposed that the inferred amino acid composition of proteins in the LUA probably reflects historical events in the establishment of the genetic code.
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
“Work on the addition of amino acids to the canonical repertoire suggest that the first amino acids used by life are also consistent with a temperate, rather than hot, origin of life (Brooks et al. 2002;Zeldovich et al. 2007;Fournier and Gogarten 2010).”
From Environmental Adaptation from the Origin of Life to the Last Universal Common Ancestor (2018) · cites this paper as Brooks et al. 2002
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
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617
The neighbor-joining method: a new method for reconstructing phylogenetic trees.
Saitou, N., & Nei, M. (1987) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a040454 · Cited by 59,959
PHYLIP-Phylogeny inference package (Version 3.2)
Felsenstein, J. (1989) · Cladistics · Cited by 17,682
The rapid generation of mutation data matrices from protein sequences
Jones, D. T., Taylor, W. R., & Thornton, J. M. (1992) · Computer applications in the biosciences · doi:10.1093/bioinformatics/8.3.275 · Cited by 7,003
Amino acid substitution matrices from protein blocks.
Henikoff, S., & Henikoff, J. G. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10915 · Cited by 6,218
Atlas of protein sequence and structure
Chang, M.-Y., Dayhoff, M. O., Eck, R. V., & Sochard, M. R. (1965) · NASA Technical Reports Server (NASA) · Cited by 4,383
A genomic perspective on protein families.
Tatusov, R., Koonin, E., & Lipman, D. (1997) · Science · doi:10.1126/science.278.5338.631 · Cited by 3,777
The SWISS-PROT protein sequence data bank and its supplement TrEMBL
Bairoch, A., & Apweiler, R. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.1.31 · Cited by 3,594
A Production of Amino Acids Under Possible Primitive Earth Conditions
Miller, S. L. (1953) · Science · doi:10.1126/science.117.3046.528 · Cited by 3,522
The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998
Bairoch, A. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.38 · Cited by 3,275
Research works printed but not linked: 1
- Dayhoff M. O., R. M. Schwartz, B. C. Orcutt, 1978 Atlas of protein sequence and structure. Vol. 5 [Suppl. 3] National Biomedical Research Foundation, Washington, D.C
Cited by
Sorted by citations
Fluorescence Lifetime Measurements and Biological Imaging
Berezin, M. Y., & Achilefu, S. (2010) · Chemical Reviews · doi:10.1021/cr900343z · Cited by 2,471
Oxidant Sensing by Reversible Disulfide Bond Formation
Cremers, C. M., & Jakob, U. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.462929 · Cited by 446
Schmidt, B., Ho, L., & Hogg, P. J. (2006) · Biochemistry · doi:10.1021/bi0603064 · Cited by 342
A universal trend of amino acid gain and loss in protein evolution
Jordan, I. K., Kondrashov, F. A., Adzhubei, I. A., Wolf, Y. I., Koonin, E. V., Kondrashov, A. S., & Sunyaev, S. (2005) · Nature · doi:10.1038/nature03306 · Cited by 297
The Triplet Code From First Principles
Trifonov, E. N. (2004) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2004.10506975 · Cited by 246
Disulfides as Redox Switches: From Molecular Mechanisms to Functional Significance
Wouters, M. A., Fan, S. W., & Haworth, N. L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2510 · Cited by 238
Gray, H. B., & Winkler, J. R. (2018) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00245 · Cited by 171
Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation
Chiu, J., & Hogg, P. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.005604 · Cited by 152
Old Yellow Enzyme-Catalysed Asymmetric Hydrogenation: Linking Family Roots with Improved Catalysis
Scholtissek, A., Tischler, D., Westphal, A. H., van Berkel, W. J. H., & Paul, C. E. (2017) · Catalysts · doi:10.3390/catal7050130 · Cited by 130
Post-Translational Control of Protein Function by Disulfide Bond Cleavage
Cook, K. M., & Hogg, P. J. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4807 · Cited by 126
Jobe, T. O., Zenzen, I., Karvansara, P. R., & Kopřiva, S. (2019) · Journal of Experimental Botany · doi:10.1093/jxb/erz250 · Cited by 119
Allosteric disulfide bonds in thrombosis and thrombolysis
Chen, V. M. Y., & Hogg, P. J. (2006) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2006.02236.x · Cited by 98
Role of aromatic amino acids in protein–nucleic acid recognition
Baker, C. M., & Grant, G. H. (2007) · Biopolymers · doi:10.1002/bip.20682 · Cited by 96
Iron-Sulfide-Bearing Chimneys as Potential Catalytic Energy Traps at Life's Emergence
Mielke, R. E., Robinson, K. J., White, L. M., McGlynn, S. E., McEachern, K., Bhartia, R., Kanik, I., & Russell, M. J. (2011) · Astrobiology · doi:10.1089/ast.2011.0667 · Cited by 99
Protein–RNA interactions: structural characteristics and hotspot amino acids
Krüger, D. M., Neubacher, S., & Grossmann, T. N. (2018) · RNA · doi:10.1261/rna.066464.118 · Cited by 88
Intrinsically Disordered Proteins: Critical Components of the Wetware
Kulkarni, P., Bhattacharya, S., Achuthan, S., Behal, A., Jolly, M. K., Kotnala, S., Mohanty, A. R., Govindan Rangarajan, C., Salgia, R., & Uversky, V. N. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00848 · Cited by 88
How much of protein sequence space has been explored by life on Earth?
Dryden, D. T. F., Thomson, A. R., & White, J. H. (2008) · Journal of The Royal Society Interface · doi:10.1098/rsif.2008.0085 · Cited by 85
“…five amino acids like those found in the Miller–Urey experiments and the Murchison meteorite (Miller et al. 1976), and that the genetic code was initially limited to these few amino acids that still predominate in proteins to the current day (e.g. Trifonov 2000; Brooks et al. 2002; Ikehara 2002).”
BackgroundIntrinsically Disordered Proteins: The Dark Horse of the Dark Proteome
Kulkarni, P., & Uversky, V. N. (2018) · PROTEOMICS · doi:10.1002/pmic.201800061 · Cited by 83
The molecular biology of selenocysteine
González-Flores, J., Shetty, S. P., Dubey, A., & Copeland, P. R. (2013) · BioMolecular Concepts · doi:10.1515/bmc-2013-0007 · Cited by 86
Fried, S. D., Fujishima, K., Makarov, M., Cherepashuk, I., & Hlouchová, K. (2022) · Journal of The Royal Society Interface · doi:10.1098/rsif.2021.0641 · Cited by 84
Search for allosteric disulfide bonds in NMR structures
Schmidt, B., & Hogg, P. J. (2007) · BMC Structural Biology · doi:10.1186/1472-6807-7-49 · Cited by 78
Tripeptide Motifs in Biology: Targets for Peptidomimetic Design
Ung, P., & Winkler, D. A. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm1012984 · Cited by 77
Sulfur metabolism and its contribution to malignancy
Ward, N. P., & DeNicola, G. M. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2019.05.001 · Cited by 74
High solubility of random-sequence proteins consisting of five kinds of primitive amino acids
Doi, N., Kakukawa, K., Oishi, Y., & Yanagawa, H. (2005) · Protein Engineering Design and Selection · doi:10.1093/protein/gzi034 · Cited by 75
Rooting the Ribosomal Tree of Life
Fournier, G. P., & Gogarten, J. P. (2010) · Molecular Biology and Evolution · doi:10.1093/molbev/msq057 · Cited by 72
Fournier, G. P., & Alm, E. J. (2015) · Journal of Molecular Evolution · doi:10.1007/s00239-015-9672-1 · Cited by 69
The evolution of Class II Aminoacyl‐tRNA synthetases and the first code
Smith, T. F., & Hartman, H. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.006 · Cited by 67
Nanobody Conjugates for Targeted Cancer Therapy and Imaging
Kang, W., Ding, C., Zheng, D., Ma, X., Yi, L., Tong, X., Wu, C., Xue, C., Yu, Y., & Zhou, Q. (2021) · Technology in Cancer Research & Treatment · doi:10.1177/15330338211010117 · Cited by 64
Lizak, C., Gerber, S., Michaud, G., Schubert, M., Fan, Y., Bucher, M., Darbre, T., Aebi, M., Reymond, J., & Locher, K. P. (2013) · Nature Communications · doi:10.1038/ncomms3627 · Cited by 61
Principles of agonist recognition in Cys-loop receptors
Lynagh, T., & Pless, S. A. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00160 · Cited by 60
Enzyme-catalyzed expressed protein ligation
Henager, S. H., Chu, N. K., Chen, Z., Bolduc, D. M., Dempsey, D. R., Hwang, Y., Wells, J. A., & Cole, P. A. (2016) · Nature Methods · doi:10.1038/nmeth.4004 · Cited by 59
Fluorescent Ribonucleoside as a FRET Acceptor for Tryptophan in Native Proteins
Xie, Y., Maxson, T., & Tor, Y. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105244t · Cited by 57
On the optimality of the genetic code, with the consideration of termination codons
Goodarzi, H., Nejad, H. A., & Torabi, N. (2004) · Biosystems · doi:10.1016/j.biosystems.2004.05.031 · Cited by 55
Environmental Adaptation from the Origin of Life to the Last Universal Common Ancestor
Cantine, M. D., & Fournier, G. P. (2018) · Origins of Life and Evolution of Biospheres · doi:10.1007/s11084-017-9542-5 · Cited by 54
Fibrinogen function achieved through multiple covalent states
Butera, D., & Hogg, P. J. (2020) · Nature Communications · doi:10.1038/s41467-020-19295-7 · Cited by 56
Dempsey, D. R., Jiang, H., Kalin, J. H., Chen, Z., & Cole, P. A. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b05098 · Cited by 54
Moore, E. K., Nunn, B. L., Goodlett, D. R., & Harvey, H. R. (2012) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2012.01.002 · Cited by 53
Functional Specificity Lies within the Properties and Evolutionary Changes of Amino Acids
Chakrabarti, S., Bryant, S. H., & Panchenko, A. R. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.08.036 · Cited by 53
Dorn, E. D., Nealson, K. H., & Adami, C. (2011) · Journal of Molecular Evolution · doi:10.1007/s00239-011-9429-4 · Cited by 52
The evolution of the genetic code: Impasses and challenges
Kun, Á., & Radványi, Á. (2017) · Biosystems · doi:10.1016/j.biosystems.2017.10.006 · Cited by 53
Sun, F.-J., & Caetano‐Anollés, G. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000018 · Cited by 51
Frozen, but no accident – why the 20 standard amino acids were selected
Doig, A. J. (2016) · FEBS Journal · doi:10.1111/febs.13982 · Cited by 52
Evolution of Life on Earth: tRNA, Aminoacyl-tRNA Synthetases and the Genetic Code
Lei, L., & Burton, Z. F. (2020) · Life · doi:10.3390/life10030021 · Cited by 53
Methionine Scanning as an NMR Tool for Detecting and Analyzing Biomolecular Interaction Surfaces
Schütz-Stoffregen, M. C., Schwer, M. M., Renschler, F. A., & Wiesner, S. (2012) · Structure · doi:10.1016/j.str.2012.02.012 · Cited by 51
The structural basis of the genetic code: amino acid recognition by aminoacyl-tRNA synthetases
Kaiser, F., Krautwurst, S., Salentin, S., Haupt, V. J., Leberecht, C., Bittrich, S., Labudde, D., & Schroeder, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-69100-0 · Cited by 47
Control of Mature Protein Function by Allosteric Disulfide Bonds
Azimi, I., Wong, J. W. H., & Hogg, P. J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3620 · Cited by 50
Cai, G., Krychiw, J. F., Myers, K. L., Fry, W. E., & Hillman, B. I. (2012) · Virology · doi:10.1016/j.virol.2012.10.012 · Cited by 45
Robustness of predictions of extremely thermally stable proteins in ancient organisms
Akanuma, S., Yokobori, S., Nakajima, Y., Bessho, M., & Yamagishi, A. (2015) · Evolution · doi:10.1111/evo.12779 · Cited by 43
A New Classification Scheme of the Genetic Code
Wilhelm, T. E., & Nikolajewa, S. (2004) · Journal of Molecular Evolution · doi:10.1007/s00239-004-2650-7 · Cited by 43
Akanuma, S. (2017) · Life · doi:10.3390/life7030033 · Cited by 42
Causes of trends in amino-acid gain and loss
Hurst, L. D., Feil, E. J., & Rocha, E. P. C. (2006) · Nature · doi:10.1038/nature05137 · Cited by 41
Sun, F.-J., & Caetano‐Anollés, G. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002799 · Cited by 39
Manipulation of enzyme properties by noncanonical amino acid incorporation
Zheng, S., & Kwon, I. (2011) · Biotechnology Journal · doi:10.1002/biot.201100267 · Cited by 37
Wehbi, S., Wheeler, A. L., Morel, B., Manepalli, N., Minh, B. Q., LAURETTA, D. S., & Masel, J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2410311121 · Cited by 36
Brooks, D. J., Fresco, J. R., & Singh, M. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth235 · Cited by 35
Self-citationSelective protein N-terminal labeling with N-hydroxysuccinimide esters
Jiang, H., D’Agostino, G. D., Cole, P. A., & Dempsey, D. R. (2020) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2020.04.018 · Cited by 31
Enzymic recognition of amino acids drove the evolution of primordial genetic codes
Douglas, J., Bouckaert, R., Carter, C. W., & Wills, P. R. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1160 · Cited by 30
Food protein-derived anxiolytic peptides: their potential role in anxiety management
Hafeez, Z., Benoit, S., Cakir‐Kiefer, C., Dary, A., & Miclo, L. (2020) · Food & Function · doi:10.1039/d0fo02432e · Cited by 29
Rogers, S. O. (2019) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2019.01.022 · Cited by 28
Large Scale Chemical Cross-linking Mass Spectrometry Perspectives
Zybailov, B. L. (2013) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.s2-001 · Cited by 28
Jacques Demongeot, A., & Seligmann, H. (2019) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2019.03.024 · Cited by 27
The RING Domain of RING Finger 12 Efficiently Builds Degradative Ubiquitin Chains
Middleton, A. J., Zhu, J., & Day, C. L. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.05.001 · Cited by 27
Prebiotic protein design supports a halophile origin of foldable proteins
Longo, L. M., & Blaber, M. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2013.00418 · Cited by 27
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1
Abraham, S. J., Cheng, R. C. K., Chew, T. A., Khantwal, C. M., Liu, C. W., Gong, S., Nakamoto, R. K., & Maduke, M. C. (2015) · Journal of Biomolecular NMR · doi:10.1007/s10858-015-9898-7 · Cited by 27
Methods for identifying and characterizing interactions involving RNA
Blakeley, B. D., DePorter, S. M., Mohan, U., Burai, R., Tolbert, B. S., & McNaughton, B. R. (2012) · Tetrahedron · doi:10.1016/j.tet.2012.07.001 · Cited by 26
PPK1 and PPK2 — which polyphosphate kinase is older?
Achbergerová, L., & Nahálka, J. (2014) · Biologia · doi:10.2478/s11756-013-0324-x · Cited by 26
Chirality in the RNA world and beyond
Sandars, P. G. H. (2005) · International Journal of Astrobiology · doi:10.1017/s1473550405002442 · Cited by 26
Structural and functional analysis of “non-smelly” proteins
Yan, J. R., Cheng, J., Kurgan, L., & Uversky, V. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03292-1 · Cited by 26
Evolution of initiator tRNAs and selection of methionine as the initiating amino acid
Bhattacharyya, S., & Varshney, U. (2016) · RNA Biology · doi:10.1080/15476286.2016.1195943 · Cited by 26
Understanding Photochirogenesis: Solvent Effects on Circular Dichroism and Anisotropy Spectroscopy
Bredehöft, J. H., Jones, N. C., Meinert, C., Evans, A. C., Hoffmann, S. V., & Meierhenrich, U. J. (2014) · Chirality · doi:10.1002/chir.22329 · Cited by 29
Codon usage and amino acid usage influence genes expression level
Paul, P., Malakar, A. K., & Chakraborty, S. (2017) · Genetica · doi:10.1007/s10709-017-9996-4 · Cited by 25
The rise and fall of deleterious mutation
Balbi, K. J., & Feil, E. J. (2007) · Research in Microbiology · doi:10.1016/j.resmic.2007.09.005 · Cited by 24
Cloning and functional expression of the first eukaryotic Na+–tryptophan symporter, AgNAT6
Meleshkevitch, E., Robinson, M., Popova, L. B., Miller, M. M., Harvey, W., & Boudko, D. (2009) · Journal of Experimental Biology · doi:10.1242/jeb.027383 · Cited by 25
Flexible Proteins at the Origin of Life
Pohorille, A., Wilson, M. A., & Shannon, G. (2017) · Life · doi:10.3390/life7020023 · Cited by 25
Solis, A. D. (2019) · BMC Evolutionary Biology · doi:10.1186/s12862-019-1464-6 · Cited by 25
Jiang, H., & Cole, P. A. (2021) · Current Protocols · doi:10.1002/cpz1.14 · Cited by 23
Histidine-Specific Bioconjugation for Single-Molecule Force Spectroscopy
Lei, H., Zhang, J., Li, Y., Wang, X., Qin, M., Wang, W., & Cao, Y. (2022) · ACS Nano · doi:10.1021/acsnano.2c07298 · Cited by 22
Aamodt, R. M. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2008.07.002 · Cited by 22
Tsuji, J., Nydza, R., Wolcott, E., Mannor, E., Moran, B., Hesson, G., Arvidson, T., Howe, K., Hayes, R., Ramirez, M., et al. (2010) · BIOS · doi:10.1893/011.081.0103 · Cited by 22
Kimura, M., & Akanuma, S. (2020) · Journal of Molecular Evolution · doi:10.1007/s00239-020-09938-0 · Cited by 23
Nanobody-based food allergen surveillance: current status and prospects
Wang, Y., Wu, S., Li, A., Lv, H., Ji, X., Hu, Y., & Wang, S. (2024) · Food Quality and Safety · doi:10.1093/fqsafe/fyae018 · Cited by 21
Genome wide exploration of the origin and evolution of amino acids
Liu, X., Zhang, J., Ni, F., Xu, D., Han, B., Han, D., Ji, Z., & Zhao, Y. (2010) · BMC Evolutionary Biology · doi:10.1186/1471-2148-10-77 · Cited by 22
Goodarzi, H., Najafabadi, H. S., Hassani, K., Nejad, H. A., & Torabi, N. (2005) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2005.01.012 · Cited by 21
GC content of vertebrate exome landscapes reveal areas of accelerated protein evolution
Huttener, R., Thorrez, L., Veld, T. I., Granvik, M., Snoeck, L., Lommel, L. V., & Schuit, F. C. (2019) · BMC Evolutionary Biology · doi:10.1186/s12862-019-1469-1 · Cited by 19
Pathogenic perspective of missense mutations of ORF3a protein of SARS-CoV-2
Hassan, S. S., Attrish, D., Ghosh, S., Choudhury, P. P., & Roy, B. (2021) · Virus Research · doi:10.1016/j.virusres.2021.198441 · Cited by 19
Vishnoi, A., Sethupathy, P., Simola, D. F., Plotkin, J. B., & Hannenhalli, S. S. (2011) · Molecular Biology and Evolution · doi:10.1093/molbev/msr085 · Cited by 22
Riedesel, H., Kolbeck, B., Schmetzer, O., & Knapp, E. (2004) · PubMed · Cited by 18
Transfer RNA and the Origins of Diversified Life
Sun, F.-J., & Caetano‐Anollés, G. (2008) · Science Progress · doi:10.3184/003685008x360650 · Cited by 18
Brooks, D. J., & Fresco, J. R. (2003) · Gene · doi:10.1016/s0378-1119(02)01176-9 · Cited by 17
Self-citationAnalysis of Site-Specific Histidine Protonation in Human Prolactin,
Tettamanzi, M. C., Keeler, C., Meshack, S., & Hodsdon, M. E. (2008) · Biochemistry · doi:10.1021/bi800444t · Cited by 16
Chiroptical properties of diamino carboxylic acids
Bredehöft, J. H., Breme, K., Meierhenrich, U. J., Hoffmann, S. V., & Thiemann, W. (2007) · Chirality · doi:10.1002/chir.20422 · Cited by 16
Structure-oriented bioinformatic approach exploring histidine-rich clusters in proteins
Cun, S., Lai, Y., Chang, Y., & Sun, H. (2013) · Metallomics · doi:10.1039/c3mt00026e · Cited by 16
Hershko, K., Simhadri, V. L., Blaisdell, A., Hunt, R., Newell, J. M., Tseng, S. C., Hershko, A. Y., Choi, J. W., Sauna, Z. E., Wu, A., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.383968 · Cited by 15
Bohórquez, H. J., Suárez, C. F., & Patarroyo, M. E. (2017) · Scientific Reports · doi:10.1038/s41598-017-08041-7 · Cited by 15
Chiarabelli, C., & Luisi, P. L. (2014) · Science Progress · doi:10.3184/003685014x13921159313230 · Cited by 15
Rigorous estimation of post-translational proteasomal splicing in the immunopeptidomePreprint
Cygan, K. J., Khaledian, E., Blumenberg, L. M., Salzler, R. R., Shah, D., Olson, W. C., Macdonald, L. E., Murphy, A. J., & Dhanik, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.26.445792 · Cited by 15
Unevolved De Novo Proteins Have Innate Tendencies to Bind Transition Metals
Wang, M. S., Hoegler, K. J., & Hecht, M. H. (2019) · Life · doi:10.3390/life9010008 · Cited by 14
Conformational characterization of disulfide bonds: A tool for protein classification
Marques, J. R. F., da Fonseca, R. R., Drury, B., & Melo, A. (2010) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2010.09.012 · Cited by 15
A hybrid FLIM-elastic net platform for label free profiling of breast cancer
Damayanti, N. P., Craig, A. P., & Irudayaraj, J. (2013) · The Analyst · doi:10.1039/c3an01097j · Cited by 14
Contribution of individual histidines to the global stability of human prolactin
Keeler, C., Tettamanzi, M. C., Meshack, S., & Hodsdon, M. E. (2009) · Protein Science · doi:10.1002/pro.100 · Cited by 14
Metadata
- Authors
- Brooks, D. J., Fresco, J. R., Lesk, A. M., & Singh, M.
- Affiliations
- Princeton University (US)
- Venue
- Molecular Biology and Evolution
- Publisher
- Oxford University Press (OUP)
- Published
- 2002-10-01
- Volume
- 19
- Issue
- 10
- Pages
- 1645-1655
- ISSN
- 0737-4038 (ISSN-L)
- 1537-1719
- OpenAlex
- W2079704642
- Cited by
- 192
- References
- 35
- Citations by year
- 2026: 9 · 2025: 8 · 2024: 7 · 2023: 10 · 2022: 7 · 2021: 10 · 2020: 11 · 2019: 15 · 2018: 6 · 2017: 10 · 2016: 7 · 2015: 4 · 2014: 6 · 2013: 8 · 2012: 12
- FWCI
- 2.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Biology and Evolution (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (9972930, 0093399)
- U.S. Department of Defense
- Wellcome Trust
- National Institutes of Health
- National Institute of General Medical Sciences (T32GM007388, 2T32GM07388-22)
- U.S. Army Medical Command
- Topics
- Physical Sciences › Physics and Astronomy › Astronomy and Astrophysics › Origins and Evolution of Life
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
- Keywords
- amino acid composition, protein evolution, origin of the genetic code, ancestral genome reconstruction, conserved residues, prebiotic amino acids, amino acid availability
- MeSH terms
- Amino Acid Sequence, Amino Acids, Computer Simulation, Genetic Code, Models, Genetic, Probability, Proteins, Time Factors, Conserved Sequence, Evolution, Molecular, Amino Acid Substitution
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