Sequence and structural differences between enzyme and nonenzyme homologs.
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Janet M Thornton | Annabel E. Todd | Christine A Orengo | C. Orengo | J. Thornton | A. Todd | Annabel E Todd
[1] Thomas L. Madden,et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. , 1997, Nucleic acids research.
[2] A. Valencia,et al. Practical limits of function prediction , 2000, Proteins.
[3] A. Subramanian,et al. Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene. , 2000, The Journal of biological chemistry.
[4] A. McCoy,et al. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. , 1998, Journal of molecular biology.
[5] C. Hill,et al. Structural basis for the activation of 20S proteasomes by 11S regulators , 2000, Nature.
[6] James C. Sacchettini,et al. Crystal structure of a plant catechol oxidase containing a dicopper center , 1998, Nature Structural Biology.
[7] K. Brew,et al. The complete amino acid sequence of bovine α-lactalbumin. , 1970 .
[8] Ping Zhou,et al. Crystal structures of [18]aneN6H2K[Co(CN)6].4H2O, [16]aneN4H2K[Co(CN)6] and [12]aneN4H3[Co(CN)6].2H2O. Insight into the electrostatic and hydrogen-bonding interaction in self-assembling supercomplexes , 1999 .
[9] Michael Y. Galperin,et al. A diverse superfamily of enzymes with ATP‐dependent carboxylate—amine/thiol ligase activity , 1997, Protein science : a publication of the Protein Society.
[10] M. Beltramini,et al. The o‐diphenol oxidase activity of arthropod hemocyanin , 1996, FEBS letters.
[11] H. Nam,et al. Crystal Structure of the Tandem Phosphatase Domains of RPTP LAR , 1999, Cell.
[12] M. Nilges,et al. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules , 1997, Current Biology.
[13] W R Taylor,et al. Protein structure alignment. , 1989, Journal of molecular biology.
[14] A G Murzin,et al. Structural classification of proteins: new superfamilies. , 1996, Current opinion in structural biology.
[15] J. Bolin,et al. Crystal Structure of the Biphenyl-Cleaving Extradiol Dioxygenase from a PCB-Degrading Pseudomonad , 1995, Science.
[16] J. Lipscomb,et al. Roles of the methane monooxygenase reductase component in the regulation of catalysis. , 1997, Biochemistry.
[17] Helen M. Kent,et al. The 1.6 Å Resolution Crystal Structure of Nuclear Transport Factor 2 (NTF2) , 1996 .
[18] Michael G. Rossmann,et al. Chemical and biological evolution of a nucleotide-binding protein , 1974, Nature.
[19] J. Tainer,et al. Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex , 1999, Nature Structural Biology.
[20] David C. Jones,et al. CATH--a hierarchic classification of protein domain structures. , 1997, Structure.
[21] A. Fisher,et al. Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 A resolution. , 1995, Biochemistry.
[22] H. Beinert,et al. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[23] S. Mande,et al. Conserved structural features and sequence patterns in the GroES fold family. , 1999, Protein engineering.
[24] N. Patel,et al. Drosophila neurotactin, a surface glycoprotein with homology to serine esterases, is dynamically expressed during embryogenesis. , 1990, Development.
[25] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[26] D T Gibson,et al. Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase. , 1998, Structure.
[27] T. N. Bhat,et al. The Protein Data Bank , 2000, Nucleic Acids Res..
[28] K. Brew,et al. The Complete Amino‐Acid Sequence of Human α‐Lactalbumin , 1972 .
[29] R. Wolfenden,et al. Cytidine deaminase. The 2.3 A crystal structure of an enzyme: transition-state analog complex. , 1994, Journal of molecular biology.
[30] R. Jensen. Enzyme recruitment in evolution of new function. , 1976, Annual review of microbiology.
[31] Rolf Apweiler,et al. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000 , 2000, Nucleic Acids Res..
[32] Patricia C. Babbitt,et al. Understanding Enzyme Superfamilies , 1997, The Journal of Biological Chemistry.
[33] D W Rice,et al. Determinants of substrate specificity in the superfamily of amino acid dehydrogenases. , 1997, Biochemistry.
[34] P C Babbitt,et al. Mechanistically diverse enzyme superfamilies: the importance of chemistry in the evolution of catalysis. , 1998, Current opinion in chemical biology.
[35] A G Murzin,et al. SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.
[36] R. Huber,et al. A gated channel into the proteasome core particle , 2000, Nature Structural Biology.
[37] P. Kraulis. A program to produce both detailed and schematic plots of protein structures , 1991 .
[38] S. Maloy,et al. PutA protein, a membrane-associated flavin dehydrogenase, acts as a redox-dependent transcriptional regulator. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[39] G. H. Reed,et al. The enolase superfamily: a general strategy for enzyme-catalyzed abstraction of the alpha-protons of carboxylic acids. , 1996, Biochemistry.
[40] A D Cameron,et al. All in the family: Structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly , 1998, Protein science : a publication of the Protein Society.
[41] C. Betzel,et al. Modulation of phospholipase A2 activity generated by molecular evolution , 1999, Cellular and Molecular Life Sciences CMLS.
[42] J. Piatigorsky,et al. Recruitment of enzymes as lens structural proteins. , 1987, Science.
[43] E. Koonin,et al. Eukaryotic transcription regulators derive from ancient enzymatic domains , 1998, Current Biology.
[44] M. Bolognesi,et al. The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families. , 2000, Journal of molecular biology.
[45] Annabel E. Todd,et al. Evolution of function in protein superfamilies, from a structural perspective. , 2001, Journal of molecular biology.
[46] Joel L. Sussman,et al. The α/β hydrolase fold , 1992 .
[47] P. Leadlay,et al. How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution. , 1996, Structure.
[48] A. Okamoto,et al. Redesigning the Substrate Specificity of an Enzyme by Cumulative Effects of the Mutations of Non-active Site Residues* , 1999, The Journal of Biological Chemistry.
[49] N. Grishin,et al. Mh1 domain of Smad is a degraded homing endonuclease. , 2001, Journal of molecular biology.
[50] A. Yoshimura,et al. Angiogenic factor , 1992, Nature.
[51] D. Cove. Evolutionary significance of autogenous regulation , 1974, Nature.
[52] C. Chothia. One thousand families for the molecular biologist , 1992, Nature.
[53] D. Herschlag,et al. Catalytic promiscuity and the evolution of new enzymatic activities. , 1999, Chemistry & biology.
[54] N. Rawlings,et al. Structure of membrane glutamate carboxypeptidase. , 1997, Biochimica et biophysica acta.
[55] A. Dunker,et al. Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum , 1998, Nature Structural Biology.
[56] C Sander,et al. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease , 1997, Proteins.
[57] B Henrissat,et al. A classification of glycosyl hydrolases based on amino acid sequence similarities. , 1991, The Biochemical journal.
[58] M. Delarue,et al. Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus , 1995, Nature Structural Biology.
[59] B. Fox,et al. Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction. , 1991, The Journal of biological chemistry.
[60] M. Perbandt,et al. Crystal structure of vipoxin at 2.0 Å: an example of regulation of a toxic function generated by molecular evolution , 1997, FEBS letters.
[61] I. Charles,et al. The pre-chorismate (shikimate) and quinate pathways in filamentous fungi: theoretical and practical aspects. , 1993, Journal of general microbiology.
[62] E. Koonin,et al. Peptide-N-glycanases and DNA repair proteins, Xp-C/Rad4, are, respectively, active and inactivated enzymes sharing a common transglutaminase fold. , 2001, Human molecular genetics.
[63] B. Henrissat,et al. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[64] G. Petsko,et al. On the origin of enzymatic species. , 1993, Trends in biochemical sciences.
[65] H J Fromm,et al. Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation. , 2000, Journal of molecular biology.
[66] W. W. Jong,et al. The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses , 1987, Nature.
[67] James E. Bray,et al. A rapid classification protocol for the CATH Domain Database to support structural genomics , 2001, Nucleic Acids Res..
[68] M. Gerstein,et al. The relationship between protein structure and function: a comprehensive survey with application to the yeast genome. , 1999, Journal of molecular biology.
[69] Z. Dauter,et al. Crystal structure of narbonin at 1.8 A resolution. , 1995, Acta crystallographica. Section D, Biological crystallography.
[70] P. Howell,et al. Crystal structure of an inactive duck delta II crystallin mutant with bound argininosuccinate. , 1999, Biochemistry.
[71] K. Aktories,et al. The N-Terminal Part of the Enzyme Component (C2I) of the BinaryClostridium botulinum C2 Toxin Interacts with the Binding Component C2II and Functions as a Carrier System for a Rho ADP-Ribosylating C3-Like Fusion Toxin , 1998, Infection and Immunity.
[72] N.,et al. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. , 1990, The Journal of biological chemistry.
[73] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1978, Archives of biochemistry and biophysics.
[74] J. Kastrup,et al. Structure of HBP, a multifunctional protein with a serine proteinase fold , 1997, Nature Structural Biology.
[75] M. Rossmann,et al. Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion , 1991, Nature.
[76] A. Murzin. How far divergent evolution goes in proteins. , 1998, Current opinion in structural biology.
[77] D. Barford,et al. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. , 1995, Science.
[78] T. Blundell,et al. Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site , 1992, Nature.
[79] E. Koonin,et al. Adaptations of the helix‐grip fold for ligand binding and catalysis in the START domain superfamily , 2001, Proteins.
[80] H. Saito,et al. Distinct functional roles of the two intracellular phosphatase like domains of the receptor‐linked protein tyrosine phosphatases LCA and LAR. , 1990, The EMBO journal.
[81] M. Hennig,et al. Crystal structure of concanavalin B at 1.65 A resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis. , 1995, Journal of molecular biology.
[82] S. Rhee,et al. Structural homology between MarA of the AraC family of transcriptional activators and the integrase family of site-specific recombinases. , 2000, Molecular microbiology.
[83] Two tricks in one bundle: helix-turn-helix gains enzymatic activity. , 2000, Nucleic acids research.
[84] C. Betzel,et al. A TIM barrel protein without enzymatic activity? Crystal‐structure of narbonin at 1.8 Å resolution , 1992, FEBS letters.