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Volumn 36, Issue 2, 2009, Pages 235-249

Searching distant homologs of the regulatory ACT domain in phenylalanine hydroxylase

Author keywords

ACT domain; Aromatic amino acid hydroxylases; Phenylalanine hydroxylase; Sequence divergence; Structural homology

Indexed keywords

30S PROTEIN S6; ACETOACETATE SYNTHASE III SMALL SUBUNIT; ACYLPHOSPHATASE; ADENOSINE TRIPHOSPHATE PHOSPHORIBOSYLTRANSFERASE; ASPARTATE KINASE; BACTERIAL ENZYME; DEXTRO RIBOSE 5 PHOSPHATE ISOMERASE; FUNGAL ENZYME; GLYCINE CLEAVAGE SYSTEM TRANSCRIPTIONAL REPRESSOR; METALLOCHAPERONE; NICKEL RESPONSIVE REGULATOR PROTEIN; NITROGEN REGULATORY PROTEIN P II 2; PERIPLASMIC DIVALENT CATION TOLERANCE PROTEIN; PHENYLALANINE 4 MONOOXYGENASE; PHOSPHOGLYCERATE DEHYDROGENASE; PII LIKE SIGNALING PROTEIN; PIIB PROTEIN; PREPHENATE DEHYDRATASE; PROTEIN S6; SGUF1 PROTEIN; SGUF2 PROTEIN; SGUF3 PROTEIN; SGUF4 PROTEIN; SGUF5 PROTEIN; SMALL CONDUCTANCE MECHANOSENSITIVE CHANNEL; THREONINE DEHYDRATASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; YBED PROTEIN; YKOF PROTEIN;

EID: 59449085226     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-008-0057-2     Document Type: Article
Times cited : (17)

References (75)
  • 2
    • 0035853296 scopus 로고    scopus 로고
    • Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains
    • V Anantharaman EV Koonin L Aravind 2001 Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains J Mol Biol 307 1271 1292
    • (2001) J Mol Biol , vol.307 , pp. 1271-1292
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 3
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • L Aravind EV Koonin 1999 Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches J Mol Biol 287 1023 1040
    • (1999) J Mol Biol , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 5
    • 0036431502 scopus 로고    scopus 로고
    • A new zinc-protein coordination site in intracellular metal trafficking: Solution structure of the Apo and Zn(II) forms of ZntA(46-118)
    • L Banci I Bertini S Ciofi-Baffoni LA Finney CE Outten TV O'Halloran 2002 A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118) J Mol Biol 323 883 897
    • (2002) J Mol Biol , vol.323 , pp. 883-897
    • Banci, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    Finney, L.A.4    Outten, C.E.5    O'Halloran, T.V.6
  • 6
    • 2242431668 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel
    • RB Bass P Strop M Barclay DC Rees 2002 Crystal structure of Escherichia coli MscS, a voltage-modulated and mechanosensitive channel Science 298 1582 1587
    • (2002) Science , vol.298 , pp. 1582-1587
    • Bass, R.B.1    Strop, P.2    Barclay, M.3    Rees, D.C.4
  • 8
    • 1642348278 scopus 로고    scopus 로고
    • Multiconformational states in phosphoglycerate dehydrogenase
    • JK Bell GA Grant LJ Banaszak 2004 Multiconformational states in phosphoglycerate dehydrogenase Biochemistry 43 3450 3458
    • (2004) Biochemistry , vol.43 , pp. 3450-3458
    • Bell, J.K.1    Grant, G.A.2    Banaszak, L.J.3
  • 10
    • 0033934642 scopus 로고    scopus 로고
    • Proteobacterial histidine-biosynthetic pathways are paraphyletic
    • JP Bond C Francklyn 2000 Proteobacterial histidine-biosynthetic pathways are paraphyletic J Mol Evol 50 339 347
    • (2000) J Mol Evol , vol.50 , pp. 339-347
    • Bond, J.P.1    Francklyn, C.2
  • 12
    • 17144395996 scopus 로고    scopus 로고
    • Structure of Pyrococcus horikoshii NikR: Nickel sensing and implications for the regulation of DNA recognition
    • PT Chivers TH Tahirov 2005 Structure of Pyrococcus horikoshii NikR: nickel sensing and implications for the regulation of DNA recognition J Mol Biol 348 597 607
    • (2005) J Mol Biol , vol.348 , pp. 597-607
    • Chivers, P.T.1    Tahirov, T.H.2
  • 13
    • 0037424269 scopus 로고    scopus 로고
    • Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis
    • Y Cho V Sharma JC Sacchettini 2003 Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis J Biol Chem 278 8333 8339
    • (2003) J Biol Chem , vol.278 , pp. 8333-8339
    • Cho, Y.1    Sharma, V.2    Sacchettini, J.C.3
  • 17
    • 17644385239 scopus 로고    scopus 로고
    • Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: Extreme asymmetry in a tetramer of identical subunits
    • S Dey GA Grant JC Sacchettini 2005 Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits J Biol Chem 280 14892 14899
    • (2005) J Biol Chem , vol.280 , pp. 14892-14899
    • Dey, S.1    Grant, G.A.2    Sacchettini, J.C.3
  • 18
    • 12144279605 scopus 로고    scopus 로고
    • Crystal structure of yeast V-ATPase subunit C reveals its stator function
    • O Drory F Frolow N Nelson 2004 Crystal structure of yeast V-ATPase subunit C reveals its stator function EMBO Rep 5 1148 1152
    • (2004) EMBO Rep , vol.5 , pp. 1148-1152
    • Drory, O.1    Frolow, F.2    Nelson, N.3
  • 19
    • 0037020177 scopus 로고    scopus 로고
    • A novel ligand-binding domain involved in regulation of amino acid metabolism in prokaryotes
    • TJ Ettema AB Brinkman TH Tani JB Rafferty J Van Der Oost 2002 A novel ligand-binding domain involved in regulation of amino acid metabolism in prokaryotes J Biol Chem 277 37464 37468
    • (2002) J Biol Chem , vol.277 , pp. 37464-37468
    • Ettema, T.J.1    Brinkman, A.B.2    Tani, T.H.3    Rafferty, J.B.4    Van Der Oost, J.5
  • 20
    • 0000122573 scopus 로고
    • PHYLIP: Phylogeny inference package (Version 3.2)
    • J Felsenstein 1989 PHYLIP: phylogeny inference package (Version 3.2) Cladistics 5 164 166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 21
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of aromatic amino acid hydroxylation
    • PF Fitzpatrick 2003 Mechanism of aromatic amino acid hydroxylation Biochemistry 42 14083 14091
    • (2003) Biochemistry , vol.42 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 22
    • 0001749787 scopus 로고    scopus 로고
    • Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms
    • T Flatmark RC Stevens 1999 Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms Chem Rev 99 2137 2160
    • (1999) Chem Rev , vol.99 , pp. 2137-2160
    • Flatmark, T.1    Stevens, R.C.2
  • 24
    • 0035012982 scopus 로고    scopus 로고
    • STRAP: Editor for STRuctural Alignments of Proteins
    • C Gille C Frommel 2001 STRAP: editor for STRuctural Alignments of Proteins Bioinformatics 17 377 378
    • (2001) Bioinformatics , vol.17 , pp. 377-378
    • Gille, C.1    Frommel, C.2
  • 25
    • 0034981940 scopus 로고    scopus 로고
    • Missense mutations in the N-terminal domain of human phenylalanine hydroxylase interfere with binding of regulatory phenylalanine
    • T Gjetting M Petersen P Guldberg F Guttler 2001 Missense mutations in the N-terminal domain of human phenylalanine hydroxylase interfere with binding of regulatory phenylalanine Am J Hum Genet 68 1353 1360
    • (2001) Am J Hum Genet , vol.68 , pp. 1353-1360
    • Gjetting, T.1    Petersen, M.2    Guldberg, P.3    Guttler, F.4
  • 26
    • 33845944628 scopus 로고    scopus 로고
    • The ACT domain: A small molecule binding domain and its role as a common regulatory element
    • GA Grant 2006 The ACT domain: a small molecule binding domain and its role as a common regulatory element J Biol Chem 281 33825 33829
    • (2006) J Biol Chem , vol.281 , pp. 33825-33829
    • Grant, G.A.1
  • 27
    • 0036067792 scopus 로고    scopus 로고
    • Glycine binds the transcriptional accessory protein GcvR to disrupt a GcvA/GcvR interaction and allow GcvA-mediated activation of the Escherichia coli gcvTHP operon
    • G Heil LT Stauffer GV Stauffer 2002 Glycine binds the transcriptional accessory protein GcvR to disrupt a GcvA/GcvR interaction and allow GcvA-mediated activation of the Escherichia coli gcvTHP operon Microbiology 148 2203 2214
    • (2002) Microbiology , vol.148 , pp. 2203-2214
    • Heil, G.1    Stauffer, L.T.2    Stauffer, G.V.3
  • 29
    • 0029051027 scopus 로고
    • The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP
    • ES Kamberov MR Atkinson AJ Ninfa 1995 The Escherichia coli PII signal transduction protein is activated upon binding 2-ketoglutarate and ATP J Biol Chem 270 17797 17807
    • (1995) J Biol Chem , vol.270 , pp. 17797-17807
    • Kamberov, E.S.1    Atkinson, M.R.2    Ninfa, A.J.3
  • 31
    • 29144518532 scopus 로고    scopus 로고
    • The ubiquitin domain superfold: Structure-based sequence alignments and characterization of binding epitopes
    • C Kiel L Serrano 2006 The ubiquitin domain superfold: structure-based sequence alignments and characterization of binding epitopes J Mol Biol 355 821 844
    • (2006) J Mol Biol , vol.355 , pp. 821-844
    • Kiel, C.1    Serrano, L.2
  • 34
    • 9244251544 scopus 로고    scopus 로고
    • Structural similarity of YbeD protein from Escherichia coli to allosteric regulatory domains
    • G Kozlov D Elias A Semesi A Yee M Cygler K Gehring 2004 Structural similarity of YbeD protein from Escherichia coli to allosteric regulatory domains J Bacteriol 186 8083 8088
    • (2004) J Bacteriol , vol.186 , pp. 8083-8088
    • Kozlov, G.1    Elias, D.2    Semesi, A.3    Yee, A.4    Cygler, M.5    Gehring, K.6
  • 35
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • AL Lamb AS Torres TV O'Halloran AC Rosenzweig 2001 Heterodimeric structure of superoxide dismutase in complex with its metallochaperone Nat Struct Biol 8 751 755
    • (2001) Nat Struct Biol , vol.8 , pp. 751-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 37
    • 15244344475 scopus 로고    scopus 로고
    • Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism
    • JS Liberles M Thorolfsson A Martinez 2005 Allosteric mechanisms in ACT domain containing enzymes involved in amino acid metabolism Amino Acids 28 1 12
    • (2005) Amino Acids , vol.28 , pp. 1-12
    • Liberles, J.S.1    Thorolfsson, M.2    Martinez, A.3
  • 39
    • 0027397303 scopus 로고
    • The cooperative binding of phenylalanine to phenylalanine 4-monooxygenase studied by 1H-NMR paramagnetic relaxation: Changes in water accessibility to the iron at the active site upon substrate binding
    • A Martinez S Olafsdottir T Flatmark 1993 The cooperative binding of phenylalanine to phenylalanine 4-monooxygenase studied by 1H-NMR paramagnetic relaxation: changes in water accessibility to the iron at the active site upon substrate binding Eur J Biochem 211 259 266
    • (1993) Eur J Biochem , vol.211 , pp. 259-266
    • Martinez, A.1    Olafsdottir, S.2    Flatmark, T.3
  • 40
    • 33745803816 scopus 로고    scopus 로고
    • A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase
    • C Mas-Droux G Curien M Robert-Genthon M Laurencin JL Ferrer R Dumas 2006 A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase Plant Cell 18 1681 1692
    • (2006) Plant Cell , vol.18 , pp. 1681-1692
    • Mas-Droux, C.1    Curien, G.2    Robert-Genthon, M.3    Laurencin, M.4    Ferrer, J.L.5    Dumas, R.6
  • 41
    • 0031571090 scopus 로고    scopus 로고
    • Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: The shape of the active-site cavity controls substrate specificity
    • A Mattevi MW Fraaije A Mozzarelli L Olivi A Coda WJ van Berkel 1997 Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity Structure 5 907 920
    • (1997) Structure , vol.5 , pp. 907-920
    • Mattevi, A.1    Fraaije, M.W.2    Mozzarelli, A.3    Olivi, L.4    Coda, A.5    Van Berkel, W.J.6
  • 42
    • 0035957514 scopus 로고    scopus 로고
    • Evolutionary conservation of the folding nucleus
    • L Mirny E Shakhnovich 2001 Evolutionary conservation of the folding nucleus J Mol Biol 308 123 129
    • (2001) J Mol Biol , vol.308 , pp. 123-129
    • Mirny, L.1    Shakhnovich, E.2
  • 43
    • 24344505390 scopus 로고    scopus 로고
    • Crystal structure and structural stability of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3
    • K Miyazono Y Sawano M Tanokura 2005 Crystal structure and structural stability of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3 Proteins 61 196 205
    • (2005) Proteins , vol.61 , pp. 196-205
    • Miyazono, K.1    Sawano, Y.2    Tanokura, M.3
  • 44
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • AG Murzin SE Brenner T Hubbard C Chothia 1995 SCOP: a structural classification of proteins database for the investigation of sequences and structures J Mol Biol 247 536 540
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 45
    • 33751411136 scopus 로고    scopus 로고
    • Folding of S6 structures with divergent amino acid composition: Pathway flexibility within partly overlapping foldons
    • M Olofsson S Hansson L Hedberg DT Logan M Oliveberg 2007 Folding of S6 structures with divergent amino acid composition: pathway flexibility within partly overlapping foldons J Mol Biol 365 237 248
    • (2007) J Mol Biol , vol.365 , pp. 237-248
    • Olofsson, M.1    Hansson, S.2    Hedberg, L.3    Logan, D.T.4    Oliveberg, M.5
  • 46
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution: A structural perspective
    • CA Orengo JM Thornton 2005 Protein families and their evolution: a structural perspective Annu Rev Biochem 74 867 900
    • (2005) Annu Rev Biochem , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 47
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • CA Orengo DT Jones JM Thornton 1994 Protein superfamilies and domain superfolds Nature 372 631 634
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 49
    • 0034730203 scopus 로고    scopus 로고
    • Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assembly
    • DE Otzen O Kristensen M Oliveberg 2000 Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly Proc Natl Acad Sci USA 97 9907 9912
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9907-9912
    • Otzen, D.E.1    Kristensen, O.2    Oliveberg, M.3
  • 50
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: An application to display phylogenetic trees on personal computers
    • RDM Page 1996 TREEVIEW: an application to display phylogenetic trees on personal computers Comput Appl Biosci 12 357 358
    • (1996) Comput Appl Biosci , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 53
  • 55
    • 0033592422 scopus 로고    scopus 로고
    • Regulation of phenylalanine biosynthesis: Studies on the mechanism of phenylalanine binding and feedback inhibition in the Escherichia coli P-protein
    • G Pohnert S Zhang A Husain DB Wilson B Ganem 1999 Regulation of phenylalanine biosynthesis: studies on the mechanism of phenylalanine binding and feedback inhibition in the Escherichia coli P-protein Biochemistry 38 12212 12217
    • (1999) Biochemistry , vol.38 , pp. 12212-12217
    • Pohnert, G.1    Zhang, S.2    Husain, A.3    Wilson, D.B.4    Ganem, B.5
  • 56
    • 11344272919 scopus 로고    scopus 로고
    • Structural classification of thioredoxin-like fold proteins
    • Y Qi NV Grishin 2005 Structural classification of thioredoxin-like fold proteins Proteins 58 376 388
    • (2005) Proteins , vol.58 , pp. 376-388
    • Qi, Y.1    Grishin, N.V.2
  • 57
    • 0036382641 scopus 로고    scopus 로고
    • Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain
    • C Rosano S Zuccotti M Bucciantini M Stefani G Ramponi M Bolognesi 2002 Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain J Mol Biol 321 785 796
    • (2002) J Mol Biol , vol.321 , pp. 785-796
    • Rosano, C.1    Zuccotti, S.2    Bucciantini, M.3    Stefani, M.4    Ramponi, G.5    Bolognesi, M.6
  • 60
    • 0028951187 scopus 로고
    • The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase
    • DJ Schuller GA Grant LJ Banaszak 1995 The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase Nat Struct Biol 2 69 76
    • (1995) Nat Struct Biol , vol.2 , pp. 69-76
    • Schuller, D.J.1    Grant, G.A.2    Banaszak, L.J.3
  • 62
    • 0037423764 scopus 로고    scopus 로고
    • Functional fingerprints of folds: Evidence for correlated structure-function evolution
    • BE Shakhnovich NV Dokholyan C DeLisi EI Shakhnovich 2003 Functional fingerprints of folds: evidence for correlated structure-function evolution J Mol Biol 326 1 9
    • (2003) J Mol Biol , vol.326 , pp. 1-9
    • Shakhnovich, B.E.1    Dokholyan, N.V.2    Delisi, C.3    Shakhnovich, E.I.4
  • 63
    • 0019321821 scopus 로고
    • Relationship between the substrate activation site and catalytic site of phenylalanine hydroxylase
    • R Shiman 1980 Relationship between the substrate activation site and catalytic site of phenylalanine hydroxylase J Biol Chem 255 10029 10032
    • (1980) J Biol Chem , vol.255 , pp. 10029-10032
    • Shiman, R.1
  • 64
    • 0027937757 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. II: Substrate binding and the role of activation in the control of enzymatic activity
    • R Shiman T Xia MA Hill DW Gray 1994 Regulation of rat liver phenylalanine hydroxylase. II: Substrate binding and the role of activation in the control of enzymatic activity J Biol Chem 269 24647 24656
    • (1994) J Biol Chem , vol.269 , pp. 24647-24656
    • Shiman, R.1    Xia, T.2    Hill, M.A.3    Gray, D.W.4
  • 65
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • IN Shindyalov PE Bourne 1998 Protein structure alignment by incremental combinatorial extension (CE) of the optimal path Protein Eng 11 739 747
    • (1998) Protein Eng , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 66
    • 0035165967 scopus 로고    scopus 로고
    • A database and tools for 3-D protein structure comparison and alignment using the combinatorial extension (CE) algorithm
    • IN Shindyalov PE Bourne 2001 A database and tools for 3-D protein structure comparison and alignment using the combinatorial extension (CE) algorithm Nucleic Acids Res 29 228 229
    • (2001) Nucleic Acids Res , vol.29 , pp. 228-229
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 67
    • 0030814166 scopus 로고    scopus 로고
    • Insights into acylphosphatase structure and catalytic mechanism
    • M Stefani N Taddei G Ramponi 1997 Insights into acylphosphatase structure and catalytic mechanism Cell Mol Life Sci 53 141 151
    • (1997) Cell Mol Life Sci , vol.53 , pp. 141-151
    • Stefani, M.1    Taddei, N.2    Ramponi, G.3
  • 68
    • 0347985688 scopus 로고    scopus 로고
    • Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: The case of Pyrococcus horikoshii CutA
    • Y Tanaka K Tsumoto T Nakanishi Y Yasutake N Sakai M Yao I Tanaka I Kumagai 2004 Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA FEBS Lett 556 167 174
    • (2004) FEBS Lett , vol.556 , pp. 167-174
    • Tanaka, Y.1    Tsumoto, K.2    Nakanishi, T.3    Yasutake, Y.4    Sakai, N.5    Yao, M.6    Tanaka, I.7    Kumagai, I.8
  • 69
    • 0024349252 scopus 로고
    • Protein structure alignment
    • WR Taylor CA Orengo 1989 Protein structure alignment J Mol Biol 208 1 22
    • (1989) J Mol Biol , vol.208 , pp. 1-22
    • Taylor, W.R.1    Orengo, C.A.2
  • 70
    • 17144364299 scopus 로고    scopus 로고
    • Vmax regulation through domain and subunit changes: The active form of phosphoglycerate dehydrogenase
    • JR Thompson JK Bell J Bratt GA Grant LJ Banaszak 2005 Vmax regulation through domain and subunit changes: the active form of phosphoglycerate dehydrogenase Biochemistry 44 5763 5773
    • (2005) Biochemistry , vol.44 , pp. 5763-5773
    • Thompson, J.R.1    Bell, J.K.2    Bratt, J.3    Grant, G.A.4    Banaszak, L.J.5
  • 71
    • 0037129928 scopus 로고    scopus 로고
    • L-Phenylalanine binding and domain organization in human phenylalanine hydroxylase: A differential scanning calorimetry study
    • M Thorolfsson B Ibarra-Molero P Fojan SB Petersen JM Sanchez-Ruiz A Martinez 2002 l-Phenylalanine binding and domain organization in human phenylalanine hydroxylase: a differential scanning calorimetry study Biochemistry 41 7573 7585
    • (2002) Biochemistry , vol.41 , pp. 7573-7585
    • Thorolfsson, M.1    Ibarra-Molero, B.2    Fojan, P.3    Petersen, S.B.4    Sanchez-Ruiz, J.M.5    Martinez, A.6
  • 72
    • 3042581007 scopus 로고    scopus 로고
    • Flexible structure alignment by chaining aligned fragment pairs allowing twists
    • Suppl 2
    • Y Ye A Godzik 2003 Flexible structure alignment by chaining aligned fragment pairs allowing twists Bioinformatics 19 Suppl 2 II246 II255
    • (2003) Bioinformatics , vol.19
    • Ye, Y.1    Godzik, A.2
  • 73
    • 3242887315 scopus 로고    scopus 로고
    • FATCAT: A web server for flexible structure comparison and structure similarity searching
    • Y Ye A Godzik 2004 FATCAT: a web server for flexible structure comparison and structure similarity searching Nucleic Acids Res 32 W582 W585
    • (2004) Nucleic Acids Res , vol.32
    • Ye, Y.1    Godzik, A.2
  • 74
    • 19544388989 scopus 로고    scopus 로고
    • Multiple flexible structure alignment using partial order graphs
    • Y Ye A Godzik 2005 Multiple flexible structure alignment using partial order graphs Bioinformatics 21 2362 2369
    • (2005) Bioinformatics , vol.21 , pp. 2362-2369
    • Ye, Y.1    Godzik, A.2


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