VIAF

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Leader 00000nz a2200037n 45 0
001 WKP|Q58784107 (VIAF cluster) (Authority/Source Record)
003 WKP
005 20241120235811.0
008 241120nneanz||abbn n and d
035 ‎‡a (WKP)Q58784107‏
024 ‎‡a 0000-0002-0727-822X‏ ‎‡2 orcid‏
035 ‎‡a (OCoLC)Q58784107‏
100 0 ‎‡a Vicente Jara-Perez‏ ‎‡c researcher ORCID ID = 0000-0002-0727-822X‏ ‎‡9 en‏
375 ‎‡a 1‏ ‎‡2 iso5218‏
400 0 ‎‡a Vicente Jara-Perez‏ ‎‡c onderzoeker‏ ‎‡9 nl‏
670 ‎‡a Author's A monomer form of the glutathione S-transferase Y7F mutant from Schistosoma japonicum at acidic pH.‏
670 ‎‡a Author's A thermodynamic characterization of the interaction of 8-anilino-1-naphthalenesulfonic acid with native globular proteins: the effect of the ligand dimerization in the analysis of the binding isotherms‏
670 ‎‡a Author's Binding studies of hydantoin racemase from Sinorhizobium meliloti by calorimetric and fluorescence analysis.‏
670 ‎‡a Author's Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum.‏
670 ‎‡a Author's Enzymatic activity assay of d-hydantoinase by isothermal titration calorimetry. Determination of the thermodynamic activation parameters for the hydrolysis of several substrates‏
670 ‎‡a Author's Kinetic analysis and modelling of the allosteric behaviour of liver and muscle glycogen phosphorylases‏
670 ‎‡a Author's Purification of angiotensin I converting enzyme from pig lung using concanavalin-A sepharose chromatography‏
670 ‎‡a Author's Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti.‏
670 ‎‡a Author's Thermodynamic and mutational studies of l-N-carbamoylase from Sinorhizobium meliloti CECT 4114 catalytic centre‏
670 ‎‡a Author's Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method‏
670 ‎‡a Author's Thermodynamic study of the dimerization of 8-anilino-1-naphthalenesulfonic acid by isothermal titration calorimetry‏
670 ‎‡a Author's Thermodynamics of glutathione binding to the tyrosine 7 to phenylalanine mutant of glutathione S-transferase from Schistosoma japonicum‏
909 ‎‡a (orcid) 000000020727822x‏ ‎‡9 1‏
919 ‎‡a thermodynamicstudyofthedimerizationof8anilino1naphthalenesulfonicacidbyisothermaltitrationcalorimetry‏ ‎‡A Thermodynamic study of the dimerization of 8-anilino-1-naphthalenesulfonic acid by isothermal titration calorimetry‏ ‎‡9 1‏
919 ‎‡a thermodynamicsofglutathionebindingtothetyrosine7tophenylalaninemutantofglutathionestransferasefromschistosomajaponicum‏ ‎‡A Thermodynamics of glutathione binding to the tyrosine 7 to phenylalanine mutant of glutathione S-transferase from Schistosoma japonicum‏ ‎‡9 1‏
919 ‎‡a sitedirectedmutagenesisindicatesanimportantroleofcysteines76and181inthecatalysisofhydantoinracemasefromsinorhizobiummeliloti‏ ‎‡A Site-directed mutagenesis indicates an important role of cysteines 76 and 181 in the catalysis of hydantoin racemase from Sinorhizobium meliloti.‏ ‎‡9 1‏
919 ‎‡a kineticanalysisandmodellingoftheallostericbehaviourofliverandmuscleglycogenphosphorylases‏ ‎‡A Kinetic analysis and modelling of the allosteric behaviour of liver and muscle glycogen phosphorylases‏ ‎‡9 1‏
919 ‎‡a thermodynamicandmutationalstudiesof50ncarbamoylasefromsinorhizobiummeliloticect4114catalyticcentre‏ ‎‡A Thermodynamic and mutational studies of l-N-carbamoylase from Sinorhizobium meliloti CECT 4114 catalytic centre‏ ‎‡9 1‏
919 ‎‡a purificationofangiotensin1convertingenzymefrompiglungusingconcanavalinasepharosechromatography‏ ‎‡A Purification of angiotensin I converting enzyme from pig lung using concanavalin-A sepharose chromatography‏ ‎‡9 1‏
919 ‎‡a monomerformoftheglutathionestransferasey7fmutantfromschistosomajaponicumatacidicph‏ ‎‡A A monomer form of the glutathione S-transferase Y7F mutant from Schistosoma japonicum at acidic pH.‏ ‎‡9 1‏
919 ‎‡a thermodynamiccharacterizationoftheinteractionof8anilino1naphthalenesulfonicacidwithnativeglobularproteinstheeffectoftheliganddimerizationintheanalysisofthebindingisotherms‏ ‎‡A A thermodynamic characterization of the interaction of 8-anilino-1-naphthalenesulfonic acid with native globular proteins: the effect of the ligand dimerization in the analysis of the binding isotherms‏ ‎‡9 1‏
919 ‎‡a bindingstudiesofhydantoinracemasefromsinorhizobiummelilotibycalorimetricandfluorescenceanalysis‏ ‎‡A Binding studies of hydantoin racemase from Sinorhizobium meliloti by calorimetric and fluorescence analysis.‏ ‎‡9 1‏
919 ‎‡a thermodynamicdeterminationofthebindingconstantsofangiotensinconvertingenzymeinhibitorsbyadisplacementmethod‏ ‎‡A Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method‏ ‎‡9 1‏
919 ‎‡a crystallographicandthermodynamicanalysisofthebindingofsoctylglutathionetothetyr7tophemutantofglutathionestransferasefromschistosomajaponicum‏ ‎‡A Crystallographic and thermodynamic analysis of the binding of S-octylglutathione to the Tyr 7 to Phe mutant of glutathione S-transferase from Schistosoma japonicum.‏ ‎‡9 1‏
919 ‎‡a enzymaticactivityassayof500hydantoinasebyisothermaltitrationcalorimetrydeterminationofthethermodynamicactivationparametersforthehydrolysisofseveralsubstrates‏ ‎‡A Enzymatic activity assay of d-hydantoinase by isothermal titration calorimetry. Determination of the thermodynamic activation parameters for the hydrolysis of several substrates‏ ‎‡9 1‏
946 ‎‡a b‏ ‎‡9 1‏
996 ‎‡2 DNB|1158998058
996 ‎‡2 NII|DA02730547
996 ‎‡2 BNE|XX1079247
996 ‎‡2 BNC|981058517705706706
996 ‎‡2 DNB|1157401678
996 ‎‡2 BNE|XX4988129
996 ‎‡2 ICCU|CUBV122913
996 ‎‡2 BNF|12139254
996 ‎‡2 BNE|XX5594786
996 ‎‡2 LC|no 99058802
996 ‎‡2 SUDOC|196229219
996 ‎‡2 BIBSYS|12035054
996 ‎‡2 BNE|XX1062545
996 ‎‡2 NUKAT|n 2009083223
996 ‎‡2 DNB|1329531213
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996 ‎‡2 BLBNB|001009435
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996 ‎‡2 LC|n 2006004709
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996 ‎‡2 BNF|14028955
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996 ‎‡2 BNE|XX5602936
996 ‎‡2 BNE|XX1798371
996 ‎‡2 LC|n 83147879
996 ‎‡2 LC|nb2005016125
996 ‎‡2 SUDOC|261642707
996 ‎‡2 NTA|074287559
996 ‎‡2 BNC|981058525866206706
996 ‎‡2 LC|no2004076347
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996 ‎‡2 ISNI|0000000066326063
996 ‎‡2 BNE|XX1105792
996 ‎‡2 BNCHL|10000000000000000072734
996 ‎‡2 BNE|XX1395292
996 ‎‡2 ISNI|000000011020307X
996 ‎‡2 LC|no2011123751
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996 ‎‡2 BNE|XX914533
996 ‎‡2 BIBSYS|13037265
996 ‎‡2 RERO|A017327203
996 ‎‡2 RERO|A018811169
996 ‎‡2 NUKAT|n 2009154027
996 ‎‡2 SUDOC|060159952
996 ‎‡2 BNE|XX4821986
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996 ‎‡2 NYNYRILM|353755
996 ‎‡2 DNB|1057134023
996 ‎‡2 BNE|XX4604530
996 ‎‡2 BNF|16416623
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996 ‎‡2 LC|n 85239679
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996 ‎‡2 SUDOC|136328377
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996 ‎‡2 BNCHL|10000000000000000837846
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996 ‎‡2 SUDOC|268071853
996 ‎‡2 SUDOC|193766078
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996 ‎‡2 B2Q|0000088830
996 ‎‡2 ISNI|0000000108145237
996 ‎‡2 DNB|1056454946
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996 ‎‡2 DNB|1157234836
996 ‎‡2 J9U|987007275741505171
996 ‎‡2 LC|nr2001053195
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996 ‎‡2 PTBNP|265529
996 ‎‡2 BNE|XX1653314
996 ‎‡2 BNCHL|10000000000000000080553
996 ‎‡2 BNE|XX1042819
996 ‎‡2 ISNI|0000000093108440
996 ‎‡2 ISNI|0000000374870191
996 ‎‡2 BNE|XX5056454
996 ‎‡2 BNCHL|10000000000000000095327
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996 ‎‡2 BNC|981058524689806706
996 ‎‡2 N6I|vtls001281433
996 ‎‡2 ISNI|0000000117573268
996 ‎‡2 NKC|osd2014827886
996 ‎‡2 BNE|XX5274260
996 ‎‡2 BNE|XX4714140
996 ‎‡2 DNB|1045803774
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996 ‎‡2 BNC|981058508449806706
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996 ‎‡2 LC|n 85050015
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996 ‎‡2 NTA|175048703
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996 ‎‡2 BNF|16919951
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996 ‎‡2 PTBNP|251193
996 ‎‡2 LC|n 82079210
996 ‎‡2 ISNI|000000006301809X
996 ‎‡2 LNL|13324
996 ‎‡2 ISNI|0000000026955447
996 ‎‡2 LC|n 2019064611
996 ‎‡2 BNC|981058509950806706
996 ‎‡2 LC|no2007134388
996 ‎‡2 LC|n 90604193
996 ‎‡2 LC|n 83219748
996 ‎‡2 DNB|1056170336
996 ‎‡2 DE633|pe50043463
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996 ‎‡2 BNE|XX1221906
996 ‎‡2 BNC|981058608966106706
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996 ‎‡2 LC|n 81138088
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996 ‎‡2 BNE|XX929624
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996 ‎‡2 BNE|XX1102333
996 ‎‡2 RERO|A003718698
996 ‎‡2 SUDOC|171887050
996 ‎‡2 BNE|XX1515382
996 ‎‡2 BNF|14640092
996 ‎‡2 CAOONL|ncf11022612
996 ‎‡2 PLWABN|9810564248905606
996 ‎‡2 BNC|981058525407906706
996 ‎‡2 BNE|XX4942740
996 ‎‡2 DNB|1057428302
996 ‎‡2 BNE|XX1068302
996 ‎‡2 SZ|139219935
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996 ‎‡2 J9U|987007460504505171
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996 ‎‡2 BNE|XX994280
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996 ‎‡2 BNC|981058611127306706
996 ‎‡2 BNC|981058510928906706
996 ‎‡2 BNE|XX4746574
996 ‎‡2 LC|no2014041326
996 ‎‡2 LC|no2019003786
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996 ‎‡2 PTBNP|1457974
996 ‎‡2 BNCHL|10000000000000000150539
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996 ‎‡2 NII|DA09705118
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996 ‎‡2 BNE|XX4760533
996 ‎‡2 BNE|XX1223124
996 ‎‡2 LC|no2024008498
996 ‎‡2 BNE|XX4579781
996 ‎‡2 NII|DA13168500
996 ‎‡2 PTBNP|56274
996 ‎‡2 BNC|981058510669006706
996 ‎‡2 LIH|LNB:C8PB;=_w_C
996 ‎‡2 LC|no2009052498
996 ‎‡2 ISNI|0000000121419220
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996 ‎‡2 CAOONL|ncf11255692
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996 ‎‡2 LC|no2013136633
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996 ‎‡2 BNF|17763492
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996 ‎‡2 DNB|1246907569
996 ‎‡2 LIH|LNB:BIY4;=BE
996 ‎‡2 DNB|1157178820
996 ‎‡2 RERO|A012824525
996 ‎‡2 BIBSYS|90932301
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996 ‎‡2 SUDOC|032819374
997 ‎‡a 0 0 lived 0 0‏ ‎‡9 1‏