Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyaseThe characterization of mutant Bacillus subtilis adenylosuccinate lyases corresponding to severe human adenylosuccinate lyase deficienciesEffect of a new non-cleavable substrate analog on wild-type and serine mutants in the signature sequence of adenylosuccinate lyase of Bacillus subtilis and Homo sapiensBiochemical and biophysical analysis of five disease-associated human adenylosuccinate lyase mutantsCrystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanismSubstrate and Product Complexes of Escherichia coli Adenylosuccinate Lyase Provide New Insights into the Enzymatic MechanismInsights from retinitis pigmentosa into the roles of isocitrate dehydrogenases in the Krebs cycleThree subunits contribute amino acids to the active site of tetrameric adenylosuccinate lyase: Lys268 and Glu275 are requiredCharacterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: asparagine 276 plays an important structural roleAdenylosuccinate lyase deficiencyTwo novel mutant human adenylosuccinate lyases (ASLs) associated with autism and characterization of the equivalent mutant Bacillus subtilis ASLHeterodimers of wild-type and subunit interface mutant enzymes of glutathione S-transferase A1-1: interactive or independent active sites?Each conserved active site tyr in the three subunits of human isocitrate dehydrogenase has a different function.Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase.Identification of Mn2+-binding aspartates from alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase.Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the distinctive subunits of human NAD-specific isocitrate dehydrogenase.Evaluation of types of interactions in subunit association in Bacillus subtilis adenylosuccinate lyase.A new nonhydrolyzable reactive cGMP analogue, (Rp)-guanosine-3',5'-cyclic-S-(4-bromo-2,3-dioxobutyl)monophosphorothioate, which targets the cGMP binding site of human platelet PDE3A.Location of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase.A new nonhydrolyzable reactive cAMP analog, (Sp)-adenosine-3',5'-cyclic-S-(4-bromo-2,3-dioxobutyl)monophosphorothioate irreversibly inactivates human platelet cGMP-inhibited cAMP phosphodiesterase.A nonhydrolyzable reactive cAMP analogue, (S(p))-8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 3',5'-cyclic S-(methyl)monophosphorothioate, irreversibly inactivates human platelet cGMP-inhibited cAMP phosphodiesterase at micromolar concentrations.Activation by phosphorylation and purification of human c-Jun N-terminal kinase (JNK) isoforms in milligram amounts.GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2.Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin.In vitro hybridization and separation of hybrids of human adenylosuccinate lyase from wild-type and disease-associated mutant enzymes.Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi.Ser95, Asn97, and Thr78 are important for the catalytic function of porcine NADP-dependent isocitrate dehydrogenaseCatalytically active monomer of glutathione S-transferase pi and key residues involved in the electrostatic interaction between subunits.Effect of Asp69 and Arg310 on the pK of His68, a key catalytic residue of adenylosuccinate lyase.Important roles of hydroxylic amino acid residues in the function of Bacillus subtilis adenylosuccinate lyase.Contribution of the mu loop to the structure and function of rat glutathione transferase M1-1.Delineation of xenobiotic substrate sites in rat glutathione S-transferase M1-1.Evaluation by mutagenesis of the roles of His309, His315, and His319 in the coenzyme site of pig heart NADP-dependent isocitrate dehydrogenase.Implication by site-directed mutagenesis of Arg314 and Tyr316 in the coenzyme site of pig mitochondrial NADP-dependent isocitrate dehydrogenase.Critical role of Lys212 and Tyr140 in porcine NADP-dependent isocitrate dehydrogenase.Ligands of the Mn2+ bound to porcine mitochondrial NADP-dependent isocitrate dehydrogenase, as assessed by mutagenesis.Subunit interface residues of glutathione S-transferase A1-1 that are important in the monomer-dimer equilibrium.Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis.Glutathione S-transferase Pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site.Adenosine 2'-monophosphate, 5'-O-[S-(4-succinimidylbenzophenone)-thiophosphate]: a new photoaffinity label for the coenzyme site of porcine NADP-specific isocitrate dehydrogenase.
P50
Q24303115-4588E848-CAF8-4306-83D4-48A5E91792BCQ24644707-118EA65A-E71E-4B2E-8B76-E11947FB773BQ24648971-C47F3F23-2BDA-4FA6-BF8E-A3233001AF17Q24653201-7118AB49-43D0-4A7A-B6A4-D8ECB9A5E827Q27639577-C4C89542-033B-4603-B44E-37135CECAD1AQ27644959-F6E3B5AA-898D-47CD-9974-1F1D00BBC8C4Q28118878-22C0EB8F-AED5-4A63-A429-FD0B70894572Q28200807-0C379C09-E0D8-4EF1-9055-1EC24BE32BB9Q28210122-08519E38-01ED-4AFA-A869-5AD78529CC03Q28251836-F5CC9607-A2FF-451F-9B48-7741ADF9102AQ28286785-98A9C2FD-ED07-4494-8810-C90753797D14Q28909819-51D0AC59-89C4-42F0-BC54-460A398FE57DQ33966836-C9837AF4-85CB-415F-B0A7-EA48797A2FA4Q34269415-0634410D-A933-412B-A9CC-0ABAD40B9F44Q34532420-6DC4EF18-9173-464B-B0A5-B057A8958C42Q34618886-B8FE44DE-4063-4E27-9D6D-40D704877AF0Q34743739-906AF610-9477-410C-87BE-1522C9D3529FQ36837796-2290311B-13D6-4A73-9E3C-588B52BDF63AQ38324543-7373A0AF-C5C0-423B-9A1E-1A7D84481626Q40738147-0F483738-F569-47CA-9996-F63DD6E9E8E7Q40748383-A00A5425-68CC-47B1-B117-EA7C37C0FEF8Q41536717-FCCD9DD7-7FFA-4506-9784-E7A886318649Q41764430-070162C3-B5D0-48EF-A70C-27FC56A13108Q41825511-D3CDF999-88F1-4978-9518-B28AF8746281Q41856033-98C08C1F-A3AC-4266-ACE4-764C46E34584Q41873487-38053F1C-D096-4CC1-85CE-B38A799DFFA6Q42144282-276DF144-D8CB-49CF-A0C5-A1C2C508A8AEQ42272675-D6267A27-A25D-4769-B18D-E97F9AD41319Q42951743-6FDC8E4A-23AC-4261-82BE-717C0E8A7A23Q42958267-54845574-3E70-4AED-A050-FB3C08312DFDQ43043666-4B9ABBBE-E2CC-4F45-A6B6-D3E730602C00Q43057895-9FA05943-D884-4FD4-8B9C-30B4CA87D9AFQ43968657-2434C789-FAE0-40D8-B941-73C205EF0979Q44020722-E76BC5E2-EA0F-46DB-BBD6-C0859D6D7B02Q44598328-A354B52A-6A6C-4074-BC48-01FDE6AE5641Q44789574-04B2A74B-9E46-4E60-B559-8018103BEB95Q44808493-608924E0-105F-4C87-B4D7-A3A0743BA117Q44925097-1A7008D5-1A5F-4A34-BB2A-1F5A2E360A6FQ45044236-E8BEAD1A-9663-473D-8575-D33C5D8A6862Q46494581-DC2D3A31-F32F-4876-9720-1C12704959A1
P50
description
American biochemist
@en
name
Roberta F. Colman
@en
Roberta F. Colman
@nl
type
label
Roberta F. Colman
@en
Roberta F. Colman
@nl
altLabel
Roberta Colman
@en
prefLabel
Roberta F. Colman
@en
Roberta F. Colman
@nl
P106
P21
P31
P569
1938-01-01T00:00:00Z
P570
2019-08-15T00:00:00Z