about
The three-dimensional structural basis of type II hyperprolinemiaA Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate † ‡Functional Role for the Conformationally Mobile Phenylalanine 223 in the Reaction of Methylenetetrahydrofolate Reductase from Escherichia coliThe Structure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N -Propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction ,Structure of Avian Thymic Hormone, a High-Affinity Avian β-Parvalbumin, in the Ca2+-Free and Ca2+-Bound StatesRecognition of Nucleoside Monophosphate Substrates by Haemophilus influenzae Class C Acid PhosphataseCrystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogensSolution structures of chicken parvalbumin 3 in the Ca(2+)-free and Ca(2+)-bound statesCrystal structure and immunogenicity of the class C acid phosphatase from Pasteurella multocidaProline: Mother Nature's cryoprotectant applied to protein crystallographyIdentification of the NAD(P)H Binding Site of Eukaryotic UDP-Galactopyranose MutaseCrystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated with Flavin Reduction and Product ReleaseCrystal Structures and Small-angle X-ray Scattering Analysis of UDP-galactopyranose Mutase from the Pathogenic Fungus Aspergillus fumigatusInvolvement of the β3-α3 Loop of the Proline Dehydrogenase Domain in Allosteric Regulation of Membrane Association of Proline Utilization AStructural Determinants of Oligomerization of Δ1-Pyrroline-5-Carboxylate Dehydrogenase: Identification of a Hexamerization Hot SpotCrystal Structures of Trypanosoma cruzi UDP-Galactopyranose Mutase Implicate Flexibility of the Histidine Loop in Enzyme ActivationStructural Studies of Yeast Δ 1 -Pyrroline-5-carboxylate Dehydrogenase (ALDH4A1): Active Site Flexibility and Oligomeric StateStructures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding siteKinetic and Structural Characterization of Tunnel-Perturbing Mutants in Bradyrhizobium japonicum Proline Utilization ADiethylaminobenzaldehyde is a covalent, irreversible inactivator of ALDH7A1Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenaseCrystal structure and tartrate inhibition of Legionella pneumophila histidine acid phosphataseEF5 Is the High-Affinity Mg(2+) Site in ALG-2Structures of Proline Utilization A Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown FunctionConservation of functionally important global motions in an enzyme superfamily across varying quaternary structuresIdentification of a Conserved Histidine as Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein.STRUCTURAL VIROLOGY. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability.Exploring structurally conserved solvent sites in protein families.Evidence that the C-terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channeling.Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics.First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions.Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.SAXS fingerprints of aldehyde dehydrogenase oligomersCrystallization of recombinant Haemophilus influenzae e (P4) acid phosphatase.In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction.Unique structural features and sequence motifs of proline utilization A (PutA).Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA).Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA.Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure.Empirical power laws for the radii of gyration of protein oligomers.
P50
Q24315802-12400D01-E398-4DC8-944A-ADB6438A7895Q27653411-81E7777E-BB6A-4C62-A941-28E30A8BCBBEQ27656526-AB2513F5-2395-431C-A5AB-537EE90EB58EQ27658535-6513717D-ABDB-45E9-B882-8DBBA2B5092FQ27659853-88A8FEEE-8BBC-4C31-9FAD-3666F50E2F29Q27664961-B704E33A-E925-4645-B82E-127336C8144DQ27666625-FB8CE4E2-46E8-49C3-A1BD-07240C0004D5Q27666630-85AB27EC-D9D9-46FE-82FE-AAD8E6705BA0Q27667160-6C75E85D-C9F7-4F46-B024-593F372ED556Q27671180-46C5CCCA-9BC7-45B6-B118-CECAC8CBE04AQ27674233-ED439321-4959-4A1E-9966-9FF53AFBCCDFQ27675129-C99AC60A-982E-40A8-A9E9-251246AEF91DQ27676971-3EDDD1CE-6143-4F70-B69B-D5F4374B7B44Q27678361-B2A4972A-2C92-4BA0-B405-1181192838CAQ27678545-79C1B7C8-DB10-41EF-BC99-21F8FC00F0FCQ27679366-E4536975-9D9D-4E88-8EF2-6F9AAEC2A60BQ27681620-42D06EDA-EFDE-428D-93AF-E604A4CDFF4BQ27681821-90BBEA9C-5FB9-4AF4-8DC4-C8E66C2D5560Q27684757-B04AA1D9-719B-4BC8-83F5-308B1FAAF045Q27697275-5C3BDA91-FACA-4FE1-8C08-31DC8507415EQ27702161-58050F2A-74DD-4A0A-90DB-5F64114FC801Q27702173-D1C8FC43-38B2-4826-9ECE-8D5798E2E6AEQ27727714-C9224807-8D46-4D91-A196-D87F46816BF1Q27728132-38476083-32F6-44A4-BF93-D47C9714F11DQ28273939-11F24E0C-C176-4718-A6EE-DFB53A6D430EQ30101149-4BFE5449-7B0F-414B-BBF7-D85A5E74DA54Q30279235-36E87F79-38DD-490C-BBD5-662AE35849BAQ30354348-CAEF6B67-A444-4547-B374-A41363D2D231Q34155651-0C9AB15D-D897-488C-A333-56A6E032AAD2Q34731559-B6ED5845-5116-48A1-923B-49FB82DCF770Q35002908-28894E95-0D45-4005-8B09-86C57F764574Q36045705-0966D436-7112-4F11-A3AB-61B0A95C8194Q36319737-8925A8DF-F7FF-4F3D-A908-215C561B6589Q36417378-76D378E7-2A32-4E7D-A70C-AB8CA24F0013Q36761390-88062682-F1F8-46BD-AA9C-60F0331AD4F2Q37024756-75184173-0383-4986-BEB1-4EDAC11D418EQ37563541-9BBA9252-7DEB-4D12-B312-C2ED1250BA23Q37626806-E9EBB687-2D69-42FC-8146-131303F70E6EQ38677885-70A4BBC6-679A-4E8E-9D13-0A3CD3FFA18AQ38814269-9F1AB072-F076-428F-9651-A7D55B5869C5
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
John J Tanner
@ast
John J Tanner
@en
John J Tanner
@es
John J Tanner
@nl
John J Tanner
@sl
type
label
John J Tanner
@ast
John J Tanner
@en
John J Tanner
@es
John J Tanner
@nl
John J Tanner
@sl
prefLabel
John J Tanner
@ast
John J Tanner
@en
John J Tanner
@es
John J Tanner
@nl
John J Tanner
@sl
P106
P31
P496
0000-0001-8314-113X