Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
about
Perturbation of the Dimer Interface of Triosephosphate Isomerase and its Effect on Trypanosoma cruziRevisiting the mechanism of the triosephosphate isomerase reaction: the role of the fully conserved glutamic acid 97 residueProbing the role of highly conserved residues in triosephosphate isomerase--analysis of site specific mutants at positions 64 and 75 in the Plasmodial enzymeWhen monomers are preferred: a strategy for the identification and disruption of weakly oligomerized proteinsReflections on the catalytic power of a TIM-barrel.Identification of fibrillogenic regions in human triosephosphate isomerase.Computer simulation of the triosephosphate isomerase catalyzed reaction.Investigating and Engineering Enzymes by Genetic Selection.Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion.The loop opening/closing motion of the enzyme triosephosphate isomeraseSubstrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.Engineering subunit association of multisubunit proteins: a dimeric streptavidin.Identification of the Serratia endonuclease dimer: structural basis and implications for catalysis.The role of quaternary interactions on the stability and activity of ascorbate peroxidaseDisruption of the aldolase A tetramer into catalytically active monomersA paradigm for enzyme-catalyzed proton transfer at carbon: triosephosphate isomerase.Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Structural basis for the biological activities of bovine seminal ribonuclease.Computer applications for prediction of protein-protein interactions and rational drug design.A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation.Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme.Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies.Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomeraseMass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii.Characterization of a monomeric Escherichia coli alkaline phosphatase formed upon a single amino acid substitution.Thermodynamic analysis of the dissociation of the aldolase tetramer substituted at one or both of the subunit interfaces.Role of an N-terminal extension in stability and catalytic activity of a hyperthermostable α/β hydrolase fold esterase.Detection of the protein dimers, multiple monomeric states and hydrated forms of Plasmodium falciparum triosephosphate isomerase in the gas phase.Structure-based directed evolution of a monomeric triosephosphate isomerase: toward a pentose sugar isomerase.Redesigning the Quaternary Structure of R67 Dihydrofolate Reductase
P2860
Q27648979-BF36803F-4DB1-458A-8556-141AB09E7D2BQ27670430-E7968EFC-9787-497A-930D-E0431E36210AQ27701621-D6E97ABD-70A0-48B0-9063-E529599968F9Q30349959-49A64261-DC49-4096-8EA0-9E16D9536AF1Q30365425-C77ACE9B-3E9B-4BF4-B87D-7939A75A2C44Q30384397-023CAB3F-9EDC-4992-A6A0-70B7A8142665Q30423772-7AE33B5D-7EEB-4742-92BB-66B45D04705AQ30731663-E7026945-96EE-4430-AFFC-C45CE040DA7CQ33893026-B58282AD-C580-4FD8-9F2B-ADDC6AB6F874Q34167001-28440493-7BF1-4224-A83B-EA6E8E5DD12EQ35855397-FDF9D7B6-4D8D-4759-9797-974AB03C97D8Q36180294-46DBAFEE-2C46-4E42-A3E6-A939C63006C5Q36279420-E34537A1-477E-4B26-8113-7A2A7886EB3EQ36280660-B91A2E43-26C2-4C14-A82B-70D8C242EA6DQ37585950-6A88DC9E-DEA9-4BD7-859F-1435D20D3616Q37992670-7991C61A-EF97-43BB-8CA0-593575FEA197Q38287400-7293E422-12F1-4182-B14B-B69720441763Q38295605-5A89095B-F7F9-41BF-8341-B37977C5656FQ38364115-BB7E4297-EA6D-4E0B-8148-27C16513795FQ39221322-2ACA409C-C168-49A1-BAFE-D310C9577500Q39682155-1207B7CA-EF21-4333-A17B-C8CE92D31422Q40529724-F221303B-CF20-4972-8CC4-BDFEFB8E440CQ41830632-36CACBE4-B0DC-4E11-9254-1B9AD44FAC29Q42845160-4ED8A78B-8BB7-4A56-8591-3BEC4F9596F3Q42845562-90D3298B-C5E3-4DED-A5CD-73EA3FA90466Q43031789-125307C3-14E2-45E6-88D4-A35B63FD54D9Q44411426-03383A45-CD45-44C8-8C9A-895C6B4C3EE9Q44689324-0E8A618B-2AFA-415E-9900-74269FE4DFCDQ47716456-8398A456-8963-47C3-AD17-427232ABAA03Q51786314-7DA08E37-46F9-49DC-B5CD-F4D8DBA625D1Q52868773-5C7E1FBF-FD6F-496F-B70A-F32BCEF3047AQ58322383-DA96D739-CCB8-4B53-A647-E623D23E7C8E
P2860
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
description
1994 nî lūn-bûn
@nan
1994 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
@ast
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
@en
type
label
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
@ast
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
@en
prefLabel
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
@ast
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
@en
P2093
P2860
P356
P1476
Design, creation, and characterization of a stable, monomeric triosephosphate isomerase.
@en
P2093
Borchert TV
Jaenicke R
Wierenga RK
P2860
P304
P356
10.1073/PNAS.91.4.1515
P407
P577
1994-02-01T00:00:00Z