Substrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.
about
The Glycolytic Enzyme Triosephosphate Isomerase of Trichomonas vaginalis Is a Surface-Associated Protein Induced by Glucose That Functions as a Laminin- and Fibronectin-Binding Protein.Structural Basis for Redox Regulation of Cytoplasmic and Chloroplastic Triosephosphate Isomerases from Arabidopsis thaliana.A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Structural insights from a novel invertebrate triosephosphate isomerase from Litopenaeus vannamei.
P2860
Substrate-Induced Dimerization of Engineered Monomeric Variants of Triosephosphate Isomerase from Trichomonas vaginalis.
description
2015 nî lūn-bûn
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2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
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2015年论文
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name
Substrate-Induced Dimerization ...... se from Trichomonas vaginalis.
@ast
Substrate-Induced Dimerization ...... se from Trichomonas vaginalis.
@en
type
label
Substrate-Induced Dimerization ...... se from Trichomonas vaginalis.
@ast
Substrate-Induced Dimerization ...... se from Trichomonas vaginalis.
@en
prefLabel
Substrate-Induced Dimerization ...... se from Trichomonas vaginalis.
@ast
Substrate-Induced Dimerization ...... se from Trichomonas vaginalis.
@en
P2093
P2860
P50
P1433
P1476
Substrate-Induced Dimerization ...... se from Trichomonas vaginalis.
@en
P2093
Ana C Migliorini-Figueira
Armando Gómez-Puyou
Carlos H Trasviña-Arenas
Carmen Portillo
Corina Diaz-Quezada
Eugenia Sanchez-Sandoval
Jaime Ortega-Lopez
Luis G Brieba
Marisol Lopez-Hidalgo
María E Cruces
P2860
P304
P356
10.1371/JOURNAL.PONE.0141747
P407
P50
P577
2015-11-30T00:00:00Z