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1.
Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure.
Biochemistry
; 55(3): 560-74, 2016 Jan 26.
Artículo
en Inglés
| MEDLINE | ID: mdl-26731489
2.
Importance of aspartate residues in balancing the flexibility and fine-tuning the catalysis of human 3-phosphoglycerate kinase.
Biochemistry
; 51(51): 10197-207, 2012 Dec 21.
Artículo
en Inglés
| MEDLINE | ID: mdl-23231058
3.
A spring-loaded release mechanism regulates domain movement and catalysis in phosphoglycerate kinase.
J Biol Chem
; 286(16): 14040-8, 2011 Apr 22.
Artículo
en Inglés
| MEDLINE | ID: mdl-21349853
4.
Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 6): 738-43, 2010 Jun 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-20516614
5.
Ligand-induced conformational rearrangements regulate the switch between membrane-proximal and distal functions of Rho kinase 2.
Commun Biol
; 3(1): 721, 2020 11 27.
Artículo
en Inglés
| MEDLINE | ID: mdl-33247217
6.
Symmetrical refolding of protein domains and subunits: example of the dimeric two-domain 3-isopropylmalate dehydrogenases.
Biochemistry
; 48(5): 1123-34, 2009 Feb 10.
Artículo
en Inglés
| MEDLINE | ID: mdl-19154118
7.
A versatile modular vector set for optimizing protein expression among bacterial, yeast, insect and mammalian hosts.
PLoS One
; 14(12): e0227110, 2019.
Artículo
en Inglés
| MEDLINE | ID: mdl-31887188
8.
Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase.
FEBS Lett
; 580(11): 2698-706, 2006 May 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-16647059
9.
Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase.
FEBS J
; 272(8): 1867-85, 2005 Apr.
Artículo
en Inglés
| MEDLINE | ID: mdl-15819882
10.
Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.
FEBS Lett
; 589(2): 240-5, 2015 Jan 16.
Artículo
en Inglés
| MEDLINE | ID: mdl-25497013
11.
Structural and energetic basis of isopropylmalate dehydrogenase enzyme catalysis.
FEBS J
; 281(22): 5063-76, 2014 Nov.
Artículo
en Inglés
| MEDLINE | ID: mdl-25211160
12.
Drugs against Mycobacterium tuberculosis 3-isopropylmalate dehydrogenase can be developed using homologous enzymes as surrogate targets.
Protein Pept Lett
; 21(12): 1295-307, 2014.
Artículo
en Inglés
| MEDLINE | ID: mdl-24909230
13.
Transient kinetic studies reveal isomerization steps along the kinetic pathway of Thermus thermophilus 3-isopropylmalate dehydrogenase.
FEBS J
; 280(8): 1764-72, 2013 Apr.
Artículo
en Inglés
| MEDLINE | ID: mdl-23421786
14.
Selectivity of kinases on the activation of tenofovir, an anti-HIV agent.
Eur J Pharm Sci
; 48(1-2): 307-15, 2013 Jan 23.
Artículo
en Inglés
| MEDLINE | ID: mdl-23201309
15.
Atomic level description of the domain closure in a dimeric enzyme: thermus thermophilus 3-isopropylmalate dehydrogenase.
Mol Biosyst
; 7(5): 1646-59, 2011 May.
Artículo
en Inglés
| MEDLINE | ID: mdl-21387033
16.
Essential role of the metal-ion in the IPM-assisted domain closure of 3-isopropylmalate dehydrogenase.
FEBS Lett
; 585(20): 3297-302, 2011 Oct 20.
Artículo
en Inglés
| MEDLINE | ID: mdl-21939659
17.
Nucleotide promiscuity of 3-phosphoglycerate kinase is in focus: implications for the design of better anti-HIV analogues.
Mol Biosyst
; 7(6): 1863-73, 2011 Jun.
Artículo
en Inglés
| MEDLINE | ID: mdl-21505655
18.
Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases.
Biochemistry
; 46(41): 11536-49, 2007 Oct 16.
Artículo
en Inglés
| MEDLINE | ID: mdl-17887729
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