Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis.
about
Directed evolution of a model primordial enzyme provides insights into the development of the genetic codeBiochemical and Structural Characterization of the Secreted Chorismate Mutase (Rv1885c) from Mycobacterium tuberculosis H37Rv: an *AroQ Enzyme Not Regulated by the Aromatic Amino AcidsStructure and function of a complex between chorismate mutase and DAHP synthase: efficiency boost for the junior partnerA comparative biochemical and structural analysis of the intracellular chorismate mutase (Rv0948c) from Mycobacterium tuberculosis H(37)R(v) and the secreted chorismate mutase (y2828) from Yersinia pestisProbing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteineThe two chorismate mutases from both Mycobacterium tuberculosis and Mycobacterium smegmatis: biochemical analysis and limited regulation of promoter activity by aromatic amino acidsA novel noncovalent complex of chorismate mutase and DAHP synthase from Mycobacterium tuberculosis: protein purification, crystallization and X-ray diffraction analysisMechanistic insights into the isochorismate pyruvate lyase activity of the catalytically promiscuous PchB from combinatorial mutagenesis and selection.Mycobacterium tuberculosis nucleoid-associated DNA-binding protein H-NS binds with high-affinity to the Holliday junction and inhibits strand exchange promoted by RecA protein.Identification, characterization, and application of a recombinant antigen for the serological investigation of feline hemotropic Mycoplasma infections.Evolution of invasion in a diverse set of Fusobacterium species.Functional mapping of protein-protein interactions in an enzyme complex by directed evolution.Preliminary X-ray crystallographic analysis of the secreted chorismate mutase from Mycobacterium tuberculosis: a tricky crystallization problem solved.Molecular dynamics simulation of the last step of a catalytic cycle: product release from the active site of the enzyme chorismate mutase from Mycobacterium tuberculosis.Design, selection, and characterization of a split chorismate mutase.Crystallization and preliminary X-ray crystallographic studies of Mycobacterium tuberculosis chorismate mutase.The importance of chorismate mutase in the biocontrol potential of Trichoderma parareesei.Discovery and structure optimization of a series of isatin derivatives as Mycobacterium tuberculosis chorismate mutase inhibitors.Building proficient enzymes with foldamer prostheses.Rational Discovery of (+) (S) Abscisic Acid as a Potential Antifungal Agent: a Repurposing Approach.When Inhibitors Do Not Inhibit: Critical Evaluation of Rational Drug Design Targeting Chorismate Mutase fromMycobacterium tuberculosis
P2860
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P2860
Characterization of the secreted chorismate mutase from the pathogen Mycobacterium tuberculosis.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Characterization of the secret ...... en Mycobacterium tuberculosis.
@en
type
label
Characterization of the secret ...... en Mycobacterium tuberculosis.
@en
prefLabel
Characterization of the secret ...... en Mycobacterium tuberculosis.
@en
P2093
P2860
P1433
P1476
Characterization of the secret ...... en Mycobacterium tuberculosis.
@en
P2093
Chandra Ramakrishnan
Donald Hilvert
Marianne Gamper
Peter Kast
Severin Sasso
P2860
P304
P356
10.1111/J.1742-4658.2004.04478.X
P407
P577
2005-01-01T00:00:00Z