The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum.
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Identification and characterization of a bacterial glutamic peptidaseGenomic analysis of the necrotrophic fungal pathogens Sclerotinia sclerotiorum and Botrytis cinereaMutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residuesInvolvement of Kallikrein-Related Peptidases in Normal and Pathologic ProcessesProtease regulation: the Yin and Yang of neural development and diseaseMechanism of farnesylated CAAX protein processing by the intramembrane protease Rce1The proprotein convertases and their implication in sterol and/or lipid metabolismVitAL: Viterbi algorithm for de novo peptide designCandida albicans possesses Sap7 as a pepstatin A-insensitive secreted aspartic proteaseSite-directed mutagenesis and structural studies suggest that the germination protease, GPR, in spores of Bacillus species is an atypical aspartic acid protease.Activation profiles of the zymogen of aspergilloglutamic peptidase.Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes.New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases.Structure and function studies on enzymes with a catalytic carboxyl group(s): from ribonuclease T1 to carboxyl peptidasesCatalytic residues and substrate specificity of scytalidoglutamic peptidase, the first member of the eqolisin in family (G1) of peptidases.Evolution of the thermopsin peptidase family (A5)Inhibition of the CaaX proteases Rce1p and Ste24p by peptidyl (acyloxy)methyl ketones.The many faces of protease-protein inhibitor interactionThe peptidases from fungi and viruses.Inhibition of a secreted glutamic peptidase prevents growth of the fungus Talaromyces emersoniiUnidirectional binding of clostridial collagenase to triple helical substrates.Genome sequence of Aspergillus luchuensis NBRC 4314.Identification of a glutamine residue essential for catalytic activity of aspergilloglutamic peptidase by site-directed mutagenesis.Isolation and properties of extracellular proteinases of Penicillium marneffei.Studies on the catalytic mechanism of a glutamic peptidase.Specific inhibition and stabilization of aspergilloglutamic peptidase by the propeptide. Identification of critical sequences and residues in the propeptide.Isotope-Labeled Aspartate Sidechain as a Non-Perturbing Infrared Probe: Application to Investigate the Dynamics of a Carboxylate Buried Inside a Protein.Rce1: mechanism and inhibition.Molecular dynamics and structure function analysis show that substrate binding and specificity are major forces in the functional diversification of Eqolisins
P2860
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P2860
The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum.
description
2004 nî lūn-bûn
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2004 թուականի Մարտին հրատարակուած գիտական յօդուած
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2004 թվականի մարտին հրատարակված գիտական հոդված
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2004年の論文
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2004年論文
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2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The molecular structure and ca ...... e from Scytalidium lignicolum.
@ast
The molecular structure and ca ...... e from Scytalidium lignicolum.
@en
The molecular structure and ca ...... e from Scytalidium lignicolum.
@nl
type
label
The molecular structure and ca ...... e from Scytalidium lignicolum.
@ast
The molecular structure and ca ...... e from Scytalidium lignicolum.
@en
The molecular structure and ca ...... e from Scytalidium lignicolum.
@nl
prefLabel
The molecular structure and ca ...... e from Scytalidium lignicolum.
@ast
The molecular structure and ca ...... e from Scytalidium lignicolum.
@en
The molecular structure and ca ...... e from Scytalidium lignicolum.
@nl
P2093
P2860
P356
P1476
The molecular structure and ca ...... e from Scytalidium lignicolum.
@en
P2093
Hiroshi Oyama
Maia M Cherney
Masao Fujinaga
Michael N G James
P2860
P304
P356
10.1073/PNAS.0400246101
P407
P577
2004-03-01T00:00:00Z