Kinetic stability as a mechanism for protease longevity.
about
Functional modulation of a protein folding landscape via side-chain distortionStructural and mutational analysis of a monomeric and dimeric form of a single domain antibody with implications for protein misfoldingA multiparametric computational algorithm for comprehensive assessment of genetic mutations in mucopolysaccharidosis type IIIA (Sanfilippo syndrome)Unfolding of Green Fluorescent Protein mut2 in wet nanoporous silica gels.Characterization of an extracellular alkaline serine protease from marine Engyodontium album BTMFS10.Role of pyridoxal 5'-phosphate in the structural stabilization of O-acetylserine sulfhydrylase.A plausible function of the prion protein: conjectures and a hypothesis.Decoding the folding of Burkholderia glumae lipase: folding intermediates en route to kinetic stabilityBiochemical mechanisms of drug action: what does it take for success?Chaperoning Anfinsen: the steric foldases.Stabilized homoserine o-succinyltransferases (MetA) or L-methionine partially recovers the growth defect in Escherichia coli lacking ATP-dependent proteases or the DnaK chaperone.Lipase-specific foldases.Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE.Proteolytic enzymes, past and future.Propeptides are sufficient to regulate organelle-specific pH-dependent activation of furin and proprotein convertase 1/3.The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stabilityFrom proteases to proteomics.Application of structural dynamic approaches provide novel insights into the enzymatic mechanism of the tumor necrosis factor-alpha-converting enzymeThe role of calcium ions in the stability and instability of a thermolysin-like protease.Investigating protein unfolding kinetics by pulse proteolysis.Propeptides as modulators of functional activity of proteases.Large-Scale Analysis of Breast Cancer-Related Conformational Changes in Proteins Using Limited Proteolysis.Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis.Identifying kinetically stable proteins with capillary electrophoresis.Group II intron folding under near-physiological conditions: collapsing to the near-native stateStructural dissection of alkaline-denatured pepsinCharacterization of a cloned subtilisin-like serine proteinase from a psychrotrophic Vibrio species.Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.Two promising alkaline β-glucosidases isolated by functional metagenomics from agricultural soil, including one showing high tolerance towards harsh detergents, oxidants and glucose.Characterization of a novel intramolecular chaperone domain conserved in endosialidases and other bacteriophage tail spike and fiber proteins.
P2860
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P2860
Kinetic stability as a mechanism for protease longevity.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Kinetic stability as a mechanism for protease longevity.
@ast
Kinetic stability as a mechanism for protease longevity.
@en
type
label
Kinetic stability as a mechanism for protease longevity.
@ast
Kinetic stability as a mechanism for protease longevity.
@en
prefLabel
Kinetic stability as a mechanism for protease longevity.
@ast
Kinetic stability as a mechanism for protease longevity.
@en
P2093
P2860
P356
P1476
Kinetic stability as a mechanism for protease longevity.
@en
P2093
Cunningham EL
P2860
P304
11008-11014
P356
10.1073/PNAS.96.20.11008
P407
P50
P577
1999-09-01T00:00:00Z