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Crystal structure of the precursor of galactose oxidase: An unusual self-processing enzymeCrystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of foldingRegulation of an intracellular subtilisin protease activity by a short propeptide sequence through an original combined dual mechanismIncrease in activation rate of Pro-Tk-subtilisin by a single nonpolar-to-polar amino acid substitution at the hydrophobic core of the propeptide domainThe discovery of new cyanobactins from Cyanothece PCC 7425 defines a new signature for processing of patellamidesAccelerated maturation of Tk-subtilisin by a Leu→Pro mutation at the C-terminus of the propeptide, which reduces the binding of the propeptide to Tk-subtilisinProteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagenExon 6 of human Jagged-1 encodes an autonomously folding unitRecombining low homology, functionally rich regions of bacterial subtilisins by combinatorial fragment exchangeThe Epichloë festucae antifungal protein has activity against the plant pathogen Sclerotinia homoeocarpa, the causal agent of dollar spot disease.HreP, an in vivo-expressed protease of Yersinia enterocolitica, is a new member of the family of subtilisin/kexin-like proteasesThe Kex2p proregion is essential for the biosynthesis of an active enzyme and requires a C-terminal basic residue for its function.Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furinPapD-like chaperones provide the missing information for folding of pilin proteins.Conserved prosegment residues stabilize a late-stage folding transition state of pepsin independently of ground states.Dynamics of thermodynamically stable, kinetically trapped, and inhibitor-bound states of pepsinThe non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the fThe order of expression is a key factor in the production of active transglutaminase in Escherichia coli by co-expression with its pro-peptide.Structural and Functional Characterization of the Major Allergen Amb a 11 from Short Ragweed PollenThe role of calcium ions in the stability and instability of a thermolysin-like protease.BRICHOS domain associated with lung fibrosis, dementia and cancer--a chaperone that prevents amyloid fibril formation?Biotechnological applications of transglutaminasesMolecular characterization of cycloinulooligosaccharide fructanotransferase from Bacillus maceransPropeptides as modulators of functional activity of proteases.A novel subtilase inhibitor in plants shows structural and functional similarities to protease propeptides.Partial characterization of an enzyme fraction with protease activity which converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores and analysis of a gene cluster involStreptomyces griseus protease B: secretion correlates with the length of the propeptide.The protein encoded at the 3' end of the serine protease gene of Aeromonas sobria functions as a chaperone in the production of the protease.Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-Like protease from Streptomyces albogriseolus.A propeptide-independent protease from Tannerella sp.6_1_58FAA_CT1 displays trypsin-like specificity.The role of substrate specificity and metal binding in defining the activity and structure of an intracellular subtilisin.The glycan domain of thrombopoietin (TPO) acts in trans to enhance secretion of the hormone and other cytokines.Processing of lysosomal beta-galactosidase. The C-terminal precursor fragment is an essential domain of the mature enzyme.Functional Characterization of Propeptides in Plant Subtilases as Intramolecular Chaperones and Inhibitors of the Mature Protease.Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria.Understanding the mechanism of prosegment-catalyzed folding by solution NMR spectroscopy.Structural dissection of alkaline-denatured pepsinThe CXC motif: a functional mimic of protein disulfide isomerase.Specific inhibition and stabilization of aspergilloglutamic peptidase by the propeptide. Identification of critical sequences and residues in the propeptide.Expression of lignin peroxidase H8 in Escherichia coli: folding and activation of the recombinant enzyme with Ca2+ and haem.
P2860
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P2860
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Pro-sequence-assisted protein folding.
@en
type
label
Pro-sequence-assisted protein folding.
@en
prefLabel
Pro-sequence-assisted protein folding.
@en
P2860
P1476
Pro-sequence-assisted protein folding.
@en
P2093
P2860
P304
P356
10.1111/J.1365-2958.1995.TB02423.X
P407
P50
P577
1995-05-01T00:00:00Z