The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo.
about
Impact of pro segments on the folding and function of human neutrophil alpha-defensinsAn amino-terminal domain of the hepatitis C virus NS3 protease is essential for interaction with NS4ABoth NS3 and NS4A are required for proteolytic processing of hepatitis C virus nonstructural proteinsCrystal structure of unautoprocessed precursor of subtilisin from a hyperthermophilic archaeon: evidence for Ca2+-induced foldingStructural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1Structure of a protein in a kinetic trapStructure of alpha-lytic protease complexed with its pro regionRegulation of transcription factor latency by receptor-activated proteolysis.The complete general secretory pathway in gram-negative bacteriaUnfolding studies of Escherichia coli maltodextrin glucosidase monitored by fluorescence spectroscopy.The alphabet of intrinsic disorder: II. Various roles of glutamic acid in ordered and intrinsically disordered proteins.Disabling the folding catalyst is the last critical step in alpha-lytic protease foldingA nine-residue synthetic propeptide enhances secretion efficiency of heterologous proteins in Lactococcus lactisCoupled site-directed mutagenesis/transgenesis identifies important functional domains of the mouse agouti proteinIdentification of a cytoplasm to vacuole targeting determinant in aminopeptidase IAmino acid substitutions influencing intracellular protein folding pathways.The Kex2p proregion is essential for the biosynthesis of an active enzyme and requires a C-terminal basic residue for its function.Ca2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: the propeptide is a potent inhibitor of the mature domain but is not required for its foldingInsights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furinImmunological approaches as therapy for Alzheimer's disease.Reassembly of active caspase-3 is facilitated by the propeptide.Novel mechanisms control the folding and assembly of lambda5/14.1 and VpreB to produce an intact surrogate light chain.Molecular characterization of a gene encoding extracellular serine protease isolated from a subtilisin inhibitor-deficient mutant of Streptomyces albogriseolus S-3253Polyanions and the proteome.Recombinant expression and antigenic properties of a 32-kilodalton extracellular alkaline protease, representing a possible virulence factor from Aspergillus fumigatus.Two conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF.Kinetic stability as a mechanism for protease longevity.Activation of a bacterial lipase by its chaperoneCrystallization and preliminary X-ray diffraction study of an active-site mutant of pro-Tk-subtilisin from a hyperthermophilic archaeonPosttranslational processing of the prohormone-cleaving Kex2 protease in the Saccharomyces cerevisiae secretory pathwaypH-induced conformational transitions of a molten-globule-like state of the inhibitory prodomain of furin: implications for zymogen activation.Alpha-crystallin binds to the aggregation-prone molten-globule state of alkaline protease: implications for preventing irreversible thermal denaturation.Protein secretion in Bacillus species.Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymesPropeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity.The role of calcium ions in the stability and instability of a thermolysin-like protease.A posttranslationally regulated protease, VheA, is involved in the liberation of juveniles from parental spheroids in Volvox carteri.Propeptides as modulators of functional activity of proteases.Streptomyces griseus protease B: secretion correlates with the length of the propeptide.Specific inhibition of mature fungal serine proteinases and metalloproteinases by their propeptides.
P2860
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P2860
The alpha-lytic protease pro-region does not require a physical linkage to activate the protease domain in vivo.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
The alpha-lytic protease pro-r ...... e the protease domain in vivo.
@en
The alpha-lytic protease pro-r ...... e the protease domain in vivo.
@nl
type
label
The alpha-lytic protease pro-r ...... e the protease domain in vivo.
@en
The alpha-lytic protease pro-r ...... e the protease domain in vivo.
@nl
prefLabel
The alpha-lytic protease pro-r ...... e the protease domain in vivo.
@en
The alpha-lytic protease pro-r ...... e the protease domain in vivo.
@nl
P356
P1433
P1476
The alpha-lytic protease pro-r ...... e the protease domain in vivo.
@en
P2093
P2888
P304
P356
10.1038/341462A0
P407
P577
1989-10-01T00:00:00Z
P6179
1013071806