Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution
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Mechanism of activation of the gastric aspartic proteinases: pepsinogen, progastricsin and prochymosinThe cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene familyStructure of human procathepsin L reveals the molecular basis of inhibition by the prosegmentThe fungal vacuole: composition, function, and biogenesisMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesStructural Insights into the Activation and Inhibition of Histo-Aspartic Protease from Plasmodium falciparumHigh-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzymeX-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsinCrystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptideConformational switching in an aspartic proteinaseRole of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase.The Saccharomyces cerevisiae BAR1 gene encodes an exported protein with homology to pepsin.Activation of cathepsin B, secreted by a colorectal cancer cell line requires low pH and is mediated by cathepsin DCharacterization of rat cathepsin E and mutants with changed active-site residues and lacking propeptides and N-glycosylation, expressed in human embryonic kidney 293T cellsCloning, expression and characterisation of murine procathepsin EPurification, cloning and autoproteolytic processing of an aspartic proteinase from Centaurea calcitrapa.Structural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursorsA bipartite membrane-binding signal in the human immunodeficiency virus type 1 matrix protein is required for the proteolytic processing of Gag precursors in a cell type-dependent mannerPEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors.Activation of human pepsinogens.The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum.Multiple functions of pro-parts of aspartic proteinase zymogens.The effects of pK(a) tuning on the thermodynamics and kinetics of folding: design of a solvent-shielded carboxylate pair at the a-position of a coiled-coilStructural studies of vacuolar plasmepsinsMolecular analysis of the feline immunodeficiency virus protease: generation of a novel form of the protease by autoproteolysis and construction of cleavage-resistant proteases.Two conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF.Acidification of the lysosome-like vacuole and the vacuolar H+-ATPase are deficient in two yeast mutants that fail to sort vacuolar proteinsHow similar are enzyme active site geometries derived from quantum mechanical theozymes to crystal structures of enzyme-inhibitor complexes? Implications for enzyme design.The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases.Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting informationThe molecular biology of human renin and its gene.Deletion of sequences upstream of the proteinase improves the proteolytic processing of human immunodeficiency virus type 1.Identification of the major pregnancy-specific antigens of cattle and sheep as inactive members of the aspartic proteinase family.Progastriscin: structure, function, and its role in tumor progression.The sole lysine residue in porcine pepsin works as a key residue for catalysis and conformational flexibility.Autoprocessing: an essential step for the activation of HIV-1 protease.Naturally-occurring and recombinant forms of the aspartic proteinases plasmepsins I and II from the human malaria parasite Plasmodium falciparum.Intramolecular inhibition of human defensin HNP-1 by its propiece.Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag-Pol influence PR autoprocessingA study into the effects of protein binding on nucleotide conformation
P2860
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P2860
Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 A resolution
description
1986 nî lūn-bûn
@nan
1986 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@ast
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@en
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@nl
type
label
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@ast
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@en
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@nl
prefLabel
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@ast
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@en
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@nl
P356
P1433
P1476
Molecular structure of an aspa ...... epsinogen, at 1.8 A resolution
@en
P2093
A R Sielecki
P2888
P356
10.1038/319033A0
P407
P577
1986-01-01T00:00:00Z
P6179
1026967260