about
Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemProteolytic Activation of Human Cathepsin ACrystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase foldPhytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae.BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeastSinapate esters in brassicaceous plants: biochemistry, molecular biology, evolution and metabolic engineering.Structure determinants and substrate recognition of serine carboxypeptidase-like acyltransferases from plant secondary metabolism.Cloning of the SNG1 gene of Arabidopsis reveals a role for a serine carboxypeptidase-like protein as an acyltransferase in secondary metabolism.Competition between folding and glycosylation in the endoplasmic reticulum.The atomic model of the human protective protein/cathepsin A suggests a structural basis for galactosialidosis.Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.Biochemical characterization of sinapoylglucose:choline sinapoyltransferase, a serine carboxypeptidase-like protein that functions as an acyltransferase in plant secondary metabolism.Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlStructure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins.Cloning and characterization of the first serine carboxypeptidase from a plant parasitic nematode, Radopholus similis.Vacuolar protein sorting in fission yeast: cloning, biosynthesis, transport, and processing of carboxypeptidase Y from Schizosaccharomyces pombe.An acyltransferase catalyzing the formation of diacylglucose is a serine carboxypeptidase-like protein.Identification of the catalytic histidine residue participating in the charge-relay system of carboxypeptidase Y.Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradationExport of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.Three-Dimensional Molecular Modeling of a Diverse Range of SC Clan Serine Proteases.Htm1p-Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation.Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation systemThe application of phosphoramidate protide technology to acyclovir confers anti-HIV inhibition.Heterologous expression and characterization of CpI, OcpA, and novel serine-type carboxypeptidase OcpB from Aspergillus oryzae.Crystallization of a soluble form of the Kex1p serine carboxypeptidase from Saccharomyces cerevisiae.ProTides of BVdU as potential anticancer agents upon efficient intracellular delivery of their activated metabolitesLysosomal protective protein/cathepsin A. Role of the "linker" domain in catalytic activation.Insect midgut carboxypeptidases with emphasis on S10 hemipteran and M14 lepidopteran carboxypeptidases.Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.The specificity of carboxypeptidase Y may be altered by changing the hydrophobicity of the S'1 binding pocket.Molecular cloning of ocpO encoding carboxypeptidase O of Aspergillus oryzae IAM2640.Sub-zero temperature inactivation of carboxypeptidase Y under high hydrostatic pressure.N-terminal acetyl group is essential for the inhibitory function of carboxypeptidase Y inhibitor (I(C)).The multiple site binding of carboxypeptidase Y inhibitor (IC) to the cognate proteinase. Implications for the biological roles of the phosphatidylethanolamine-binding protein.Multiple endoplasmic reticulum-associated pathways degrade mutant yeast carboxypeptidase Y in mammalian cells.An expression and bioinformatics analysis of the Arabidopsis serine carboxypeptidase-like gene family.
P2860
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P2860
description
1994 nî lūn-bûn
@nan
1994 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
2.8-A structure of yeast serine carboxypeptidase
@ast
2.8-A structure of yeast serine carboxypeptidase
@en
2.8-A structure of yeast serine carboxypeptidase
@nl
type
label
2.8-A structure of yeast serine carboxypeptidase
@ast
2.8-A structure of yeast serine carboxypeptidase
@en
2.8-A structure of yeast serine carboxypeptidase
@nl
prefLabel
2.8-A structure of yeast serine carboxypeptidase
@ast
2.8-A structure of yeast serine carboxypeptidase
@en
2.8-A structure of yeast serine carboxypeptidase
@nl
P2093
P356
P1433
P1476
2.8-A structure of yeast serine carboxypeptidase
@en
P2093
J A Endrizzi
S J Remington
P304
P356
10.1021/BI00203A007
P407
P577
1994-09-20T00:00:00Z