Homologues of insulinase, a new superfamily of metalloendopeptidases.
about
Glycine-rich region of mitochondrial processing peptidase alpha-subunit is essential for binding and cleavage of the precursor proteinsDegradation of the cleaved leader peptide of thiolase by a peroxisomal proteinaseCrystal and Solution Structures of a Prokaryotic M16B Peptidase: an Open and Shut CaseCrystal structure of the cytochrome bc1 complex from bovine heart mitochondriaFusion of a fission yeastCharacterization and nucleotide sequence of pqqE and pqqF in Methylobacterium extorquens AM1The beta subunit of the mitochondrial processing peptidase from rat liver: cloning and sequencing of a cDNA and comparison with a proposed family of metallopeptidasesCharacterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay.N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes.An unusual active site identified in a family of zinc metalloendopeptidasesCellular proteolysis. An overview.Tn5-directed cloning of pqq genes from Pseudomonas fluorescens CHA0: mutational inactivation of the genes results in overproduction of the antibiotic pyoluteorin.The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.Architecture and function of metallopeptidase catalytic domains.Role of alpha-subunit of mitochondrial processing peptidase in substrate recognition.Botulinum Neurotoxins: Biology, Pharmacology, and Toxicology.Substrate specificity of the metalloproteinase pregnancy-associated plasma protein-A (PAPP-A) assessed by mutagenesis and analysis of synthetic peptides: substrate residues distant from the scissile bond are critical for proteolysisThe mitochondrial processing peptidase: function and specificity.The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain.Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes.Preparation and characterization of novel substrates of insulin proteinase (EC 3.4.99.45).Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts.Activation of a matrix processing peptidase from the crystalline cytochrome bc1 complex of bovine heart mitochondria.Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme.Catalysis, subcellular localization, expression and evolution of the targeting peptides degrading protease, AtPreP2.
P2860
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P2860
Homologues of insulinase, a new superfamily of metalloendopeptidases.
description
1991 nî lūn-bûn
@nan
1991 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
name
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@ast
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@en
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@nl
type
label
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@ast
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@en
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@nl
prefLabel
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@ast
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@en
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@nl
P2860
P356
P1433
P1476
Homologues of insulinase, a new superfamily of metalloendopeptidases.
@en
P2093
Barrett AJ
P2860
P304
P356
10.1042/BJ2750389
P407
P478
275 ( Pt 2)
P577
1991-04-01T00:00:00Z