Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae.
about
The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae.The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities.S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase.Molecular cloning and expression of rat brain endopeptidase 3.4.24.16Families of zinc metalloproteases.(+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase.Evidence for a Zn(2+)-binding site in human serum butyrylcholinesterase.A metalloproteinase extracellularly released by Crithidia deanei.Mammalian microsomal and soluble Ras-processing peptidase activities are distinct.
P2860
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P2860
Purification and characterization of a novel metalloendopeptidase from Saccharomyces cerevisiae.
description
1993 nî lūn-bûn
@nan
1993 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Purification and characterizat ...... from Saccharomyces cerevisiae.
@ast
Purification and characterizat ...... from Saccharomyces cerevisiae.
@en
Purification and characterizat ...... from Saccharomyces cerevisiae.
@nl
type
label
Purification and characterizat ...... from Saccharomyces cerevisiae.
@ast
Purification and characterizat ...... from Saccharomyces cerevisiae.
@en
Purification and characterizat ...... from Saccharomyces cerevisiae.
@nl
prefLabel
Purification and characterizat ...... from Saccharomyces cerevisiae.
@ast
Purification and characterizat ...... from Saccharomyces cerevisiae.
@en
Purification and characterizat ...... from Saccharomyces cerevisiae.
@nl
P356
P1433
P1476
Purification and characterizat ...... from Saccharomyces cerevisiae.
@en
P2093
P304
P356
10.1021/BI00093A005
P407
P577
1993-10-26T00:00:00Z