Yeast carboxypeptidase Y can be translocated and glycosylated without its amino-terminal signal sequence.
about
The fungal vacuole: composition, function, and biogenesisSec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex.Functional differences in yeast protein disulfide isomerases.Proteomics and glycomics analyses of N-glycosylated structures involved in Toxoplasma gondii--host cell interactions.Efficiency and diversity of protein localization by random signal sequencesN-terminal acetylation inhibits protein targeting to the endoplasmic reticulumA nucleus-based quality control mechanism for cytosolic proteinsVacuolar protein sorting in fission yeast: cloning, biosynthesis, transport, and processing of carboxypeptidase Y from Schizosaccharomyces pombe.Protein-specific features of the general secretion pathway in yeast: the secretion of acid phosphatase.Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent.Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids.Signal sequences specify the targeting route to the endoplasmic reticulum membraneThe BOS1 gene encodes an essential 27-kD putative membrane protein that is required for vesicular transport from the ER to the Golgi complex in yeastA mutation in the signal recognition particle 7S RNA of the yeast Yarrowia lipolytica preferentially affects synthesis of the alkaline extracellular protease: in vivo evidence for translational arrestCassette mutagenic analysis of the yeast invertase signal peptide: effects on protein translocation.Single-amino-acid substitutions within the signal sequence of yeast prepro-alpha-factor affect membrane translocationIntracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting informationMutations in the signal sequence of prepro-alpha-factor inhibit both translocation into the endoplasmic reticulum and processing by signal peptidase in yeast cells.The yeast acid phosphatase can enter the secretory pathway without its N-terminal signal sequence.Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity.Analysis of the glycoproteome of Toxoplasma gondii using lectin affinity chromatography and tandem mass spectrometry.Intracellular transport in interphase and mitotic yeast cells.An amino-terminal deletion mutation of pseudorabies virus glycoprotein gIII affects protein localization and RNA accumulation.Expression of a functionally active human hepatic UDP-glucuronosyltransferase (UGT1A6) lacking the N-terminal signal sequence in the endoplasmic reticulum.In vivo and in vitro analysis of ptl1, a yeast ts mutant with a membrane-associated defect in protein translocationThe vacuolar protein-targeting signal of yeast carboxypeptidase is functional in oocytes from Xenopus laevis.Heteroloaous expression of yeast prepro‐a‐factor in rat GH3cells
P2860
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P2860
Yeast carboxypeptidase Y can be translocated and glycosylated without its amino-terminal signal sequence.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
1987年论文
@zh
1987年论文
@zh-cn
name
Yeast carboxypeptidase Y can b ...... mino-terminal signal sequence.
@ast
Yeast carboxypeptidase Y can b ...... mino-terminal signal sequence.
@en
type
label
Yeast carboxypeptidase Y can b ...... mino-terminal signal sequence.
@ast
Yeast carboxypeptidase Y can b ...... mino-terminal signal sequence.
@en
prefLabel
Yeast carboxypeptidase Y can b ...... mino-terminal signal sequence.
@ast
Yeast carboxypeptidase Y can b ...... mino-terminal signal sequence.
@en
P2860
P356
P1476
Yeast carboxypeptidase Y can b ...... mino-terminal signal sequence.
@en
P2093
E Blachly-Dyson
T H Stevens
P2860
P304
P356
10.1083/JCB.104.5.1183
P407
P577
1987-05-01T00:00:00Z