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Role of Magmas in protein transport and human mitochondria biogenesisA new chloroplast protein import intermediate reveals distinct translocation machineries in the two envelope membranes: energetics and mechanistic implicationsMAS5, a yeast homolog of DnaJ involved in mitochondrial protein import.Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria.Biogenesis of mitochondrial heme lyases in yeast. Import and folding in the intermembrane space.Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix.A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viabilityThe mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.Protein unfolding by mitochondria. The Hsp70 import motorRole of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocationSequential action of two hsp70 complexes during protein import into mitochondriaTranslocation can drive the unfolding of a preprotein domain.Strong precursor-pore interactions constrain models for mitochondrial protein importProtein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix.Transport of proteins into the various subcompartments of mitochondria.Secretion of nuclease across the outer membrane of Serratia marcescens and its energy requirements.Two distinct mechanisms drive protein translocation across the mitochondrial outer membrane in the late step of the cytochrome b(2) import pathway.Sequential action of mitochondrial chaperones in protein import into the matrixOverexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation.Intramitochondrial sorting of the precursor to yeast cytochrome c oxidase subunit Va.A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins.Involvement of 70-kD heat-shock proteins in peroxisomal import.Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP.The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysisCo-operative binding of hsp60 may promote transfer from hsp70 and correct folding of imported proteins in mitochondria [corrected]Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteinsStress-induced transcriptional activation.A 69 kDa immunodominant antigen of Trypanosoma (Nannomonas) congolense is homologous to immunoglobulin heavy chain binding protein (BiP).The two mammalian mitochondrial stress proteins, grp 75 and hsp 58, transiently interact with newly synthesized mitochondrial proteins.Carbonyl reductases and pluripotent hydroxysteroid dehydrogenases of the short-chain dehydrogenase/reductase superfamily.Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria.Secretory protein biogenesis and traffic in the early secretory pathwayTight knots in proteins: can they block the mitochondrial pores?Unfolding of preproteins upon import into mitochondria.Peptides fused to the amino-terminal end of diphtheria toxin are translocated to the cytosolA bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein.Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small tom proteins, and import receptors.Overexpression of protein disulfide isomerase DsbC stabilizes multiple-disulfide-bonded recombinant protein produced and transported to the periplasm in Escherichia coli.
P2860
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P2860
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
@zh-cn
1990年学术文章
@zh-hans
1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
@yue
1990年學術文章
@zh
1990年學術文章
@zh-hant
name
How do polypeptides cross the mitochondrial membranes?
@en
How do polypeptides cross the mitochondrial membranes?
@nl
type
label
How do polypeptides cross the mitochondrial membranes?
@en
How do polypeptides cross the mitochondrial membranes?
@nl
prefLabel
How do polypeptides cross the mitochondrial membranes?
@en
How do polypeptides cross the mitochondrial membranes?
@nl
P2093
P1433
P1476
How do polypeptides cross the mitochondrial membranes?
@en
P2093
P304
P356
10.1016/0092-8674(90)90437-J
P407
P577
1990-11-01T00:00:00Z