Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum. - Wikidata - wikimedia - TriplyDB

Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum.

Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum.

http://www.wikidata.org/entity/Q36358019

about

Signal recognition particle mediates post-translational targeting in eukaryotes The yeast N(alpha)-acetyltransferase NatA is quantitatively anchored to the ribosome and interacts with nascent polypeptides The similarity between N-terminal targeting signals for protein import into different organelles and its evolutionary relevance Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.A functional chaperone triad on the yeast ribosome Hph1p and Hph2p, novel components of calcineurin-mediated stress responses in Saccharomyces cerevisiae.Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis.Chaperonins facilitate KNOTTED1 cell-to-cell trafficking and stem cell function.Enzymatic blockade of the ubiquitin-proteasome pathway N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum Towards a functional understanding of protein N-terminal acetylation Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence.Suppression of a defect in mitochondrial protein import identifies cytosolic proteins required for viability of yeast cells lacking mitochondrial DNA.Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational regulation.A calmodulin-dependent translocation pathway for small secretory proteins Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).Proteasomal degradation of preemptive quality control (pQC) substrates is mediated by an AIRAPL-p97 complex.Dendritic cells, DRiPs, and DALIS in the control of antigen processing.The Protease Ste24 Clears Clogged Translocons Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER)A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel.Interrelation between protein synthesis, proteostasis and life span A portrait of the GET pathway as a surprisingly complicated young man.The secretory pathway: exploring yeast diversity.All roads lead to Rome (but some may be harder to travel): SRP-independent translocation into the endoplasmic reticulum.The Brl domain in Sec63p is required for assembly of functional endoplasmic reticulum translocons.Identification of antibody-interacting proteins that contribute to the production of recombinant antibody in mammalian cells.Regulation of GPCR expression through an interaction with CCT7, a subunit of the CCT/TRiC complex.Post-translational secretion of fusion proteins in the halophilic archaea Haloferax volcanii.Roles of cytosolic Hsp70 and Hsp40 molecular chaperones in post-translational translocation of presecretory proteins into the endoplasmic reticulum.Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides.The role of T-cell reactivity towards the autoantigen α-NAC in atopic dermatitis.Mutations in the Sec61p Channel Affecting Signal Sequence Recognition and Membrane Protein Topology

P2860

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P2860

Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum.

http://www.wikidata.org/entity/Q36358019

description

2000 nî lūn-bûn

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2000年の論文

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年学术文章

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2000年學術文章

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2000年學術文章

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2000年學術文章

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name

Spontaneous release of cytosol ...... nto the endoplasmic reticulum.

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Spontaneous release of cytosol ...... nto the endoplasmic reticulum.

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Spontaneous release of cytosol ...... nto the endoplasmic reticulum.

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Spontaneous release of cytosol ...... nto the endoplasmic reticulum.

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Journal of Cell Biology

P1476

Spontaneous release of cytosol ...... nto the endoplasmic reticulum.

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P2860

A protein complex required for signal-sequence-specific sorting and translocation

Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells

Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins

BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane.

Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo.

The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.

Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.

YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism.

Residues in chaperonin GroEL required for polypeptide binding and release

Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast

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167-178

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scholarly article

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10.1083/JCB.151.1.167

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1

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151

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11018062

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endoplasmic reticulum

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2189806

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