Tryptic dissection and reconstitution of translocation activity for nascent presecretory proteins across microsomal membranes.
about
The signal recognition particle receptor is a complex that contains two distinct polypeptide chainsProtein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particleTranslocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory proteinThe Sec-dependent pathwayKinetics of endosome acidification detected by mutant and wild-type Semliki Forest virus.Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulumA microsomal GTPase is required for glycopeptide export from the mammalian endoplasmic reticulumMultiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeastMolecular cloning of a cDNA encoding the glycoprotein of hen oviduct microsomal signal peptidase.The influenza hemagglutinin precursor as an acid-sensitive probe of the biosynthetic pathway.Profile of Peter Walter.Biogenesis of the platelet receptor for fibrinogen: evidence for separate precursors for glycoproteins IIb and IIIa.Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein.Mechanisms for the incorporation of proteins in membranes and organelles.Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptorCharacterization of secretory protein translocation: ribosome-membrane interaction in endoplasmic reticulumpH-induced alterations in the fusogenic spike protein of Semliki Forest virusFormation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein.In vitro mutagenesis of trypsinogen: role of the amino terminus in intracellular protein targeting to secretory granulesDifferential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts.Competitive Inhibition of the Endoplasmic Reticulum Signal Peptidase by Non-cleavable Mutant Preprotein CargosFunctional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog.Conformational studies of the synthetic precursor-specific region of preproparathyroid hormoneThe N-terminal region of the 37-kDa translocated fragment of Pseudomonas exotoxin A aborts translocation by promoting its own export after microsomal membrane insertion.The preS1 protein of hepatitis B virus is acylated at its amino terminus with myristic acid.Constitutive apical secretion of an 80-kD sulfated glycoprotein complex in the polarized epithelial Madin-Darby canine kidney cell line.An ATP-binding membrane protein is required for protein translocation across the endoplasmic reticulum membrane.Early events in the cellular formation of proparathyroid hormone.Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum.A membrane component essential for vectorial translocation of nascent proteins across the endoplasmic reticulum: requirements for its extraction and reassociation with the membraneThe purification of M13 procoat, a membrane protein precursor.Characterization of molecules involved in protein translocation using a specific antibody.Sorting of an apical plasma membrane glycoprotein occurs before it reaches the cell surface in cultured epithelial cells.Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking.In vitro membrane assembly of a polytopic, transmembrane protein results in an enzymatically active conformationReconstitution of the fusogenic activity of vesicular stomatitis virus.Identification of signal sequence binding proteins integrated into the rough endoplasmic reticulum membrane.The budding mechanism of spikeless vesicular stomatitis virus particles.Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
P2860
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P2860
Tryptic dissection and reconstitution of translocation activity for nascent presecretory proteins across microsomal membranes.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1979
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Tryptic dissection and reconst ...... s across microsomal membranes.
@en
Tryptic dissection and reconst ...... s across microsomal membranes.
@nl
type
label
Tryptic dissection and reconst ...... s across microsomal membranes.
@en
Tryptic dissection and reconst ...... s across microsomal membranes.
@nl
prefLabel
Tryptic dissection and reconst ...... s across microsomal membranes.
@en
Tryptic dissection and reconst ...... s across microsomal membranes.
@nl
P2093
P2860
P356
P1476
Tryptic dissection and reconst ...... s across microsomal membranes.
@en
P2093
Jackson RC
Lingappa VR
P2860
P304
P356
10.1073/PNAS.76.4.1795
P407
P577
1979-04-01T00:00:00Z