Spatial orientation of glycoproteins in membranes of rat liver rough microsomes. II. Transmembrane disposition and characterization of glycoproteins.
about
Segregation of the polypeptide translocation apparatus to regions of the endoplasmic reticulum containing ribophorins and ribosomes. II. Rat liver microsomal subfractions contain equimolar amounts of ribophorins and ribosomesMechanisms for the incorporation of proteins in membranes and organelles.Recovery of ribophorins and ribosomes in "inverted rough" vesicles derived from rat liver rough microsomesAlteration of membrane barrier in stripped rough microsomes from rat liver on incubation with GTP: its relevance to the stimulation by this nucleotide of the dolichol pathway for protein glycosylation.Viral membrane proteins acquire galactose in trans Golgi cisternae during intracellular transportViral glycoproteins destined for apical or basolateral plasma membrane domains traverse the same Golgi apparatus during their intracellular transport in doubly infected Madin-Darby canine kidney cells.Biosynthesis and processing of ribophorins in the endoplasmic reticulum.Retention of membrane proteins by the endoplasmic reticulumSignals for the incorporation and orientation of cytochrome P450 in the endoplasmic reticulum membrane.Synthesis and insertion of cytochrome P-450 into endoplasmic reticulum membranesO-glycosylation of intact and truncated ribophorins in brefeldin A-treated cells: newly synthesized intact ribophorins are only transiently accessible to the relocated glycosyltransferases.3-Hydroxy-3-methylglutaryl-CoA reductase: a transmembrane glycoprotein of the endoplasmic reticulum with N-linked "high-mannose" oligosaccharides.Cytochrome P-450 membrane signals.Functional and structural characteristics of endoplasmic reticulum proteins associated with ribosome binding sites.Analytical characterization of beetroot vacuole membrane.Determination of the membrane topology of the phenobarbital-inducible rat liver cytochrome P-450 isoenzyme PB-4 using site-specific antibodies.Transmembrane disposition of the phlorizin binding protein of intestinal brush borders.Studies on membrane proteins involved in ribosome binding on the rough endoplasmic reticulum. Ribophorins have no ribosome-binding activity.Sidedness of phospholipid synthesis on brain membranes.
P2860
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P2860
Spatial orientation of glycoproteins in membranes of rat liver rough microsomes. II. Transmembrane disposition and characterization of glycoproteins.
description
1978 nî lūn-bûn
@nan
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
1978年论文
@zh
1978年论文
@zh-cn
name
Spatial orientation of glycopr ...... acterization of glycoproteins.
@ast
Spatial orientation of glycopr ...... acterization of glycoproteins.
@en
type
label
Spatial orientation of glycopr ...... acterization of glycoproteins.
@ast
Spatial orientation of glycopr ...... acterization of glycoproteins.
@en
prefLabel
Spatial orientation of glycopr ...... acterization of glycoproteins.
@ast
Spatial orientation of glycopr ...... acterization of glycoproteins.
@en
P2093
P2860
P356
P1476
Spatial orientation of glycopr ...... acterization of glycoproteins.
@en
P2093
Kreibich G
Pereyra BN
Rodriguez Boulan E
Sabatini DD
P2860
P304
P356
10.1083/JCB.78.3.894
P407
P577
1978-09-01T00:00:00Z