Topology of P-glycoproteins. (Q48933765)

17 February 2018

title

Topology of P-glycoproteins. (English)

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17 February 2018

author name string

Skach WR

series ordinal

1

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17 February 2018

language of work or name

English

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publication date

1 January 1998

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17 February 2018

published in

Methods in Enzymology

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17 February 2018

volume

292

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17 February 2018

page(s)

265-278

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17 February 2018

Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence

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Multidrug resistance protein (Mdr)-alkaline phosphatase hybrids in Escherichia coli suggest a major revision in the topology of the C-terminal half of Mdr.

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Mechanism of protein translocation across the endoplasmic reticulum membrane

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Bovine opsin has more than one signal sequence.

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Structural requirements for membrane assembly of proteins spanning the membrane several times

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Insertion of a multispanning membrane protein occurs sequentially and requires only one signal sequence

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The erythrocyte anion transport protein is contranslationally inserted into microsomes

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Involvement of cytoplasmic factors regulating the membrane orientation of P-glycoprotein sequences

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Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components

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Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma

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Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus

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Distinct biogenesis mechanisms for the water channels MIWC and CHIP28 at the endoplasmic reticulum

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Membrane protein spanning segments as export signals

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Efficientin vitrosynthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter

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A former amino terminal signal sequence engineered to an internal location directs translocation of both flanking protein domains

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A stop transfer sequence confers predictable transmembrane orientation to a previously secreted protein in cell-free systems

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[4] Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA

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Preparation of microsomal membranes for cotranslational protein translocation.

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Asparagine-linked oligosaccharides are localized to single extracytosolic segments in multi-span membrane glycoproteins

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Identification of a translocated protein segment in a voltage-dependent channel

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SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

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Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation

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Unusual topogenic sequence directs prion protein biogenesis

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10.1016/S0076-6879(98)92021-3

Identifiers

DOI

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17 February 2018

PubMed ID

9711560

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17 February 2018