Results 361 to 370 of about 1,758,715 (411)
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Coat proteins in intracellular membrane transport

Current Opinion in Cell Biology, 1994
Transport of newly synthesized material from the endoplasmic reticulum (ER) towards the Golgi complex, through the Golgi cisternae, and out of the trans-Golgi network (TGN) is thought to be mediated by vesicular carriers. Different types of vesicle are involved in this biosynthetic membrane traffic.
Rainer Pepperkok, Thomas E. Kreis
openaire   +3 more sources

Coat proteins: shaping membrane transport

Nature Reviews Molecular Cell Biology, 2003
Coat proteins allow the selective transfer of macromolecules from one membrane-enclosed compartment to another by concentrating macromolecules into specialized membrane patches and then deforming these patches into small coated vesicles. Recent findings indicate that coat proteins might also participate in the differentiation of membrane domains within
Juan S. Bonifacino   +1 more
openaire   +3 more sources

Biosensors based on membrane transport proteins

Biosensors and Bioelectronics, 1991
We propose a novel class of biosensors based on membrane bound receptors or transport proteins as the sensing element. The protein is incorporated in a planar lipid bilayer which covers the transducer. The transducer may detect an electric current, a voltage, or a change in fluorescence.
York-Dieter Stierhof   +4 more
openaire   +3 more sources

Oligomeric state of membrane transport proteins analyzed with blue native electrophoresis and analytical ultracentrifugation.

Journal of Molecular Biology, 2002
Blue native electrophoresis is used widely for the analysis of non-dissociated protein complexes with respect to composition, oligomeric state and molecular mass.
E. Heuberger   +4 more
semanticscholar   +1 more source

Protein transport across the ER membrane

Trends in Biochemical Sciences, 1990
Protein transport across the endoplasmic reticulum (ER) membrane may be divided into two phases: an initiation or targeting cycle, which has been fairly well characterized, and the actual transfer of the polypeptide chain through the membrane, the mechanism of which is still unknown.
openaire   +3 more sources

Fast flip-flop of cholesterol and fatty acids in membranes: implications for membrane transport proteins.

Current Opinion in Lipidology, 2003
PURPOSE OF REVIEW The rates by which unesterified fatty acids and cholesterol move through and desorb from membranes have been difficult to measure, in part because of the simple structures of these lipids but also because methods have generally not ...
J. Hamilton
semanticscholar   +1 more source

Use of the glyceraldehyde-3-phosphate dehydrogenase promoter for production of functional mammalian membrane transport proteins in the yeast Pichia pastoris.

Biochemical and Biophysical Research Communications - BBRC, 1998
The promoter of the glyceraldehyde-3-phosphate dehydrogenase gene (PGAP) was employed to produce the mammalian peptide transporters hPEPT1 and rPEPT2 as models for polytopic transmembrane proteins in the methylotrophic yeast Prichia pastoris.
Frank Döring   +3 more
semanticscholar   +1 more source

Substrate affinities for membrane transport proteins determined by 13C cross-polarization magic-angle spinning nuclear magnetic resonance spectroscopy.

Journal of the American Chemical Society, 2004
We have devised methods in which cross-polarization magic-angle spinning (CP-MAS) solid-state NMR is exploited to measure rigorous parameters for binding of (13)C-labeled substrates to membrane transport proteins. The methods were applied to two proteins
S. G. Patching   +5 more
semanticscholar   +1 more source

Molecular dissection of membrane-transport proteins: mass spectrometry and sequence determination of the galactose-H+ symport protein, GalP, of Escherichia coli and quantitative assay of the incorporation of [ring-2-13C]histidine and (15)NH(3).

Biochemical Journal, 2002
The molecular mass of the galactose-H(+) symport protein GalP, as its histidine-tagged derivative GalP(His)(6), has been determined by electrospray MS (ESI-MS) with an error of
H. Venter   +4 more
semanticscholar   +1 more source

14-3-3 proteins in membrane protein transport

Biological Chemistry, 2006
14-3-3 proteins affect the cell surface expression of several unrelated cargo membrane proteins, e.g., MHC II invariant chain, the two-pore potassium channels KCNK3 and KCNK9, and a number of different reporter proteins exposing Arg-based endoplasmic reticulum localization signals in mammalian and yeast cells.
Mrowiec, Thomas, Schwappach, Blanche
openaire   +2 more sources

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