Titlebook: Endoplasmic Reticulum; N. Borgese,J. R. Harris Book 1993 Springer Science+Business Media New York 1993 Lipid.Organe.Regulation.Translation

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osteocytes

Phospholipid Translocation in the Endoplasmic Reticulum, 20 years. The conclusions appear relatively consistent in the case of the plasma membrane of eukaryotes, for which it is admitted that phospholipids are organized in an asymmetrical bilayer. The existence of the bilayer was inferred from X-ray diffraction studies as well as .P-NMR and freeze-fractu

TATE

Cytochrome P-450 in the Endoplasmic Reticulum Biosynthesis, Distribution, Induction, and Degradatioanes of various cells and function in the metabolism of a wide variety of exogenous compounds such as drugs and chemical carcinogens and endogenous ones such as steroids, fatty acids, and retinoids (Porter and Coon, 1991). Various P-450 forms have been characterized by their specific, but overlappin

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NADH-Cytochrome b5 Reductase and Cytochrome b5 the Problem of Posttranslational Targeting to the Enctive site and only a small lumenal domain (or possibly no lumenal amino acid residues at all) so that large portions of their polypeptide chain must not be translocated across the ER membrane. The biosynthesis of this class of proteins, their mechanism of targeting to the ER and of correct insertio

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Synapse

Folding, Assembly, and Posttranslational Modification of Proteins within the Lumen of the Endoplasm pathway, are usually fully folded, as judged by their biological activity and recognition by conformation-specific antibodies. Indeed, correct folding and assembly is the major criterion used by the “quality control” system that selectively permits exit of secretory and cell-surface proteins from t

Anguish

Biological Functions and Biosynthesis of Glycolipid-Anchored Membrane Proteins,to function is, however, difficult to generalize. For example, GPI-anchored class I histocompatibility antigens do appear to gain access to much of the cell surface (Edidin and Stroynowski, 1991), although their lateral diffusion is not uniformly higher than for transmembrane proteins (Bulow ., 1988

initiate

Friction

Antigen Processing and Presentation the Role of the Endoplasmic Reticulum, the major histocompatibility complex (MHC). Processing of target proteins occurs through two distinct pathways. Exogenous proteins are degraded in an endolysosome compartment, which intersects the biosynthetic pathway of MHC class II molecules (Neefjes ., 1990). Thus, peptides derived from degradat

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https://doi.org/10.1007/978-1-4302-6569-6 pathway, are usually fully folded, as judged by their biological activity and recognition by conformation-specific antibodies. Indeed, correct folding and assembly is the major criterion used by the “quality control” system that selectively permits exit of secretory and cell-surface proteins from t