Protein Targeting, Transport, and TranslocationRoss Dalbey, Gunnar von Heijne Elsevier, 09/04/2002 - 336 من الصفحات Protein Targeting, Transport, and Translocation presents an in-depth overview on the topic of protein synthesis, covering all areas of protein science, including protein targeting, secretion, folding, assembly, structure, localization, quality control, degradation, and antigen presentation. Chapters also include sections on the history of the field as well as summary panels for quick reference. Numerous color illustrations complement the presentation of material. This book is an essential reference for anyone in biochemistry and protein science, as well as an excellent textbook for advanced students in these and related fields.
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الصفحة xii
... proteases, indicating that they were translocated into the lumen of the microsomal vesicles to which the added proteases had no access. Once this coupled in vitro translation–translocation system was set up, it was only a matter of time ...
... proteases, indicating that they were translocated into the lumen of the microsomal vesicles to which the added proteases had no access. Once this coupled in vitro translation–translocation system was set up, it was only a matter of time ...
الصفحة 6
... protease that removes signal sequences.The addition to a bacterial culture of carbonyl cyanide p-chlorophenylhydrazone (CCCP), an uncoupler of the membrane electrochemical potential, causes accumulation of non-translocated preproteins ...
... protease that removes signal sequences.The addition to a bacterial culture of carbonyl cyanide p-chlorophenylhydrazone (CCCP), an uncoupler of the membrane electrochemical potential, causes accumulation of non-translocated preproteins ...
الصفحة 7
... protease in spheroplasts. Cells are converted to spheroplasts by a lysozyme and osmotic shock treatment, which causes the outer membrane to peel away from the inner membrane (Osborn et al., 1972). This enables the added protease access ...
... protease in spheroplasts. Cells are converted to spheroplasts by a lysozyme and osmotic shock treatment, which causes the outer membrane to peel away from the inner membrane (Osborn et al., 1972). This enables the added protease access ...
الصفحة 8
... protease and therefore the protein can no longer be immunoprecipitated with the antibody against the epitope. A third approach involves engineering a unique protease cleavage site within the membrane protein. The protease that ...
... protease and therefore the protein can no longer be immunoprecipitated with the antibody against the epitope. A third approach involves engineering a unique protease cleavage site within the membrane protein. The protease that ...
الصفحة 9
... protease experiment with a cytoplasmic extract under conditions where the ER vesicles, termed microsomes, were intact. In these experiments, proteins translocated into the ER lumen are protease resistant; cytoplasmic proteins are protease ...
... protease experiment with a cytoplasmic extract under conditions where the ER vesicles, termed microsomes, were intact. In these experiments, proteins translocated into the ER lumen are protease resistant; cytoplasmic proteins are protease ...
المحتوى
35 | |
47 | |
74 | |
Chapter 6 Membrane Protein Insertion into Bacterial Membranes and the Endoplasmic Reticulum | 107 |
Chapter 7 Disulfide Bond Formation in Prokaryotes and Eukaryotes | 131 |
Chapter 8 The Unfolded Protein Response | 151 |
The Endoplasmic Reticulum and its Cytoplasmic Proteasome Connection | 180 |
Chapter 10 Translocation of Proteins into Mitochondria | 214 |
Chapter 12 Import of Proteins into Peroxisomes | 268 |
Chapter 13 Nucleocytoplasmic Transport | 293 |
Chapter 14 Protein Transport to the Yeast Vacuole | 322 |
Chapter 15 The Secretory Pathway | 358 |
Chapter 16 Vesicular Transport | 377 |
Chapter 17 ConclusionPerspective | 402 |
Index | 407 |
Chapter 11 The Import and Sorting of Protein into Chloroplasts | 240 |
طبعات أخرى - عرض جميع المقتطفات
عبارات ومصطلحات مألوفة
Acad Sci USA activity amino acid bacterial bilayer binding Biochem biogenesis Biol Chem Blobel brane cargo Cell Biol chaperones chloroplast cisternae clathrin co-translational compartment complex components cytoplasmic cytosolic degradation disulfide bond domain DsbA DsbC EMBO encoded endoplasmic reticulum endosome enzymes Escherichia coli eukaryotic export folding function fusion genes Golgi Görlich homolog hydrophobic importin inner membrane insertion interaction involved Ire1p isomerase kinase lipid lumen machinery matrix mediated membrane proteins misfolded mitochondrial molecular molecules mRNA mutants N-terminal nascent chain Natl Acad Sci nuclear organelle outer membrane peptidase periplasmic peroxisomal peroxisomal membrane Pex5p plasma membrane polypeptide pore precursor preprotein presequence Proc Natl Acad protease proteasome protein import protein translocation receptor residues ribosome role SecA SecB secretory pathway secretory proteins SecYEG signal peptide signal sequence structure substrate subunit synthesized teins thylakoid translocase translocon transmembrane transport unfolded proteins vacuolar vacuole vesicles vitro yeast
مقاطع مشهورة
الصفحة 46 - Biochem 133: 17-21. von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14: 4683-4690.
الصفحة 399 - R. (1980). Identification of 23 complementation groups required for posttranslational events in the yeast secretory pathway. Cell 21, 205-215.
الصفحة 319 - Robbins, J., Dilworth, SM, Laskey, RA, and Dingwall, C. (1991). Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence. Cell 64, 615-623.
الصفحة 399 - BS, and Rothman, JE (1986). A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack. Cell, 46, 171-184.
الصفحة 32 - J., 1972. Mechanism of assembly of the outer membrane of Salmonella typhimurium: Isolation and characterization of cytoplasmic and outer membrane, J.
الصفحة 238 - Schatz, G., and Dobberstein, B. (1996). Common principles of protein translocation across membranes.
الصفحة 44 - Berks, BC (1996) A common export pathway for proteins binding complex redox cofactors? Mol Microbiol 22: 393-404. Berks, BC, Sargent, F. and Palmer, T. (2000) The Tat protein export pathway. Mol Microbiol 35: 260-274.