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 7
... residues long) uncharged peptides into the periplasmic loops, which function as epitopes for antibodies (Konninger et al., 1999). Immunoprecipitation assays, together with protease-mapping studies, can then determine whether a given ...
... residues long) uncharged peptides into the periplasmic loops, which function as epitopes for antibodies (Konninger et al., 1999). Immunoprecipitation assays, together with protease-mapping studies, can then determine whether a given ...
الصفحة 9
... residues of invertase, prior to radioactive labeling, leads to the appearance of 58kDa invertase precursor species. This species corresponds to the non-glycosylated mature protein with the leader sequence intact. Later studies showed ...
... residues of invertase, prior to radioactive labeling, leads to the appearance of 58kDa invertase precursor species. This species corresponds to the non-glycosylated mature protein with the leader sequence intact. Later studies showed ...
الصفحة 10
... residues, is transferred from dolichol phosphate to the asparagine (Asn) residues of the growing polypeptide in the lumen of the ER. The glucosidase I and II, which remove the glucose residues of the N-linked core oligosaccharide, are ...
... residues, is transferred from dolichol phosphate to the asparagine (Asn) residues of the growing polypeptide in the lumen of the ER. The glucosidase I and II, which remove the glucose residues of the N-linked core oligosaccharide, are ...
الصفحة 22
... residues long since 35 to 40 residues are within the polypeptide channel of the ribosome. Such crosslinking experiments showed that the signal sequence interacts with the SRP 54 kDa subunit of SRP in the eukaryotic system (Krieg et al ...
... residues long since 35 to 40 residues are within the polypeptide channel of the ribosome. Such crosslinking experiments showed that the signal sequence interacts with the SRP 54 kDa subunit of SRP in the eukaryotic system (Krieg et al ...
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.