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 12
... secB mutant did not show a temperature-sensitive phenotype and, in fact, a null secB E. coli mutant was viable in minimal media where protein synthesis is slower and therefore the need for SecB is reduced. Similar approaches using LacZ ...
... secB mutant did not show a temperature-sensitive phenotype and, in fact, a null secB E. coli mutant was viable in minimal media where protein synthesis is slower and therefore the need for SecB is reduced. Similar approaches using LacZ ...
الصفحة 14
... secB 81 Export chaperone Non-essential on 16.6 kDa minimal media; export defect for certain proteins secD 9.5 67 kDa inner c.s. lethal export membrane protein defect secE 90 13.6 kDa inner c.s. lethal export (prlG) membrane protein ...
... secB 81 Export chaperone Non-essential on 16.6 kDa minimal media; export defect for certain proteins secD 9.5 67 kDa inner c.s. lethal export membrane protein defect secE 90 13.6 kDa inner c.s. lethal export (prlG) membrane protein ...
الصفحة 20
... SecB functions (Hartlet al., 1990). [125I]-SecB binds with high affinity to inner membrane vesicles containing SecA; additionally, [125I]-proOmpA binds to vesicles with high affinity in a SecB-dependent manner. This shows that SecB ...
... SecB functions (Hartlet al., 1990). [125I]-SecB binds with high affinity to inner membrane vesicles containing SecA; additionally, [125I]-proOmpA binds to vesicles with high affinity in a SecB-dependent manner. This shows that SecB ...
الصفحة 29
... SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor. EMBO J19:134–143. Bedouelle, H., Bassford, P.J., Jr., Fowler, A.V. et al. (1980) Mutations which alter the function of the signal ...
... SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor. EMBO J19:134–143. Bedouelle, H., Bassford, P.J., Jr., Fowler, A.V. et al. (1980) Mutations which alter the function of the signal ...
الصفحة 31
... SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 63:269–279. Herman, P.K., Stack, J.H., DeModena, J.A. and Emr, S.D. (1991) A novel protein kinase homolog essential for protein sorting to the ...
... SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane. Cell 63:269–279. Herman, P.K., Stack, J.H., DeModena, J.A. and Emr, S.D. (1991) A novel protein kinase homolog essential for protein sorting to the ...
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.