Crossref
journal-article
Elsevier BV
Current Opinion in Cell Biology (78)
References
45
Referenced
137
10.1126/science.2538923
/ Science / A Multiubiquitin Chain is Confined to Specific Lysine in a Targeted Short-lived Protein by Chau (1989)10.1016/0092-8674(90)90104-M
/ Cell / Protein Degradation in the Endoplasmic Reticulum by Klausner (1990)10.1146/annurev.cb.05.110189.001425
/ Annu Rev Cell Biol / Protein Oligomerization in the Endoplasmic Reticulum by Hurtley (1989)10.1146/annurev.cb.06.110190.002155
/ Annu Rev Cell Biol / The T Cell Antigen Receptor: Insights into Organelle Biology by Klausner (1990)10.1016/0092-8674(88)90553-3
/ Cell / Degradation from the Endoplasmic Reticulum: Disposing of Newly Synthesized Proteins by Lippincott-Schwartz (1988)10.1083/jcb.107.6.2149
/ J Cell Biol / Selective Degradation of T Cell Antigen Receptor Chains Retained in a Pre-Golgi Compartment by Chen (1988)10.1083/jcb.109.1.73
/ J Cell Biol / Pre-Golgi Degradation of Newly Synthesized T-Cell Antigen Receptor Chains: Intrinsic Sensitivity and the Role of Subunit Assembly by Bonifacino (1989)10.1093/intimm/2.8.743
/ Int Immunol / Recognition for Degradation in the Endoplasmic Reticulum and Lysosomes Prevents the Transport of Single TCRβ and CD3δ Subunits of the T-Cell Antigen Receptor to the Surface of Cells by Wileman (1990)10.1083/jcb.108.5.1647
/ J Cell Biol / The Propertide of Preprosomatostatin Mediates Intracellular Transport and Secretion of α-Globin from Mammalian Cells by Stoller (1989)10.1002/j.1460-2075.1987.tb02739.x
/ EMBO J / Regulation of Membrane IgM Expression in Secretory B Cells: Translational and Post-Translational Events by Sitia (1987)10.1016/S0021-9258(19)30090-0
/ J Biol Chem / A Frameshift Mutation in a Patient with Tay-Sachs Disease Causes Premature termination and Defective Intracellular Transport of the α-Subunit of β-Hexosaminidase by Lau (1989)10.1126/science.2294595
/ Science / A Peptide Sequence Confers Retention and Rapid Degradation Within the Endoplasmic Reticulum by Bonifacino (1990)10.1016/0092-8674(90)90447-M
/ Cell / Colocalized Transmembrane Determinants for ER Degradation and Subunit Assembly Explain the Intracellular Fate of TCR Chains by Bonifacino (1990)10.1091/mbc.1.12.907
/ Cell Regulation / The Transmembrane Anchor of the T-Cell Antigen Receptor β Chain Contains a Structural Determinant of Pre-Golgi Proteolysis by Wileman (1990)10.1002/j.1460-2075.1991.tb07827.x
/ EMBO J / Role of Potentially Charged Residues in Targeting Proteins for Retention and Degradation Within the Endoplasmic Reticulum by Bonifacino (1991)10.1016/S0021-9258(19)69144-1
/ J Biol Chem / Evidence Indicating that Inactivation of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase by Low Density Lipoprotein or by 25-Hydroxycholesterol Requires Mediator Protein(s) with Rapid Turnover Rate by Chang (1981){'key': '10.1016/0955-0674(91)90028-W_BIB17', 'first-page': '5205', 'article-title': 'Regulation of Synthesis and Degradation of Rat Liver 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase by Low Density Lipoprotein and 25-Hydroxycholesterol in UT-1 cells', 'volume': '79', 'author': 'Faust', 'year': '1982'}
/ Regulation of Synthesis and Degradation of Rat Liver 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase by Low Density Lipoprotein and 25-Hydroxycholesterol in UT-1 cells by Faust (1982)10.1016/S0021-9258(18)89764-2
/ J Biol Chem / Domain Structure of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase, a Glycoprotein of the Endoplasmic Reticulum by Liscum (1985)10.1016/0092-8674(85)90078-9
/ Cell / Membrane-Bound Domain of HMG CoA Reductase is Required for Sterol-Enhanced Degradation of the Enzyme by Gil (1985)10.1016/S0021-9258(18)68719-8
/ J Biol Chem / The Membrane Domain of 3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase Confers Endoplasmic Reticulum Localization and Sterol-Regulated Degradation onto β-Galactosidase by Skalnik (1988)10.1083/jcb.104.6.1693
/ J Cell Biol / Partial Deletion of Membrane-Bound Domain of 3-Hydroxy-3-Methylglutaryl Coenzyme A Reductase Eliminates Sterol-Enhanced Degradation and Prevents Formation of Crystalloid Endoplasmic Reticulum by Jingami (1987)10.1016/S0021-9258(17)35306-1
/ J Biol Chem / An Alternatively Spliced Miniexon Alters the Subcellular Fate of the Human Asialoglycoprotein Receptor H2 Subunit. Endoplasmic Reticulum Retention and Degradation or Cell Surface Expression by Lederkremer (1991)10.1083/jcb.109.6.3315
/ J Cell Biol / Intracellular Degradation of Unassembled Asiaglycoprotein Receptor Subunit: a Pre-Golgi, Nonlysosomal Endoproteolytic Cleavage by Amara (1989)10.1016/S0022-2275(20)38269-9
/ J Lipid Res / Intrahepatic Assembly of Very Low-density Lipoproteins: Immunologic Characterization of Apolipoprotein B in Lipoproteins and Hepatic Membrane Fractions and its Intracellular Distribution by Davis (1989)10.1016/S0021-9258(19)38481-9
/ J Biol Chem / Degradation of Newly Synthesized Apolipoprotein B100 in a Pre-Golgi Compartment by Sato (1990)10.1016/S0021-9258(18)45839-5
/ J Biol Chem / The Regulated Degradation of 3-Hydroxy-3-Methylglutaryl-CoA Reductase Requires a Short-Lived Protein and Occurs in the Endoplasmic Reticulum by Chun (1990)10.1016/S0021-9258(19)38770-8
/ J Biol Chem / Apolipoprotein B is Both Integrated and Translocated Across the Endoplasmic Reticulum Membrane. Evidence for Two Functionally Distinct Pools by Davis (1990)10.1038/346382a0
/ Nature / New Variation on the Translocation of Proteins During Early Biogenesis of Apolipoprotein by Chuck (1990)10.1016/0092-8674(91)90506-T
/ Cell / MHC Class II-Restricted Presentation of Intracellular Antigen by Weiss (1991)10.1126/science.2142801
/ Science / Transmembrane Helical Interactions and the Assembly of the T Cell Receptor Complex by Manolios (1990)10.1038/351414a0
/ Nature / Membrane Protein Association by Potential Intramembrane Charge Pairs by Cosson (1991)10.1083/jcb.110.4.973
/ J Cell Biol / The γ- and ε-Subunits of the CD3 Complex Inhibit Pre-Golgi Degradation of Newly Synthesized T Cell Receptors by Wileman (1990)10.1038/344247a0
/ Nature / Novel Post-Translational Regulation of TCR Expression in CD4+8+ Thymocytes Influenced by CD4 by Bonifacino (1990)10.1083/jcb.110.6.1935
/ J Cell Biol / Studies on the Mechanism of Autophagy: Maturation of the Autophagic Vacuole by Dunn (1990)10.1016/0092-8674(81)90133-1
/ Cell / B Lymphocyte Differentiation and the Control of IgM μ Chain Expression by Sidman (1981)10.1016/S0021-9258(18)34731-8
/ J Biol Chem / Regulation of Catabolism of IgM Heavy Chains in a B Lymphoma Cell Line by Dulis (1982)10.1016/0092-8674(83)90531-7
/ Cell / Assembly In Vivo of Mouse Acetyl Choline Receptor: Identification of an α Subunit Species that May be an Assembly Intermediate by Merlie (1983)10.1083/jcb.111.6.2613
/ J Cell Biol / Mutational Analysis of Muscle Nicotinic Acetylcholine Receptor Subunit Assembly by Blount (1990)10.1083/jcb.103.4.1193
/ J Cell Biol / Analysis of Progressive Deletions of the Transmembrane and Cytoplasmic Domains of Influenza Hemagglutinin by Doyle (1986)10.1016/S0021-9258(18)37701-9
/ J Biol Chem / Transport-Deficient Mutations in the Low Density Lipoprotein Receptor. Alterations in the Cysteine-Rich and Cystein-Poor Regions of the Protein Block Intracellular Transport by Esser (1988)10.1016/S0021-9258(18)77448-6
/ J Biol Chem / Intracellular Degradation of the Transport Impaired Human PiZ α1-Antitrypsin Variant. Biochemical Mapping of the Degradative Event Among Compartments of the Secretory Pathway by Le (1990)10.1128/MCB.10.1.47
/ Mol Cell Biol / Molecular Basis of α1-Antitrypsin Deficiency and Emphysema Associated with the α1-Antitrypsin M-Mineral Sprongs Allele by Curiel (1990)10.1016/0092-8674(90)90148-8
/ Cell / Defective Intracellular Transport and Processing of CFTFR is the Molecular Basis of Most Cystic Fibrosis by Cheng (1990)10.1016/S0021-9258(19)77646-7
/ J Biol Chem / Biogenesis of Acetylcholinesterase Molecular Forms in Muscle. Evidence for a Rapidly Turning Over, Catalytically Inactive Precursor Pool by Rotundo (1988)10.1016/S0021-9258(18)94043-3
/ J Biol Chem / Intracellular Transport, Sorting, and Turnover of Acetylcholinesterase. Evidence for an Endoglycosidase H-Sensitive Form in Golgi Apparatus, Sarcoplasmic Reticulum, and Clathrin-Coated Vesicles and its Rapid Degradation by a Non-Lysosomal Mechanism by Rotundo (1989)
Dates
Type | When |
---|---|
Created | 21 years, 7 months ago (Jan. 22, 2004, 5:19 a.m.) |
Deposited | 4 years, 2 months ago (June 13, 2021, 10:06 p.m.) |
Indexed | 1 month, 2 weeks ago (July 7, 2025, 1:25 a.m.) |
Issued | 34 years ago (Aug. 1, 1991) |
Published | 34 years ago (Aug. 1, 1991) |
Published Print | 34 years ago (Aug. 1, 1991) |
@article{Bonifacio_1991, title={Degradation of proteins within the endoplasmic reticulum}, volume={3}, ISSN={0955-0674}, url={http://dx.doi.org/10.1016/0955-0674(91)90028-w}, DOI={10.1016/0955-0674(91)90028-w}, number={4}, journal={Current Opinion in Cell Biology}, publisher={Elsevier BV}, author={Bonifacio, Juan S. and Lippincott-Schwartz, Jennifer}, year={1991}, month=aug, pages={592–600} }