Diversity of degradation signals in the ubiquitin–proteasome system
暂无分享,去创建一个
[1] Jeffrey L Brodsky,et al. The Recognition and Retrotranslocation of Misfolded Proteins from the Endoplasmic Reticulum , 2008, Traffic.
[2] John A Tainer,et al. A SIM-ultaneous role for SUMO and ubiquitin. , 2008, Trends in biochemical sciences.
[3] Songyu Wang,et al. Lectins sweet-talk proteins into ERAD , 2008, Nature Cell Biology.
[4] A. Weissman,et al. Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation. , 2007, Seminars in cell & developmental biology.
[5] Y. Kwon,et al. The mammalian N-end rule pathway: new insights into its components and physiological roles. , 2007, Trends in biochemical sciences.
[6] Y. Wolf,et al. Global Analysis of Posttranslational Protein Arginylation , 2007, PLoS biology.
[7] P. Muchowski,et al. Chaperone Functions of the E3 Ubiquitin Ligase CHIP* , 2007, Journal of Biological Chemistry.
[8] E. Wiertz,et al. Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3 , 2007, The Journal of cell biology.
[9] J Wade Harper,et al. Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. , 2007, Molecular cell.
[10] Michal Sharon,et al. Mechanism of auxin perception by the TIR1 ubiquitin ligase , 2007, Nature.
[11] Takashi Yamane,et al. Structural basis for the selection of glycosylated substrates by SCFFbs1 ubiquitin ligase , 2007, Proceedings of the National Academy of Sciences.
[12] Bernd Bukau,et al. The N-end rule pathway for regulated proteolysis: prokaryotic and eukaryotic strategies. , 2007, Trends in cell biology.
[13] Wei Li,et al. A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate , 2007, Nature.
[14] M. Hochstrasser,et al. Autoregulation of an E2 enzyme by ubiquitin-chain assembly on its catalytic residue , 2007, Nature Cell Biology.
[15] P. Coffino,et al. Proteasome substrate degradation requires association plus extended peptide , 2007, The EMBO journal.
[16] Joon-No Lee,et al. Sterol-regulated Degradation of Insig-1 Mediated by the Membrane-bound Ubiquitin Ligase gp78* , 2006, Journal of Biological Chemistry.
[17] M. Hochstrasser,et al. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase , 2006, Nature.
[18] Anindya Dutta,et al. UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative autoregulation. , 2006, Molecular cell.
[19] C. Fan,et al. Sequential Quality-Control Checkpoints Triage Misfolded Cystic Fibrosis Transmembrane Conductance Regulator , 2006, Cell.
[20] Thomas Sommer,et al. A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery , 2006, Nature Cell Biology.
[21] Tom A. Rapoport,et al. Distinct Ubiquitin-Ligase Complexes Define Convergent Pathways for the Degradation of ER Proteins , 2006, Cell.
[22] D. Ng,et al. Have you HRD? Understanding ERAD Is DOAble! , 2006, Cell.
[23] M. Hochstrasser,et al. An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery. , 2006, Proceedings of the National Academy of Sciences of the United States of America.
[24] S. Gygi,et al. Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology , 2006, Nature Cell Biology.
[25] J. Schneider-Mergener,et al. ClpS is an essential component of the N-end rule pathway in Escherichia coli , 2006, Nature.
[26] M. Hochstrasser,et al. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways , 2006, The EMBO journal.
[27] M. Rauh,et al. Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome) , 2005, Nature Genetics.
[28] Min Jae Lee,et al. RGS4 and RGS5 are in vivo substrates of the N-end rule pathway. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[29] A. Varshavsky,et al. The N-end rule pathway as a nitric oxide sensor controlling the levels of multiple regulators , 2005, Nature.
[30] M. Pagano,et al. Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. , 2005, Molecular cell.
[31] H. Paulson,et al. CHIP Suppresses Polyglutamine Aggregation and Toxicity In Vitro and In Vivo , 2005, The Journal of Neuroscience.
[32] R. Poon,et al. The N-terminal Regulatory Domain of Cyclin A Contains Redundant Ubiquitination Targeting Sequences and Acceptor Sites , 2005, Cell cycle.
[33] T. Sommer,et al. Ubx2 links the Cdc48 complex to ER-associated protein degradation , 2005, Nature Cell Biology.
[34] Woong Kim,et al. Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. , 2005, Molecular cell.
[35] M. Nita-Lazar,et al. Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. , 2005, Molecular cell.
[36] B. Song,et al. Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. , 2005, Molecular cell.
[37] J. Weissman,et al. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. , 2005, Molecular cell.
[38] R. Takahashi,et al. In vivo evidence of CHIP up‐regulation attenuating tau aggregation , 2005, Journal of neurochemistry.
[39] Min Jae Lee,et al. A Family of Mammalian E3 Ubiquitin Ligases That Contain the UBR Box Motif and Recognize N-Degrons , 2005, Molecular and Cellular Biology.
[40] T. Sommer,et al. ERAD: the long road to destruction , 2005, Nature Cell Biology.
[41] R. Mayer,et al. Ubiquitin and ubiquitin-like proteins as multifunctional signals , 2005, Nature Reviews Molecular Cell Biology.
[42] K. Cadwell,et al. Ubiquitination on Nonlysine Residues by a Viral E3 Ubiquitin Ligase , 2005, Science.
[43] Kazuhiro Iwai,et al. Glycoprotein‐specific ubiquitin ligases recognize N‐glycans in unfolded substrates , 2005, EMBO reports.
[44] A. Shearer,et al. Lipid‐mediated, reversible misfolding of a sterol‐sensing domain protein , 2005, The EMBO journal.
[45] D. Ng,et al. Search and Destroy: ER Quality Control and ER-Associated Protein Degradation , 2005, Critical reviews in biochemistry and molecular biology.
[46] Raymond J. Deshaies,et al. Function and regulation of cullin–RING ubiquitin ligases , 2005, Nature Reviews Molecular Cell Biology.
[47] M. Pagano,et al. Structural Basis of the Cks 1-Dependent Recognition of p 27 Kip 1 by the SCFSkp 2 Ubiquitin Ligase , 2005 .
[48] Mike Tyers,et al. A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin. , 2004, Biochimica et biophysica acta.
[49] A. Ciechanover,et al. The Tumor Suppressor Protein p16INK4a and the Human Papillomavirus Oncoprotein-58 E7 Are Naturally Occurring Lysine-less Proteins That Are Degraded by the Ubiquitin System , 2004, Journal of Biological Chemistry.
[50] J. Harper,et al. Interwoven Ubiquitination Oscillators and Control of Cell Cycle Transitions , 2004, Science's STKE.
[51] K. Nakayama,et al. Interaction of U‐box‐type ubiquitin‐protein ligases (E3s) with molecular chaperones , 2004, Genes to cells : devoted to molecular & cellular mechanisms.
[52] D. Ng,et al. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control , 2004, The Journal of cell biology.
[53] T. Mizushima,et al. Structural basis of sugar-recognizing ubiquitin ligase , 2004, Nature Structural &Molecular Biology.
[54] R. Spiro. Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation , 2004, Cellular and Molecular Life Sciences CMLS.
[55] A. Ciechanover,et al. N-terminal ubiquitination: more protein substrates join in. , 2004, Trends in cell biology.
[56] Robert E. Cohen,et al. Proteasomes and their kin: proteases in the machine age , 2004, Nature Reviews Molecular Cell Biology.
[57] A. Shearer,et al. Structural Control of Endoplasmic Reticulum-associated Degradation , 2004, Journal of Biological Chemistry.
[58] A. Ciechanover,et al. The Tumor Suppressor Protein p 16 INK 4 a and the Human Papillomavirus Oncoprotein-58 E 7 Are Naturally Occurring Lysine-less Proteins , 2004 .
[59] S. Miyamoto,et al. Sequential Modification of NEMO/IKKγ by SUMO-1 and Ubiquitin Mediates NF-κB Activation by Genotoxic Stress , 2003, Cell.
[60] M. Pagano,et al. Proteasome-Mediated Degradation of p21 via N-Terminal Ubiquitinylation , 2003, Cell.
[61] Tony Pawson,et al. Mathematical Modeling Suggests Cooperative Interactions between a Disordered Polyvalent Ligand and a Single Receptor Site , 2003, Current Biology.
[62] M. Hochstrasser,et al. Ubiquitin-dependent degradation of the yeast Mat(alpha)2 repressor enables a switch in developmental state. , 2003, Genes & development.
[63] Yukiko Yoshida,et al. A novel role for N-glycans in the ERAD system. , 2003, Journal of biochemistry.
[64] K. Nakayama,et al. Ubiquitylation as a quality control system for intracellular proteins. , 2003, Journal of biochemistry.
[65] R. Deshaies,et al. Redundant Degrons Ensure the Rapid Destruction of Sic1 at the G1/S Transition of the Budding Yeast Cell Cycle , 2003, Cell Cycle.
[66] Geng Wu,et al. Structure of a -TrCP1-Skp1--Catenin Complex , 2003 .
[67] D. Wolf,et al. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin–proteasome connection , 2003, The EMBO journal.
[68] M. Tyers,et al. Structural Basis for Phosphodependent Substrate Selection and Orientation by the SCFCdc4 Ubiquitin Ligase , 2003, Cell.
[69] Holly McDonough,et al. CHIP: a link between the chaperone and proteasome systems , 2003, Cell stress & chaperones.
[70] K. Koretke,et al. Bioinformatic analysis of ClpS, a protein module involved in prokaryotic and eukaryotic protein degradation. , 2003, Journal of structural biology.
[71] Geng Wu,et al. Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. , 2003, Molecular cell.
[72] N. Emmerich,et al. Ubiquitylation of BAG-1 Suggests a Novel Regulatory Mechanism during the Sorting of Chaperone Substrates to the Proteasome* , 2002, The Journal of Biological Chemistry.
[73] G. Dittmar,et al. Proteasome subunit Rpn1 binds ubiquitin-like protein domains , 2002, Nature Cell Biology.
[74] R. Aebersold,et al. Crucial Step in Cholesterol Homeostasis Sterols Promote Binding of SCAP to INSIG-1, a Membrane Protein that Facilitates Retention of SREBPs in ER , 2002, Cell.
[75] R. Hampton. ER-associated degradation in protein quality control and cellular regulation. , 2002, Current opinion in cell biology.
[76] H. Kawasaki,et al. E3 ubiquitin ligase that recognizes sugar chains , 2002, Nature.
[77] A. Varshavsky,et al. An Essential Role of N-Terminal Arginylation in Cardiovascular Development , 2002, Science.
[78] Christopher J. Schofield,et al. Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL , 2002, Nature.
[79] W. C. Hwang,et al. Structural and Functional Analysis of the Human Mitotic-specific Ubiquitin-conjugating Enzyme, UbcH10* , 2002, The Journal of Biological Chemistry.
[80] M. Ivan,et al. Structure of an HIF-1α-pVHL Complex: Hydroxyproline Recognition in Signaling , 2002, Science.
[81] S. Elledge,et al. Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex , 2002, Nature.
[82] Hai Rao,et al. Recognition of Specific Ubiquitin Conjugates Is Important for the Proteolytic Functions of the Ubiquitin-associated Domain Proteins Dsk2 and Rad23* , 2002, The Journal of Biological Chemistry.
[83] Keiji Tanaka,et al. CHIP is a chaperone‐dependent E3 ligase that ubiquitylates unfolded protein , 2001, EMBO reports.
[84] Tony Pawson,et al. Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication , 2001, Nature.
[85] D. Cyr,et al. CHIP Is a U-box-dependent E3 Ubiquitin Ligase , 2001, The Journal of Biological Chemistry.
[86] M. Hochstrasser,et al. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. , 2001, Genes & development.
[87] Michael I. Wilson,et al. C. elegans EGL-9 and Mammalian Homologs Define a Family of Dioxygenases that Regulate HIF by Prolyl Hydroxylation , 2001, Cell.
[88] K. Nasmyth,et al. Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability , 2001, Nature.
[89] M. Ivan,et al. HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O2 Sensing , 2001, Science.
[90] Michael I. Wilson,et al. Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O2-Regulated Prolyl Hydroxylation , 2001, Science.
[91] A. Matouschek,et al. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. , 2001, Molecular cell.
[92] A. Helenius. Quality control in the secretory assembly line. , 2001, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.
[93] D. Cyr,et al. Is a U-box-dependent E 3 Ubiquitin Ligase IDENTIFICATION OF Hsc 70 AS A TARGET FOR UBIQUITYLATION * , 2001 .
[94] D. Harats,et al. The Ubiquitin-Proteasome Pathway Mediates the Regulated Degradation of Mammalian 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase* , 2000, The Journal of Biological Chemistry.
[95] Stephen J. Elledge,et al. Insights into SCF ubiquitin ligases from the structure of the Skp1–Skp2 complex , 2000, Nature.
[96] R. G. Kulka,et al. Degradation Signals Recognized by the Ubc6p-Ubc7p Ubiquitin-Conjugating Enzyme Pair , 2000, Molecular and Cellular Biology.
[97] A. Varshavsky,et al. RGS4 Is Arginylated and Degraded by the N-end Rule Pathway in Vitro * , 2000, The Journal of Biological Chemistry.
[98] A. Varshavsky,et al. Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway , 2000, Nature.
[99] E. Koonin,et al. The U box is a modified RING finger — a common domain in ubiquitination , 2000, Current Biology.
[100] M. Tyers,et al. Proteolysis and the cell cycle: with this RING I do thee destroy. , 2000, Current opinion in genetics & development.
[101] Martin Rechsteiner,et al. Recognition of the polyubiquitin proteolytic signal , 2000, The EMBO journal.
[102] P. Connell,et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins , 2000, Nature Cell Biology.
[103] D. Cyr,et al. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation , 2000, Nature Cell Biology.
[104] E. Hafen,et al. Dispatched, a Novel Sterol-Sensing Domain Protein Dedicated to the Release of Cholesterol-Modified Hedgehog from Signaling Cells , 1999, Cell.
[105] R. Conaway,et al. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. , 1999, Genes & development.
[106] R. Gardner,et al. A ‘distributed degron’ allows regulated entry into the ER degradation pathway , 1999, The EMBO journal.
[107] S. Reed,et al. Deregulated cyclin E induces chromosome instability , 1999, Nature.
[108] B. Amati,et al. Kip1 meets SKP2: new links in cell-cycle control , 1999, Nature Cell Biology.
[109] M. Hochstrasser,et al. Substrate Targeting in the Ubiquitin System , 1999, Cell.
[110] S. Elledge,et al. Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase. , 1999, Science.
[111] Stephen J. Elledge,et al. The SCFβ-TRCP–ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro , 1999 .
[112] M. Hochstrasser,et al. Degradation Signal Masking by Heterodimerization of MATα2 and MATa1 Blocks Their Mutual Destruction by the Ubiquitin-Proteasome Pathway , 1998, Cell.
[113] R. G. Kulka,et al. Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae , 1998, The EMBO journal.
[114] Christophe Béroud,et al. Software and database for the analysis of mutations in the VHL gene , 1998, Nucleic Acids Res..
[115] W. Pavan,et al. Murine model of Niemann-Pick C disease: mutation in a cholesterol homeostasis gene. , 1997, Science.
[116] James M. Roberts,et al. Cyclin E-CDK2 is a regulator of p27Kip1. , 1997, Genes & development.
[117] M. Cummings,et al. The Tail of a Ubiquitin-conjugating Enzyme Redirects Multi-ubiquitin Chain Synthesis from the Lysine 48-linked Configuration to a Novel Nonlysine-linked Form* , 1996, The Journal of Biological Chemistry.
[118] M. Kirschner,et al. Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates. , 1996, Molecular biology of the cell.
[119] X. Hua,et al. Regulated Cleavage of Sterol Regulatory Element Binding Proteins Requires Sequences on Both Sides of the Endoplasmic Reticulum Membrane (*) , 1996, The Journal of Biological Chemistry.
[120] L. Baldi,et al. Critical Role for Lysines 21 and 22 in Signal-induced, Ubiquitin-mediated Proteolysis of IB- (*) , 1996, The Journal of Biological Chemistry.
[121] M. Hochstrasser. Ubiquitin-dependent protein degradation. , 1996, Annual review of genetics.
[122] T. Maniatis,et al. Signal-induced degradation of I kappa B alpha requires site-specific ubiquitination. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[123] A. Hershko,et al. Reversible phosphorylation controls the activity of cyclosome-associated cyclin-ubiquitin ligase. , 1995, Proceedings of the National Academy of Sciences of the United States of America.
[124] T. Maniatis,et al. Signal induced degradation of IkBa requires site-specific ubiquitina-tion , 1995 .
[125] Kim Nasmyth,et al. The B-type cyclin kinase inhibitor p40 SIC1 controls the G1 to S transition in S. cerevisiae , 1994, Cell.
[126] S. Jentsch,et al. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor , 1993, Cell.
[127] V. Chau,et al. The bacterially expressed yeast CDC34 gene product can undergo autoubiquitination to form a multiubiquitin chain-linked protein. , 1993, The Journal of biological chemistry.
[128] J. H. Strauss,et al. Sindbis virus RNA polymerase is degraded by the N-end rule pathway. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[129] S. Antonarakis,et al. Hypoxia-inducible nuclear factors bind to an enhancer element located 3' to the human erythropoietin gene. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[130] A. Varshavsky. Naming a targeting signal , 1991, Cell.
[131] A. Varshavsky,et al. The recognition component of the N‐end rule pathway. , 1990, The EMBO journal.
[132] A. Goffeau,et al. Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae. , 1990, The Journal of biological chemistry.
[133] J. Goldstein,et al. Regulation of the mevalonate pathway , 1990, Nature.
[134] D. Ecker,et al. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. , 1989, Science.
[135] A. Varshavsky,et al. The degradation signal in a short-lived protein , 1989, Cell.
[136] A. Ciechanover,et al. Purification and characterization of arginyl-tRNA-protein transferase from rabbit reticulocytes. Its involvement in post-translational modification and degradation of acidic NH2 termini substrates of the ubiquitin pathway. , 1988, The Journal of biological chemistry.
[137] H. Narita,et al. The membrane domain of 3-hydroxy-3-methylglutaryl-coenzyme A reductase confers endoplasmic reticulum localization and sterol-regulated degradation onto beta-galactosidase. , 1988, The Journal of biological chemistry.
[138] A. Varshavsky,et al. In vivo half-life of a protein is a function of its amino-terminal residue. , 1986, Science.
[139] A. Hershko,et al. The protein substrate binding site of the ubiquitin-protein ligase system. , 1986, The Journal of biological chemistry.
[140] J. Goldstein,et al. Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme , 1985, Cell.
[141] R. Stroud,et al. Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. , 1985, The Journal of biological chemistry.
[142] D. Russell,et al. Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum , 1984, Nature.
[143] A. Hershko,et al. ATP-dependent degradation of ubiquitin-protein conjugates. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[144] R. Cummings,et al. 3-Hydroxy-3-methylglutaryl-CoA reductase: a transmembrane glycoprotein of the endoplasmic reticulum with N-linked "high-mannose" oligosaccharides. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[145] A Ciechanover,et al. Proposed role of ATP in protein breakdown: conjugation of protein with multiple chains of the polypeptide of ATP-dependent proteolysis. , 1980, Proceedings of the National Academy of Sciences of the United States of America.
[146] A. Goldberg,et al. Studies on the relationship between the degradative rates of proteins in vivo and their isoelectric points. , 1979, The Biochemical journal.
[147] A. Goldberg,et al. Relationship between in vivo degradative rates and isoelectric points of proteins. , 1975, Proceedings of the National Academy of Sciences of the United States of America.
[148] M. Rabinovitz. TRANSLATIONAL REPRESSION IN THE CONTROL OF GLOBIN CHAIN INITIATION BY HEMIN , 1974, Annals of the New York Academy of Sciences.
[149] A. Goldberg,et al. Intracellular protein degradation in mammalian and bacterial cells. , 1974, Annual review of biochemistry.
[150] K. Weber,et al. In vivo Degradation of Mutant Lac Repressor , 1970, Nature.
[151] R T Schimke,et al. Control of enzyme levels in animal tissues. , 1970, Annual review of biochemistry.