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1. Full Text Omnipotent role of archaeal elongation factor 1 alpha (EF1α) in translational elongation and termination, and quality control of protein synthesis
by Kazuki Saito and Kan Kobayashi and Miki Wada and Izumi Kikuno and Akira Takusagawa and Masahiro Mochizuki and Toshio Uchiumi and Ryuichiro Ishitani and Osamu Nureki and Koichi Ito and Paul Schimmel
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2010, Volume 107, Issue 45, pp. 19242 - 19247
The molecular mechanisms of translation termination and mRNA surveillance in archaea remain unclear. In eukaryotes, eRF3 and HBS1, which are homologous to the... 
Terminator codon | Yeasts | Messenger RNA | Protein synthesis | Archaea | Ribosomes | Stop codon | Eukaryotic cells | Transfer RNA | Crystal structure | Genetic code | tRNA mimicy | Protein quality control | DOM34 | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | EUKARYOTES | STOP CODON RECOGNITION | genetic code | RELEASE FACTOR ERF1 | MESSENGER-RNA | protein quality control | FUNCTIONAL-ANALYSIS | TRANSFER-RNA HYDROLYSIS | RIBOSOME | INSIGHTS | Translation elongation factors | Usage | Analysis | Quality control | Protein biosynthesis | Research | Genetic translation | Quality management | Eukaryotes | Microorganisms | Genomics | Models | Catalysis | Ribonucleic acid--RNA | Biological Sciences
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2. Full Text Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo– designed heme protein
by Sutherland, George A and Grayson, Katie J and Adams, Nathan B. P and Mermans, Daphne M. J and Jones, Alexander S and Robertson, Angus J and Auman, Dirk B and Brindley, Amanda A and Sterpone, Fabio and Tuffery, Pierre and Derreumaux, Philippe and Leslie Dutton, P and Robinson, Colin and Hitchcock, Andrew and Neil Hunter, C
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 18, pp. 6672 - 6681
Protein transport across the cytoplasmic membrane of bacterial cells is mediated by either the general secretion (Sec) system or the twin-arginine translocase... 
biotechnology | COMPLEX | twin-arginine translocase | BIOCHEMISTRY & MOLECULAR BIOLOGY | Escherichia coli (E | coli | SEC-INDEPENDENT PROTEIN | maquette | BACTERIAL TAT PATHWAY | BINDING PROTEIN | SIGNAL PEPTIDE | MOTIF | protein translocation | TRANSPORT | protein export | protein quality control | EXPORT PATHWAY | protein folding | Tat system | PERIPLASM | protein design | CHARGE | Amino Acid Sequence | Temperature | Escherichia coli - enzymology | Hemeproteins - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Substrate Specificity | Escherichia coli Proteins - metabolism | Protein Folding | Protein Sorting Signals | Membrane Transport Proteins - chemistry | Protein Transport | Proton Magnetic Resonance Spectroscopy | Periplasm - metabolism | Hemeproteins - chemistry | Escherichia coli - metabolism | Bacterial Proteins - metabolism | Membrane Transport Proteins - metabolism | Protein Stability | Escherichia coli Proteins - chemistry | Oxidoreductases, N-Demethylating - metabolism | Circular Dichroism | Methylamines - metabolism | Index Medicus | Membrane Biology | Escherichia coli (E. coli)
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3. Full Text Assembly and Function of Heterotypic Ubiquitin Chains in Cell-Cycle and Protein Quality Control
by Yau, Richard G and Doerner, Kerstin and Castellanos, Erick R and Haakonsen, Diane L and Werner, Achim and Wang, Nan and Yang, X. William and Martinez-Martin, Nadia and Matsumoto, Marissa L and Dixit, Vishva M and Rape, Michael
Cell, ISSN 0092-8674, 11/2017, Volume 171, Issue 4, pp. 918 - 933.e20
Posttranslational modification with ubiquitin chains controls cell fate in all eukaryotes. Depending on the connectivity between subunits, different ubiquitin... 
proteasome | anaphase-promoting complex | ubiquitin chain | Huntingtin | protein quality control | Huntington’s disease | ubiquitin | branched ubiquitin chain | Huntington's disease | APC/C | ANAPHASE-PROMOTING COMPLEX | MULTIUBIQUITIN CHAIN | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEGRADATION | IDENTIFICATION | POLYUBIQUITINATION | TRANSLATION | REVEALS | LIGASE | CELL BIOLOGY | Protein Biosynthesis | Ubiquitination | Cell Cycle | Signal Transduction | Mitosis | Humans | Ubiquitin - metabolism | Antibodies, Bispecific - analysis | Anaphase-Promoting Complex-Cyclosome - metabolism | Ubiquitin | Nervous system diseases | Ligases | Proteolysis | Analysis | Quality control | Physiological aspects | Medical colleges | Human acts | Antibodies | Cells | Viral antibodies | Human behavior | Index Medicus
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4. Full Text Protein Quality Control Degradation in the Nucleus
by Enam, Charisma and Geffen, Yifat and Ravid, Tommer and Gardner, Richard G
Annual Review of Biochemistry, ISSN 0066-4154, 6/2018, Volume 87, Issue 1, pp. 725 - 749
Nuclear proteins participate in diverse cellular processes, many of which are essential for cell survival and viability. To maintain optimal nuclear... 
protein quality control | nucleus | proteostasis | chaperones | proteinopathies | ubiquitin-protein ligases | EXPOSED HYDROPHOBICITY | MEMBRANE PROTEINS | UBIQUITIN-PROTEASOME SYSTEM | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | 26S PROTEASOME | SACCHAROMYCES-CEREVISIAE | TRANSCRIPTIONAL REGULATOR | ENDOPLASMIC-RETICULUM | MISFOLDED PROTEINS | CYTOSOLIC PROTEINS | Neoplasms - metabolism | Proteostasis Deficiencies - metabolism | Protein Biosynthesis | Humans | Stress, Physiological | Ubiquitin-Protein Ligases - metabolism | Substrate Specificity | Nuclear Proteins - metabolism | Protein Folding | Saccharomyces cerevisiae - metabolism | Nuclear Envelope - metabolism | Cell Nucleus - metabolism | Metabolic Networks and Pathways | Models, Biological | Proteolysis | Proteasome Endopeptidase Complex - metabolism | Protein Aggregation, Pathological - metabolism | Aging - metabolism | Proteins | Analysis | Conformation | Ubiquitin | Cell survival | Toxicity | Nuclei | Degradation | Survival analysis | Protein folding | Quality control | Proteasomes | Nuclei (cytology) | Viability | Nuclear physics
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5. Full Text Initiation of Quality Control during Poly(A) Translation Requires Site-Specific Ribosome Ubiquitination
by Juszkiewicz, Szymon and Hegde, Ramanujan S
Molecular Cell, ISSN 1097-2765, 02/2017, Volume 65, Issue 4, pp. 743 - 750.e4
Diverse cellular stressors have been observed to trigger site-specific ubiquitination on several ribosomal proteins. However, the ubiquitin ligases,... 
translation | protein quality control | poly(A) | nonstop mRNA | ribosome stalling | ubiquitination | Protein Biosynthesis | Ribosomal Proteins - genetics | Humans | RNA, Messenger - genetics | Ubiquitin - metabolism | Ribosomes - metabolism | RNA, Messenger - metabolism | Ribosomal Proteins - metabolism | Carrier Proteins - genetics | Ubiquitination | Carrier Proteins - metabolism | Transfection | RNA Interference | Ribosomes - genetics | Proteolysis | HEK293 Cells | Mutation | Ubiquitin | Lysine | Ligases | Quality control | Genetic translation | Cells | Quality management | RNA | Index Medicus | Short
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6. Full Text MARCH6 and TRC8 facilitate the quality control of cytosolic and tail‐anchored proteins
by Stefanovic‐Barrett, Sandra and Dickson, Anna S and Burr, Stephen P and Williamson, James C and Lobb, Ian T and Boomen, Dick JH and Lehner, Paul J and Nathan, James A
EMBO reports, ISSN 1469-221X, 05/2018, Volume 19, Issue 5, pp. e45603 - n/a
Misfolded or damaged proteins are typically targeted for destruction by proteasome‐mediated degradation, but the mammalian ubiquitin machinery involved is... 
ERAD | MARCH | protein quality control | TRC | intramembrane proteolysis | TRC8 | MARCH6 | COMPLEX | UBIQUITIN-PROTEASOME SYSTEM | NUCLEAR | SIGNAL PEPTIDE PEPTIDASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ELIMINATION | DEGRADATION SIGNALS | CELL BIOLOGY | HRD1 | MEMBRANE-PROTEINS | LIGASE | Ubiquitin | CRISPR | Spectroscopy | Peptidase | Mass spectroscopy | Hydrophobicity | Screens | Substrates | Genetic screening | Degradation | Proteins | Oxygenase | Mutagenesis | Protein folding | Proteolysis | Quality control | Heme | Signal peptide peptidase | Scientific imaging | Mass spectrometry | Index Medicus | Post-translational Modifications, Proteolysis & Proteomics | Protein Biosynthesis & Quality Control
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7. Full Text Alanine Tails Signal Proteolysis in Bacterial Ribosome-Associated Quality Control
by Lytvynenko, Iryna and Paternoga, Helge and Thrun, Anna and Balke, Annika and Müller, Tina A and Chiang, Christina H and Nagler, Katja and Tsaprailis, George and Anders, Simon and Bischofs, Ilka and Maupin-Furlow, Julie A and Spahn, Christian M.T and Joazeiro, Claudio A.P
Cell, ISSN 0092-8674, 06/2019, Volume 178, Issue 1, pp. 76 - 90.e22
In ribosome-associated quality control (RQC), Rqc2/NEMF closely supports the E3 ligase Ltn1/listerin in promoting ubiquitylation and degradation of aberrant... 
RqcH | RQC | CAT tails | Rqc2 | protein quality control | ssrA | bacterial proteolysis | ribosome stalling | Ltn1 | Ala tails | FIBRONECTIN-BINDING PROTEIN | MESSENGER-RNA | BACILLUS-SUBTILIS | CONTROL COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | HIGH-RESOLUTION | FUNCTIONAL-ANALYSIS | TRANSLATIONAL SURVEILLANCE | DEGRADATION | PEPTIDE | E3 UBIQUITIN LIGASE | CELL BIOLOGY | Ubiquitin | Microbiology | Proteases | Ligases | Proteolysis | Quality control | Bacteria | Molecular biology | Quality management
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8. Full Text Quality control of a cytoplasmic protein complex: Chaperone motors and the ubiquitin-proteasome system govern the fate of orphan fatty acid synthase subunit Fas2 of yeast
by Scazzari, Mario and Amm, Ingo and Wolf, Dieter H
Journal of Biological Chemistry, ISSN 0021-9258, 02/2015, Volume 290, Issue 8, pp. 4677 - 4687
For the assembly of protein complexes in the cell, the presence of stoichiometric amounts of the respective protein subunits is of utmost importance. A surplus... 
LUMINAL PROTEIN | BUDDING YEAST | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIGASE UBR1 | ER-ASSOCIATED DEGRADATION | ENDOPLASMIC-RETICULUM | END RULE PATHWAY | CYTOSOLIC PROTEINS | ACID SYNTHASE | SACCHAROMYCES-CEREVISIAE | METHIONINE | Fatty Acid Synthases - metabolism | Saccharomyces cerevisiae - genetics | Valosin Containing Protein | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | HSP70 Heat-Shock Proteins - genetics | Ubiquitin-Conjugating Enzymes - genetics | Saccharomyces cerevisiae Proteins - genetics | HSP70 Heat-Shock Proteins - metabolism | Proteasome Endopeptidase Complex - genetics | Saccharomyces cerevisiae - metabolism | Chromosomes, Fungal - genetics | Chromosomes, Fungal - metabolism | Ubiquitin-Conjugating Enzymes - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Cell Cycle Proteins - genetics | Adenosine Triphosphatases - genetics | Proteasome Endopeptidase Complex - metabolism | Fatty Acid Synthases - genetics | Index Medicus | Cytosolic Protein Quality Control | Fatty Acid Synthase (FAS) | Chaperone | Protein Synthesis and Degradation | Protein Complex | Ubiquitylation (Ubiquitination) | Protein Degradation | Proteasome
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9. Full Text Protein Quality Control of the Endoplasmic Reticulum and Ubiquitin-Proteasome-Triggered Degradation of Aberrant Proteins: Yeast Pioneers the Path
by Berner, Nicole and Reutter, Karl-Richard and Wolf, Dieter H
Annual Review of Biochemistry, ISSN 0066-4154, 6/2018, Volume 87, Issue 1, pp. 751 - 782
Cells must constantly monitor the integrity of their macromolecular constituents. Proteins are the most versatile class of macromolecules but are sensitive to... 
ERAD | ubiquitin-proteasome system | endoplasmic reticulum-associated degradation | protein quality control | protein retrotranslocation | Cdc48 | chaperones | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | INNER NUCLEAR-MEMBRANE | ER-ASSOCIATED DEGRADATION | SACCHAROMYCES-CEREVISIAE | MISFOLDED SECRETORY PROTEIN | INTEGRAL MEMBRANE-PROTEINS | MANNOSIDASE-LIKE PROTEIN | END RULE PATHWAY | N-GLYCANASE | LIGASE DOA10 | Endoplasmic Reticulum-Associated Degradation | Humans | Ubiquitin - metabolism | Valosin Containing Protein - metabolism | Endoplasmic Reticulum - metabolism | Protein Folding | Saccharomyces cerevisiae - metabolism | Animals | Models, Biological | Proteolysis | Saccharomyces cerevisiae Proteins - metabolism | Cytosol - metabolism | Proteasome Endopeptidase Complex - metabolism | Proteins | Yeast fungi | Analysis | Genetic aspects | Properties | Endoplasmic reticulum | Conformation | Biodegradation | Ubiquitin | Yeast | Macromolecules | Cytosol | Cells | Degradation | Molecules | Protein folding | Quality control | Proteasomes | Aging | Folding
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10. Full Text CHIP regulates aquaporin-2 quality control and body water homeostasis
by Wu, Qi and Moeller, Hanne B and Stevens, Donté A and Sanchez-Hodge, Rebekah and Childers, Gabrielle and Kortenoeven, Marleen L.A and Cheng, Lei and Rosenbaek, Lena L and Rubel, Carrie and Patterson, Cam and Pisitkun, Trairak and Schisler, Jonathan C and Fenton, Robert A
Journal of the American Society of Nephrology, ISSN 1046-6673, 03/2018, Volume 29, Issue 3, pp. 936 - 948
The importance of the kidney distal convoluted tubule (DCT) and cortical collecting duct (CCD) is highlighted by various water and electrolyte disorders that... 
HEAT-SHOCK PROTEINS | COLLECTING DUCT CELLS | DATABASE | DISTAL CONVOLUTED TUBULE | UROLOGY & NEPHROLOGY | SYSTEMS-LEVEL ANALYSIS | ENDOCYTOSIS | CHANNEL AQUAPORIN-2 | APICAL MEMBRANE | PLASMA-MEMBRANE | E3 UBIQUITIN LIGASE | Protein Quality Control | kidney | CHIP | Proteomics | AQP2 | Water handling | Basic Research
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11. Full Text A conserved basic residue cluster is essential for the protein quality control function of the Arabidopsis calreticulin 3
by Liu, Yidan and Li, Jianming
Plant Signaling & Behavior, ISSN 1559-2316, 04/2013, Volume 8, Issue 4, pp. e238641 - e238646
Calreticulin (CRT) is a highly conserved chaperone-like lectin that regulates Ca 2+ homeostasis and participates in protein quality control in the endoplasmic... 
protein quality control | chaperone-like lectin | protein folding | plant innate immunity | brassinosteroid | receptor kinase | Brassinosteroid | Chaperone-like lectin | Plant innate immunity | Protein quality control | Protein folding | Receptor kinase | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANT SCIENCES | Protein Kinases - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Arabidopsis - physiology | Arabidopsis Proteins - genetics | Protein Kinases - genetics | Plant Immunity - genetics | Genes, Plant | Endoplasmic Reticulum - metabolism | Molecular Sequence Data | Peptide Elongation Factor Tu - chemistry | Calreticulin - genetics | Protein Folding | Arabidopsis - metabolism | Arabidopsis - genetics | Arabidopsis Proteins - metabolism | Calreticulin - metabolism | Conserved Sequence | Mutation | Plant Lectins - metabolism | Transgenes | Plant Lectins - genetics | Index Medicus | Short Communication
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12. Full Text Structural basis for translational surveillance by the large ribosomal subunit-associated protein quality control complex
by Dmitry Lyumkis and Dario Oliveira dos Passos and Erich B. Tahara and Kristofor Webb and Eric J. Bennett and Staal Vinterbo and Clinton S. Potter and Bridget Carragher and Claudio A. P. Joazeiro
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2014, Volume 111, Issue 45, pp. 15981 - 15986
All organisms have evolved mechanisms to manage the stalling of ribosomes upon translation of aberrant mRNA. In eukaryotes, the large ribosomal... 
Proteins | Datasets | Yeasts | Quality assurance | Messenger RNA | Ubiquitins | Ribosomes | Electron microscopy | Transfer RNA | Tunnels | Tae2/nemf | Protein quality control | Listerin/Ltn1 E3 ubiquitin ligase | Cryo-EM | Translational surveillance | SYSTEM | listerin/Ltn1 E3 ubiquitin ligase | MULTIDISCIPLINARY SCIENCES | ELECTRON-MICROSCOPY | CRYO-EM IMAGES | FREALIGN | Tae2/Nemf | LISTERIN | DISSOCIATION | SCREEN | translational surveillance | protein quality control | SIGNAL RECOGNITION PARTICLE | cryo-EM | E3 UBIQUITIN LIGASE | REVEALS | Protein Structure, Tertiary | Ribosome Subunits, Large, Eukaryotic - genetics | Saccharomyces cerevisiae - genetics | Protein Biosynthesis - physiology | Ubiquitin-Protein Ligases - metabolism | RNA, Transfer, Amino Acyl - genetics | Structure-Activity Relationship | RNA-Binding Proteins | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | Proteolysis | RNA, Transfer, Amino Acyl - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Proteasome Endopeptidase Complex - metabolism | Ubiquitination - physiology | Ubiquitin-Protein Ligases - genetics | Genetic research | Genetic aspects | Research | Structure | Genetic translation | Eukaryotes | Surveillance | Microscopy | Ribonucleic acid--RNA | Chemical synthesis | Index Medicus | Biological Sciences | Nemf | listerin | Tae2 | Ltn1 E3 ubiquitin ligase
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13. Full Text SUMOylation: A Novel Protein Quality Control Modifier in the Heart
by Maejima, Yasuhiro and Sadoshima, Junichi
Circulation Research, ISSN 0009-7330, 09/2014, Volume 115, Issue 8, pp. 686 - 689
cardiomyopathies | proteasome endopeptidase complex | small ubiquitin-related modifier proteins | SURVIVAL | CARDIAC & CARDIOVASCULAR SYSTEMS | CARDIAC-HYPERTROPHY | DISEASE | PERIPHERAL VASCULAR DISEASE | AUTOPHAGY | HEMATOLOGY | Myocytes, Cardiac - metabolism | Animals | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-Conjugating Enzymes - metabolism | Ubiquitin - metabolism | Index Medicus | proteasome | proteinopathy | SUMO | Protein quality control | cardiomyopathy
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14. Full Text A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins
by Sung, Min-Kyung and Porras-Yakushi, Tanya R and Reitsma, Justin M and Huber, Ferdinand M and Sweredoski, Michael J and Hoelz, André and Hess, Sonja and Deshaies, Raymond J
eLife, ISSN 2050-084X, 08/2016, Volume 5, Issue AUGUST
Overproduced yeast ribosomal protein (RP) Rp126 fails to assemble into ribosomes and is degraded in the nucleus/nucleolus by a ubiquitin-proteasome system... 
COMPLEX | BUDDING YEAST | BIOLOGY | GLOBAL ANALYSIS | MESSENGER-RNA EXPORT | LARGE GENE LISTS | SACCHAROMYCES-CEREVISIAE | CELL | MASS-SPECTROMETRY | E3 UBIQUITIN LIGASE | REVEALS | Saccharomyces cerevisiae - genetics | Ubiquitin-Protein Ligases - metabolism | Saccharomyces cerevisiae Proteins - genetics | Ribosomal Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Metabolic Networks and Pathways | Proteolysis | Ubiquitin-Conjugating Enzymes - metabolism | Gene Deletion | Saccharomyces cerevisiae Proteins - metabolism | Ubiquitin-Protein Ligases - genetics | Tumor Suppressor Proteins | Quality Control | Amino acid sequence | Methods | Bioengineering | Biodegradation | Ubiquitin | Immunoglobulins | rRNA | Hypersensitivity | Ribosomes | Homeostasis | Nuclei | Proteins | Nucleoli | Ubiquitination | Ribosomal proteins | Quality control | Proteasomes | Oxidation | Ubiquitin-protein ligase | Fitness | Huwe1 protein | Index Medicus
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