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1. Full Text The NF-κB signalling pathway in osteoarthritis
by Rigoglou, Stella and Papavassiliou, Athanasios G
The international journal of biochemistry & cell biology, ISSN 1357-2725, 11/2013, Volume 45, Issue 11, pp. 2580 - 2584
NF-κB | Signal transduction | Cartilage destruction | Osteoarthritis | Chondrocytes | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Animals | Signal Transduction | Models, Biological | Humans | Osteoarthritis - metabolism | NF-kappa B - metabolism | Osteoarthritis - pathology | Osteoarthritis - therapy | Index Medicus | Degradation | Biomedical materials | Pathways | Cytokines | Biocompatibility | Gene expression | Arrays | Signalling
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2. Full Text MitoCPR—A surveillance pathway that protects mitochondria in response to protein import stress
by Weidberg, Hilla and Amon, Angelika
Science (American Association for the Advancement of Science), ISSN 0036-8075, 04/2018, Volume 360, Issue 6385, p. eaan4146
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Saccharomyces cerevisiae - metabolism | Mitochondrial Membrane Transport Proteins - metabolism | Peptidyl Transferases - metabolism | Proteolysis | Saccharomyces cerevisiae Proteins - metabolism | Stress, Physiological | Adenosine Triphosphatases - metabolism | Mitochondria - metabolism | Proteasome Endopeptidase Complex - metabolism | Autophagy-Related Proteins - metabolism | Protein Transport | Respiratory function | Yeast | Amino acids | Lipids | Iron | Translocase | Mitochondrial DNA | Chaperones | Imports | Drug resistance | Cytosol | Nuclei | Channels | Accumulation | Defects | Degradation | Proteins | Mitochondria | Triphosphatase | Pathways | Metabolites | Precursors | Protein folding | Failure analysis | Heme | Inhibition | Lipid metabolism | Sulfur | Protein transport | Localization | Deoxyribonucleic acid--DNA | Biodegradation | Stresses | Adenosine | Multidrug resistance | Gene expression | Signaling | Surveillance | Proteasomes | Proteomes | Electron transport | Adenosine triphosphatase | Index Medicus
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3. Full Text STUB1 regulates TFEB‐induced autophagy–lysosome pathway
by Sha, Youbao and Rao, Lang and Settembre, Carmine and Ballabio, Andrea and Eissa, N Tony
The EMBO journal, ISSN 0261-4189, 09/2017, Volume 36, Issue 17, pp. 2544 - 2552
CHIP (C terminus of HSC70‐Interacting Protein) | TFEB | lysosomes | STUB1 | autophagy | CHIP (C terminus of HSC70-Interacting Protein) | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Phosphorylation | Signal Transduction | Humans | Ubiquitin-Protein Ligases - metabolism | Autophagy - physiology | Mice, Knockout | Animals | Lysosomes - metabolism | HEK293 Cells | Basic Helix-Loop-Helix Leucine Zipper Transcription Factors - metabolism | HeLa Cells | Ubiquitin-Protein Ligases - genetics | Fibroblasts - metabolism | TOR protein | Ubiquitin | Transcription | Serine | Biosynthesis | Autophagy | Accumulation | Proteins | Degradation | Mitochondria | Animal tissues | Rodents | Proteasomes | Mice | Ubiquitin-protein ligase | Phagocytosis | Index Medicus | Post-translational Modifications, Proteolysis & Proteomics | Autophagy & Cell Death | Metabolism
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4. Full Text Mutations in NGLY1 cause an inherited disorder of the endoplasmic reticulum-associated degradation pathway
by Enns, Gregory M and Shashi, Vandana and Bainbridge, Matthew and Gambello, Michael J and Zahir, Farah R and Bast, Thomas and Crimian, Rebecca and Schoch, Kelly and Platt, Julia and Cox, Rachel and Bernstein, Jonathan A and Scavina, Mena and Walter, Rhonda S and Bibb, Audrey and Jones, Melanie and Hegde, Madhuri and Graham, Brett H and Need, Anna C and Oviedo, Angelica and Schaaf, Christian P and Boyle, Sean and Butte, Atul J and Chen, Rong and Clark, Michael J and Haraksingh, Rajini and Cowan, Tina M and He, Ping and Langlois, Sylvie and Zoghbi, Huda Y and Snyder, Michael and Gibbs, Richard A and Freeze, Hudson H and Goldstein, David B and FORGE Canada Consortium
Genetics in medicine, ISSN 1098-3600, 10/2014, Volume 16, Issue 10, pp. 751 - 758
Life Sciences & Biomedicine | Genetics & Heredity | Science & Technology | Abnormalities, Multiple - pathology | Humans | Child, Preschool | Family Health | Infant | Male | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - genetics | Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase - deficiency | Young Adult | Developmental Disabilities - pathology | Seizures - pathology | Microcephaly - pathology | Fatal Outcome | Female | Retrospective Studies | Abnormalities, Multiple - genetics | Movement Disorders - pathology | Endoplasmic Reticulum-Associated Degradation - genetics | Signal Transduction - genetics | Muscle Hypotonia - pathology | Exome - genetics | Pedigree | Adolescent | Abnormalities, Multiple - enzymology | Mutation | Genome-Wide Association Study - methods | Sequence Analysis, DNA - methods | Index Medicus | choreoathetosis | alacrima | seizures | liver disease | NGLY1
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5. Full Text Activation of the p62‐Keap1‐NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells
by Sun, Xiaofang and Ou, Zhanhui and Chen, Ruochan and Niu, Xiaohua and Chen, De and Kang, Rui and Tang, Daolin
Hepatology (Baltimore, Md.), ISSN 0270-9139, 01/2016, Volume 63, Issue 1, pp. 173 - 184
Gastroenterology & Hepatology | Life Sciences & Biomedicine | Science & Technology | NF-E2-Related Factor 2 - physiology | RNA-Binding Proteins - physiology | Signal Transduction | Humans | Mice, Inbred C57BL | Animals | Iron - physiology | Cell Death - physiology | Carcinoma, Hepatocellular - pathology | Liver Neoplasms - metabolism | Liver Neoplasms - pathology | Mice | Tumor Cells, Cultured | Intracellular Signaling Peptides and Proteins - physiology | Kelch-Like ECH-Associated Protein 1 | Carcinoma, Hepatocellular - metabolism | Liver cancer | Quinone oxidoreductase | Reactive oxygen species | Transcription | Oxidoreductase | RNA-mediated interference | Quinone | Ferritin | Heme oxygenase (decyclizing) | Fibrosarcoma | Hepatocellular carcinoma | Iron | Oxygenase | Molecular modelling | Buthionine sulfoximine | Cell death | Heme | Xenografts | Antitumor activity | Index Medicus | erastin | chemoresistance | degradation | sorafenib | chemosensitivity
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6. Full Text Visible-light-driven photocatalytic degradation of sulfamethazine by surface engineering of carbon nitride：Properties, degradation pathway and mechanisms
by Zhou, Chengyun and Zeng, Zhuotong and Zeng, Guangming and Huang, Danlian and Xiao, Rong and Cheng, Min and Zhang, Chen and Xiong, Weiping and Lai, Cui and Yang, Yang and Wang, Wenjun and Yi, Huan and Li, Bisheng
Journal of hazardous materials, ISSN 0304-3894, 12/2019, Volume 380, pp. 120815 - 120815
L-cysteine | Nitrogen vacancy | Sulfamethazine degradation | Photocatalysis | Carbon nitride | Engineering | Engineering, Environmental | Life Sciences & Biomedicine | Technology | Environmental Sciences & Ecology | Science & Technology | Environmental Sciences | Index Medicus
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7. Full Text The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
by Peter Walter and David Ron
Science (American Association for the Advancement of Science), ISSN 0036-8075, 11/2011, Volume 334, Issue 6059, pp. 1081 - 1086
Proteins | Oligomers | REVIEWS | Yeasts | Transcription factors | Messenger RNA | Splicing | Genes | Gene expression regulation | Dimers | Apoptosis | Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Fundamental and applied biological sciences. Psychology | Biological and medical sciences | Analytical, structural and metabolic biochemistry | Molecular and cellular biology | Endoplasmic Reticulum-Associated Degradation | Endoribonucleases - metabolism | Signal Transduction | eIF-2 Kinase - metabolism | Humans | Gene Expression Regulation | Endoplasmic Reticulum - metabolism | Homeostasis | Unfolded Protein Response | Yeasts - genetics | Activating Transcription Factor 6 - metabolism | Animals | Proteolysis | Endoplasmic Reticulum Stress | Protein-Serine-Threonine Kinases - metabolism | Yeasts - metabolism | Stress (Physiology) | Research | Protein folding | Signal transduction | Cellular biology | Gene expression | Index Medicus
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8. Full Text Proteolysis of α‐synuclein fibrils in the lysosomal pathway limits induction of inclusion pathology
by Sacino, Amanda N and Brooks, Mieu M and Chakrabarty, Paramita and Saha, Kaustuv and Khoshbouei, Habibeh and Golde, Todd E and Giasson, Benoit I
Journal of neurochemistry, ISSN 0022-3042, 02/2017, Volume 140, Issue 4, pp. 662 - 678
endocytosis | degradation | Parkinson's disease | α‐synuclein | lysosome | inclusions | α-synuclein | Biochemistry & Molecular Biology | Neurosciences | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Cricetinae | Cricetulus | Humans | Cells, Cultured | Mice, Inbred C3H | Mice, Knockout | Animals | Lysosomes - metabolism | Amyloid - metabolism | Proteolysis | Inclusion Bodies - pathology | Lysosomes - pathology | Signal Transduction - physiology | Mice | Inclusion Bodies - metabolism | alpha-Synuclein - metabolism | CHO Cells | Index Medicus | Parkinson’s disease
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