Ubiquitination in Health and Diseases
Ubiquitination is a biological process mediated by ubiquitin itself, the E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme, E3 ubiquitin ligase, and deubiquitinating enzyme, respectively. Currently, these multiple biological steps are revealed to participate in various life phenomena,...
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Format: | Electronic Book Chapter |
Language: | English |
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Basel, Switzerland
MDPI - Multidisciplinary Digital Publishing Institute
2021
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Online Access: | DOAB: download the publication DOAB: description of the publication |
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072 | 7 | |a JFFP |2 bicssc | |
100 | 1 | |a Ishigami, Tomoaki |4 edt | |
700 | 1 | |a Ishigami, Tomoaki |4 oth | |
245 | 1 | 0 | |a Ubiquitination in Health and Diseases |
260 | |a Basel, Switzerland |b MDPI - Multidisciplinary Digital Publishing Institute |c 2021 | ||
300 | |a 1 electronic resource (292 p.) | ||
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506 | 0 | |a Open Access |2 star |f Unrestricted online access | |
520 | |a Ubiquitination is a biological process mediated by ubiquitin itself, the E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme, E3 ubiquitin ligase, and deubiquitinating enzyme, respectively. Currently, these multiple biological steps are revealed to participate in various life phenomena, such as cell proliferation, regulation of cell surface proteins expression, and mitochondrial function, which are profoundly related to human health and diseases. Although clinical applications targeting ubiquitination are still limited compared to those directed toward kinase systems such as tyrosine kinases, multiple enzymatic consequences should be future therapeutic implications. This Special Issue of IJMS entitled "Ubiquitination in Health and Disease" successfully published15 distinguished manuscripts, with a total of 66 international authors and. This book provides the latest and most useful information for researchers and scientists in this field. | ||
540 | |a Creative Commons |f https://creativecommons.org/licenses/by/4.0/ |2 cc |4 https://creativecommons.org/licenses/by/4.0/ | ||
546 | |a English | ||
650 | 7 | |a Humanities |2 bicssc | |
650 | 7 | |a Social interaction |2 bicssc | |
653 | |a deubiquitinase | ||
653 | |a degradation | ||
653 | |a therapeutic target | ||
653 | |a cancer | ||
653 | |a hematopoiesis | ||
653 | |a hematopoietic stem cells | ||
653 | |a immune response | ||
653 | |a regulation of gene expression | ||
653 | |a ubiquitin system | ||
653 | |a genetic diseases | ||
653 | |a ubiquitin ligase | ||
653 | |a deubiquitinases | ||
653 | |a monoubiquitin signaling | ||
653 | |a vesicular trafficking | ||
653 | |a protein complex formation | ||
653 | |a inflammation | ||
653 | |a inhibitor | ||
653 | |a innate immune | ||
653 | |a interferon | ||
653 | |a LUBAC | ||
653 | |a NF-κB | ||
653 | |a ubiquitin | ||
653 | |a Parkinson's disease | ||
653 | |a dopa-responsive dystonia | ||
653 | |a tyrosine hydroxylase | ||
653 | |a α-synuclein | ||
653 | |a fatty acid-binding protein 3 | ||
653 | |a ubiquitination | ||
653 | |a proteasomal degradation | ||
653 | |a ubiquitin-proteasome system | ||
653 | |a mitochondria | ||
653 | |a E3 ubiquitin ligase | ||
653 | |a MITOL/MARCH5 | ||
653 | |a salt-sensitive hypertension | ||
653 | |a Nedd4L/Nedd4-2 | ||
653 | |a epithelial sodium channel | ||
653 | |a aldosterone sensitive distal nephron | ||
653 | |a excitation-transcription coupling | ||
653 | |a RNF183 | ||
653 | |a RNF186 | ||
653 | |a RNF182 | ||
653 | |a RNF152 | ||
653 | |a RING finger | ||
653 | |a mTOR | ||
653 | |a endoplasmic reticulum stress | ||
653 | |a osmotic stress | ||
653 | |a ubiquitin code | ||
653 | |a virus infection | ||
653 | |a virus-host interaction | ||
653 | |a tau protein | ||
653 | |a semisynthesis | ||
653 | |a disulfide-coupling | ||
653 | |a polyubiquitin | ||
653 | |a fibrils | ||
653 | |a aggregation | ||
653 | |a neurodegeneration | ||
653 | |a deubiquitination | ||
653 | |a inhibitors | ||
653 | |a protein quality control | ||
653 | |a proteolysis | ||
653 | |a protein stabilization | ||
653 | |a regulatory T cells | ||
653 | |a mesenchymal stem cell | ||
653 | |a cortical bone derived stem cell | ||
653 | |a myocardial infarction | ||
653 | |a blood pressure | ||
653 | |a renal salt reabsorption | ||
653 | |a vascular function | ||
653 | |a ubiquitin proteasome system | ||
653 | |a ubiquitin-proteasome pathway | ||
653 | |a cilia | ||
653 | |a ciliogenesis | ||
653 | |a differentiation | ||
653 | |a proliferation | ||
653 | |a ciliopathy | ||
653 | |a E3s | ||
653 | |a DUBs | ||
653 | |a UPS | ||
653 | |a neurodegenerative disease | ||
653 | |a immune-related diseases | ||
856 | 4 | 0 | |a www.oapen.org |u https://mdpi.com/books/pdfview/book/3729 |7 0 |z DOAB: download the publication |
856 | 4 | 0 | |a www.oapen.org |u https://directory.doabooks.org/handle/20.500.12854/76311 |7 0 |z DOAB: description of the publication |