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Ubiquitination in Health and Diseases

Ubiquitination in Health and Diseases

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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.

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Keywords

  • aggregation
  • aldosterone sensitive distal nephron
  • Blood pressure
  • Cancer
  • Cilia
  • ciliogenesis
  • ciliopathy
  • cortical bone derived stem cell
  • degradation
  • deubiquitinase
  • deubiquitinases
  • deubiquitination
  • differentiation
  • disulfide-coupling
  • dopa-responsive dystonia
  • DUBs
  • E3 ubiquitin ligase
  • E3s
  • Endoplasmic Reticulum Stress
  • epithelial sodium channel
  • excitation-transcription coupling
  • fatty acid-binding protein 3
  • fibrils
  • genetic diseases
  • hematopoiesis
  • Hematopoietic Stem Cells
  • Humanities
  • Immune response
  • immune-related diseases
  • Inflammation
  • inhibitor
  • Inhibitors
  • innate immune
  • interferon
  • LUBAC
  • mesenchymal stem cell
  • Mitochondria
  • MITOL/MARCH5
  • monoubiquitin signaling
  • mTOR
  • Myocardial Infarction
  • Nedd4L/Nedd4-2
  • neurodegeneration
  • neurodegenerative disease
  • NF-κB
  • osmotic stress
  • parkinson’s disease
  • polyubiquitin
  • proliferation
  • proteasomal degradation
  • protein complex formation
  • protein quality control
  • protein stabilization
  • proteolysis
  • regulation of gene expression
  • regulatory T cells
  • renal salt reabsorption
  • RING finger
  • RNF152
  • RNF182
  • RNF183
  • RNF186
  • salt-sensitive hypertension
  • semisynthesis
  • Social interaction
  • Social issues & processes
  • Society & culture: general
  • Society & Social Sciences
  • tau protein
  • thema EDItEUR::J Society and Social Sciences::JB Society and culture: general::JBF Social and ethical issues
  • thema EDItEUR::N History and Archaeology::NH History
  • Therapeutic target
  • tyrosine hydroxylase
  • Ubiquitin
  • ubiquitin code
  • ubiquitin ligase
  • ubiquitin proteasome system
  • ubiquitin system
  • ubiquitin-proteasome system
  • Ubiquitination
  • ubiquitin–proteasome pathway
  • UPS
  • Vascular function
  • vesicular trafficking
  • Virus infection
  • virus-host interaction
  • α-synuclein

Links

DOI: 10.3390/books978-3-0365-0547-3

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