Biochemistry Research International

Ubiquitin Proteasome System in Stress and Disease


Publishing date
01 Feb 2013
Status
Published
Submission deadline
14 Sep 2012

Lead Editor

1Laboratory of Chromatin Structure and Functions, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow 119991, Russia

2Department of Biology, Technion – Israel Institute of Technology, Haifa 32000, Israel

3Department of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel

4Department of Microbiology & Immunology, University of California, San Francisco, CA 94143-0414, USA


Ubiquitin Proteasome System in Stress and Disease

Description

Proteasome is an ATP-dependent multisubunit protease complex that is the major regulator of intracellular proteins turnover. It selectively degrades proteins modified by covalent attachment of polyubiquitin chains and some specific proteins without prior polyubiquitination. Among well-known proteasome substrates are regulatory proteins, for example, cyclins, transcription factors, and components of signal transduction pathways and proteins that have abnormal structure because of mutations in gene coding regions or transcription/translational errors, or action stress factors like heat shock and reactive oxygen species. No doubt, ubiquitin-proteasome system (UPS) is vital for normal cell function and its survival upon stress conditions. UPS dysfunction can contribute to or be a cause of severe human disorders like neurodegenerative diseases, cancers, muscle dystrophy, and so on.

We invite investigators to contribute original research articles and reviews that will further detail our understanding of molecular mechanisms of stress resistance and diseases with large contribution of UPS and describe new ways of identification and correction of UPS dysfunction. Potential topics include, but are not limited to:

  • Stress- and disease-associated changes in substrate recognition by UPS
  • Novel inhibitors or activators of UPS components
  • Regulation of UPS biogenesis under nonphysiological conditions
  • Modulation of UPS components activity by cellular and viral proteins
  • Role of ubiquitin and ubiquitin-like modifiers in stress resistance and diseases

Before submission authors should carefully read over the journal's Author Guidelines, which are located at http://www.hindawi.com/journals/bcri/guidelines/. Prospective authors should submit an electronic copy of their complete manuscript through the journal Manuscript Tracking System at http://mts.hindawi.com/ according to the following timetable:


Articles

  • Special Issue
  • - Volume 2012
  • - Article ID 454796
  • - Editorial

Ubiquitin Proteasome System in Stress and Disease

Dmitry Karpov | Michael H. Glickman | ... | Philip Coffino
  • Special Issue
  • - Volume 2012
  • - Article ID 823597
  • - Review Article

A Critical Appraisal of Quantitative Studies of Protein Degradation in the Framework of Cellular Proteostasis

Beatriz Alvarez-Castelao | Carmen Ruiz-Rivas | José G. Castaño
  • Special Issue
  • - Volume 2012
  • - Article ID 837015
  • - Review Article

The Ubiquitin-Proteasome System in Huntington’s Disease: Are Proteasomes Impaired, Initiators of Disease, or Coming to the Rescue?

Sabine Schipper-Krom | Katrin Juenemann | Eric A. J. Reits
  • Special Issue
  • - Volume 2012
  • - Article ID 242764
  • - Review Article

Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family

Michel Becuwe | Antonio Herrador | ... | Sébastien Léon
  • Special Issue
  • - Volume 2012
  • - Article ID 123706
  • - Review Article

Ubiquitin C-Terminal Hydrolase L1 in Tumorigenesis

Jennifer Hurst-Kennedy | Lih-Shen Chin | Lian Li
  • Special Issue
  • - Volume 2012
  • - Article ID 875148
  • - Review Article

Strategies to Identify Recognition Signals and Targets of SUMOylation

Elisa Da Silva-Ferrada | Fernando Lopitz-Otsoa | ... | Rune Matthiesen
Biochemistry Research International
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