An inter-subunit disulfide bond of artemin acts as a redox switch for its chaperone-like activity
Published 2018 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
An inter-subunit disulfide bond of artemin acts as a redox switch for its chaperone-like activity
Authors
Keywords
Artemin, Cysteine-rich protein, Redox-dependent chaperone, Disulfide bond
Journal
CELL STRESS & CHAPERONES
Volume 23, Issue 4, Pages 685-693
Publisher
Springer Nature
Online
2018-02-10
DOI
10.1007/s12192-018-0880-7
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Artemin protects cells and proteins against oxidative and salt stress
- (2017) Zeinab Takalloo et al. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
- Real-time monitoring of artemin in vivo chaperone activity using luciferase as an intracellular reporter
- (2016) Zeinab Takalloo et al. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
- Artemin, a diapause-specific chaperone, contributes to the stress tolerance of Artemia franciscana cysts and influences their release from females
- (2014) A. M. King et al. JOURNAL OF EXPERIMENTAL BIOLOGY
- Molecular chaperones and proteostasis regulation during redox imbalance
- (2014) Katerina Niforou et al. Redox Biology
- Regulation of intracellular signalling through cysteine oxidation by reactive oxygen species
- (2012) H. Miki et al. JOURNAL OF BIOCHEMISTRY
- The Brine Shrimp Artemia: Adapted to Critical Life Conditions
- (2012) Gonzalo M. Gajardo et al. Frontiers in Physiology
- Deletion of extra C-terminal segment and its effect on the function and structure of artemin
- (2011) Fatemeh Shirzad et al. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
- Human Protein-disulfide Isomerase Is a Redox-regulated Chaperone Activated by Oxidation of Domain a′
- (2011) Chao Wang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Artemin as an Efficient Molecular Chaperone
- (2011) S. Shirin Shahangian et al. PROTEIN JOURNAL
- The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues
- (2010) Yan Hu et al. CELL STRESS & CHAPERONES
- Diapause termination and development of encysted Artemia embryos: roles for nitric oxide and hydrogen peroxide
- (2010) H. M. Robbins et al. JOURNAL OF EXPERIMENTAL BIOLOGY
- Stress-related proteins compared in diapause and in activated, anoxic encysted embryos of the animal extremophile, Artemia franciscana
- (2010) James S. Clegg JOURNAL OF INSECT PHYSIOLOGY
- Disulfides as Redox Switches: From Molecular Mechanisms to Functional Significance
- (2009) Merridee A. Wouters et al. ANTIOXIDANTS & REDOX SIGNALING
- Redox-Regulated Chaperones
- (2009) Caroline Kumsta et al. BIOCHEMISTRY
- Sequence and structural analysis of artemin based on ferritin: A comparative study
- (2009) Behnam Rasti et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- ArHsp21, a developmentally regulated small heat-shock protein synthesized in diapausing embryos ofArtemia franciscana
- (2008) Zhijun Qiu et al. BIOCHEMICAL JOURNAL
- ArHsp22, a developmentally regulated small heat shock protein produced in diapause-destined Artemia embryos, is stress inducible in adults
- (2008) Zhijun Qiu et al. FEBS Journal
Publish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn MoreAdd your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload Now