Molecular chaperones in human disorders. (2019)

• Record Type: Book
• Further Information: Note: Edited by Rossen Donev.
• Editors: Donev, Rossen
• Contents: 1. Functional principles and regulation of molecular chaperones Johannes Buchner 2. Chaperones and retinal disorders Nikolai O. Artemyev 3. Protein misfolding and degradation in genetic diseases Rasmus Hartmann-Petersen 4. Chaperone dysfunction in hereditary myopathic diseases Andreas Roos 5. Diseases caused by functional disorder of molecular chaperones residing in the endoplasmic reticulum Masafumi Sakono 6. Structural and functional insights on the roles of molecular chaperones in the mistargeting and aggregation phenotypes associated with primary hyperoxaluria type I Angel Luis Pey 7. Inflammatory response and its relation to sphingolipid metabolism proteins: Targeting inflammation with molecular chaperones Elif Ozkirimli 8. When safeguarding goes wrong: impact of oxidative stress on proteins homeostasis in health and neurodegenerative disorders Dana Reichmann 9. Computational approach to unravel the misfolding mechanism of Glucosylceramidase mutations in Gaucher Disease George Priya Doss P. C 10. Cytosolic quality control proteins, SGTA and the Bag6 complex, in disease Rivka L. Isaacson
• Publisher Details: Cambridge, MA : Academic Press is an imprint of Elsevier
• Publication Date: 2019
• Extent: 1 online resource
• Subjects: 572/.633; Molecular chaperones; SCIENCE / Life Sciences / Biochemistry; Electronic books
• Languages: English
• ISBNs: 9780128155585; 0128155582
• Related ISBNs: 9780128155578; 0128155574
• Notes: Note: Online resource; title from PDF title page (ScienceDirect, viewed January 17, 2019).
• Access Rights: Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
• Access Usage: Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.