Optimization of expression and purification of mitochondrial HSP 40 (Tid1-L) chaperone: Role of mortalin and tid1 in the reactivation and amyloid inhibition of proteins-Reference-Cited by-同舟云学术

Optimization of expression and purification of mitochondrial HSP 40 (Tid1-L) chaperone: Role of mortalin and tid1 in the reactivation and amyloid inhibition of proteins

Published:2020-11 Issue:11 Volume:27 Page:3099-3105
ISSN:1319-562X
Container-title:Saudi Journal of Biological Sciences
language:en
Short-container-title:Saudi Journal of Biological Sciences

Author:

Khan Mohammad Rashid,Khan Mohd Shahnawaz,Ahmed Anwar,Malik Ajamaluddin,Qamar Wajhul

Funder

National Plan for Science, Technology and Innovation

King Abdulaziz City for Science and Technology

Publisher

Elsevier BV

Subject

General Agricultural and Biological Sciences

Reference38 articles.

1. The amino-terminal domain of ClpB supports binding to strongly aggregated proteins;Barnett;J. Biol. Chem.,2005

2. Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains;Barnett;J. Biol. Chem.,2000

3. Cloning and subcellular localization of human mitochondrial hsp70;Bhattacharyya;J. Biol. Chem.,1995

4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding;Bradford;Anal. Biochem.,1976

5. The Hsp70 and Hsp60 chaperone machines;Bukau;Cell,1998

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1. Structural insights into GrpEL1-mediated nucleotide and substrate release of human mitochondrial Hsp70;2024-05-13

2. Mortalin: Protein partners, biological impacts, pathological roles, and therapeutic opportunities;Frontiers in Cell and Developmental Biology;2023-02-02