Results 81 to 90 of about 110,947 (209)

Chaperones and Proteostasis: Role in Parkinson’s Disease

, 2020
Proper folding to attain a defined three-dimensional structure is a prerequisite for the functionality of a protein. Improper folding that eventually leads to formation of protein aggregates is a hallmark of several neurodegenerative disorders.
Shirisha Nagotu, Neha Joshi, Atchaya Raveendran   +2 more
core   +1 more source

Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria [PDF]

, 1994
ATP dependent proteolytic degradation of misfolded proteins in the mitochondrial matrix is mediated by the PIM1 protease and depends on the molecular chaperone proteins mt-hsp70 and Mdj1p. Chaperone function is essential to maintain misfolded proteins in
van Dyck, L., Arlt, H., Neupert, W., Dyck, Luc van, Neupert, Walter, Arlt, Heike, Wagner, I., Vandyck, L., Langer, Thomas, Langer, T., Wagner, Ingrid   +10 more
core  

Pharmacological therapies for monogenic obesity caused by MC4R dysfunction

, 2010
PhDMutations in the melanocortin-4 receptor (MC4R) are the most common cause of monogenic obesity. The majority of MC4R mutations are predicted to cause the receptor to aberrantly fold.
Gooljar, Sakina B
core  

Reduced protein solubility – cause or consequence in amyloid disease?

QRB Discovery
In this perspective, we ask the question whether the apparently lower solubility of specific proteins in amyloid disease is a cause or consequence of the protein deposition seen in such diseases. We focus on Alzheimer’s disease and start by reviewing the
Max Lindberg, Jing Hu, Emma Sparr, Sara Linse   +3 more
doaj   +1 more source

Microbial molecular chaperones

, 2001
Protein folding in the cell, long thought to be a spontaneous process, in fact often requires the assistance of molecular chaperones. This is thought to be largely because of the danger of incorrect folding and aggregation of proteins, which is a ...
Peter A. Lund, Lund, P A, Lund, Peter, Lund, Peter A.   +3 more
core   +1 more source

Molecular chaperones and neuronal proteostasis. [PDF]

, 2015
Protein homeostasis (proteostasis) is essential for maintaining the functionality of the proteome. The disruption of proteostasis, due to genetic mutations or an age-related decline, leads to aberrantly folded proteins that typically lose their function.
Smith, HL, Li, W, Cheetham, ME
core  

The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly

Biomolecules
A complex composed of Pba3-Pba4 and subunits α5, α6, and α7 is identified as an early intermediate in proteasome core particle assembly in wild-type Saccharomyces cerevisiae cells.
Ana C. Matias, Margarida N. Tiago, Jessica Zimmermann, R. Jürgen Dohmen, Paula C. Ramos   +4 more
doaj   +1 more source

Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD

, 2012
Schreiner M, Niemann H. Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Structural Biology. 2012;12(1): 13.Background Type III secretion systems are used by
Niemann, H.H., Madeleine Schreiner, Hartmut H Niemann, Schreiner, Madeleine, Schreiner, M., Niemann, Hartmut ; https://orcid.org/   +5 more
core   +2 more sources

History of the study of amyloidosis: from the Rokitansky’s theory to the present day

Терапевтический архив
In the history of amyloidosis studying the concept of liquids dyscrasia has been predominated and finally it is resulted in accepting a serum protein-precursor as a leading amyloidogenic factor in the disease pathogenesis.
Vilen V. Rameev, Lidia V. Lysenko
doaj   +1 more source

Folding while Bound to Chaperones

, 2017
Chaperones are important in preventing protein aggregation and aiding protein folding. How chaperones aid protein folding remains a key question in understanding their mechanism.
Horowitz, Scott, Koldewey, Philipp, Stull, Frederick, Bardwell, James CA   +3 more
core