Results 11 to 20 of about 4,011,919 (357)

Editorial: Molecular Chaperones and Neurodegeneration [PDF]

Frontiers in Neuroscience, 2017
Peer ...
Cintia Roodveldt, Tiago F. Outeiro, Janice E. A. Braun   +2 more
doaj   +8 more sources

Molecular chaperones: guardians of the proteome in normal and disease states [version 1; referees: 2 approved]

F1000Research, 2015
Proteins must adopt a defined three-dimensional structure in order to gain functional activity, or must they? An ever-increasing number of intrinsically disordered proteins and amyloid-forming polypeptides challenge this dogma. While molecular chaperones
Wilson Jeng, Sukyeong Lee, Nuri Sung, Jungsoon Lee, Francis T.F. Tsai   +4 more
doaj   +2 more sources

Proximity proteomics of C9orf72 dipeptide repeat proteins identifies molecular chaperones as modifiers of poly-GA aggregation [PDF]

Acta Neuropathologica Communications, 2022
The most common inherited cause of two genetically and clinico-pathologically overlapping neurodegenerative diseases, amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), is the presence of expanded GGGGCC intronic hexanucleotide ...
Feilin Liu, Dmytro Morderer, Melissa C. Wren, Sara A. Vettleson-Trutza, Yanzhe Wang, Benjamin E. Rabichow, Michelle R. Salemi, Brett S. Phinney, Björn Oskarsson, Dennis W. Dickson, Wilfried Rossoll   +10 more
doaj   +2 more sources

Engineering and evolution of molecular chaperones and protein disaggregases with enhanced activity

Frontiers in Molecular Biosciences, 2016
Cells have evolved a sophisticated proteostasis network to ensure that proteins acquire and retain their native structure and function. Critical components of this network include molecular chaperones and protein disaggregases, which function to prevent ...
Korrie eMack, James eShorter
doaj   +2 more sources

Redox-regulated molecular chaperones [PDF]

Cellular and Molecular Life Sciences, 2002
The conserved heat shock protein Hsp33 functions as a potent molecular chaperone with a highly sophisticated regulation. On transcriptional level, the Hsp33 gene is under heat shock control; on posttranslational level, the Hsp33 protein is under oxidative stress control.
Paul C. F. Graf, Ursula Jakob
openalex   +5 more sources

Mitochondrial molecular chaperones [PDF]

, 1994
After synthesis in the cytosol, most mitochondrial proteins must traverse mitochondrial membranes to reach their functional location. During this process, proteins become unfolded and then refold to attain their native conformation after crossing the ...
Atencio, Caplan, Caplan, Cheng, Craig, Cyr, Deshales, Eilers, Gambill, Glick, Glick, Hartl, Hartl, Hwang, Johnson, Kang, Kiebler, Langer, Liberek, Manning-Krieg, Neupert, Ostermann, Palleros, Rassow, Rospert, Sanders, Scherer, Schleyer, Schröder, Simon, Vestweber, Voos, Xia   +32 more
core   +3 more sources

Editorial: Molecular chaperones and human disease [PDF]

Frontiers in Molecular Biosciences, 2022
Graham Chakafana, Stanley Makumire, Xolani Henry Makhoba   +2 more
doaj   +2 more sources

Molecular Chaperones in Osteosarcoma: Diagnosis and Therapeutic Issues. [PDF]

Cells, 2021
Lallier M, Marchandet L, Moukengue B, Charrier C, Baud'huin M, Verrecchia F, Ory B, Lamoureux F.   +7 more
europepmc   +3 more sources

Editorial: Molecular chaperones and polyamines in disease [PDF]

Frontiers in Molecular Biosciences
Stanley Makumire, Graham Chakafana, Xolani H. Makhoba   +2 more
doaj   +2 more sources

Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations. [PDF]

Signal Transduct Target Ther
Kuzu OF, Granerud LJT, Saatcioglu F.
europepmc   +3 more sources