Chaperone-mediated protein folding
AL Fink - Physiological reviews, 1999 - journals.physiology.org
The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …
of protein cofactors known as molecular chaperones. These molecules recognize and bind …
Modulation of neurodegeneration by molecular chaperones
PJ Muchowski, JL Wacker - Nature Reviews Neuroscience, 2005 - nature.com
Many neurodegenerative disorders are characterized by conformational changes in proteins
that result in misfolding, aggregation and intra-or extra-neuronal accumulation of amyloid …
that result in misfolding, aggregation and intra-or extra-neuronal accumulation of amyloid …
Molecular mechanism of J-domain-triggered ATP hydrolysis by Hsp70 chaperones
R Kityk, J Kopp, MP Mayer - Molecular cell, 2018 - cell.com
Efficient targeting of Hsp70 chaperones to substrate proteins depends on J-domain
cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and …
cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and …
Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
It is a general feature of molecular chaperones that they are highly conserved throughout
evolution. Prokaryotic and eukaryotic Hsp70 proteins, for example, are over 50% identical at …
evolution. Prokaryotic and eukaryotic Hsp70 proteins, for example, are over 50% identical at …
Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones
Hsp70 chaperones assist a large variety of protein folding processes within the entire
lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ …
lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ …
Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy
J Sarparanta, PH Jonson, C Golzio, S Sandell… - Nature …, 2012 - nature.com
Limb-girdle muscular dystrophy type 1D (LGMD1D) was linked to chromosome 7q36 over a
decade ago, but its genetic cause has remained elusive. Here we studied nine LGMD …
decade ago, but its genetic cause has remained elusive. Here we studied nine LGMD …
Role of the J-domain in the cooperation of Hsp40 with Hsp70
MK Greene, K Maskos, SJ Landry - … of the National Academy of Sciences, 1998 - pnas.org
The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at
intermediate stages of folding, assembly, and translocation across membranes. Binding of …
intermediate stages of folding, assembly, and translocation across membranes. Binding of …
The Arabidopsis Chaperone J3 Regulates the Plasma Membrane H+-ATPase through Interaction with the PKS5 Kinase
Y Yang, Y Qin, C **e, F Zhao, J Zhao, D Liu… - The Plant …, 2010 - academic.oup.com
The plasma membrane H+-ATPase (PM H+-ATPase) plays an important role in the
regulation of ion and metabolite transport and is involved in physiological processes that …
regulation of ion and metabolite transport and is involved in physiological processes that …
Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40
Y Minami, J Höhfeld, K Ohtsuka, FU Hartl - Journal of Biological Chemistry, 1996 - jbc.org
The effects of the human DnaJ homolog, Hsp40, on the ATPase and chaperone functions of
the constitutively expressed Hsp70 homolog, Hsc70, were analyzed. Hsp40 stimulates the …
the constitutively expressed Hsp70 homolog, Hsc70, were analyzed. Hsp40 stimulates the …
The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions
Molecular chaperones are highly conserved in all free‐living organisms. There are many
types of chaperones, and most are conveniently grouped into families. Genome sequencing …
types of chaperones, and most are conveniently grouped into families. Genome sequencing …