Results 71 to 80 of about 227,395 (295)
Editorial: Molecular Chaperones and Neurodegeneration [PDF]
Frontiers in Neuroscience, 2017 Peer ...
Roodveldt, Cintia +2 more
openaire +8 more sources
FEBS Open Bio, EarlyView.Pharmacological inhibition of PERK in a DEN‐induced mouse model of liver cancer does not reduce tumor burden but alters cellular stress signaling. Despite blocking PERK activity, downstream stress responses, including CHOP expression, remain active, suggesting compensatory mechanisms within the unfolded protein response that may influence tumor ...
Ada Lerma‐Clavero +5 more
wiley +1 more source
The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins [PDF]
, 2017 Indexación: Scopus.Piscirickettsia salmonis is the predominant bacterial pathogen affecting the Chilean salmonid industry. This bacterium is the etiological agent of piscirickettsiosis, a significant fish disease.
Artigues, A. +14 more
core +1 more source
ATP‐driven molecular chaperone machines [PDF]
Biopolymers, 2013 ABSTRACTThis review is focused on the mechanisms by which ATP binding and hydrolysis drive chaperone machines assisting protein folding and unfolding. A survey of the key, general chaperone systems Hsp70 and Hsp90, and the unfoldase Hsp100 is followed by a focus on the Hsp60 chaperonin machine which is understood in most detail.
Clare, Daniel K, Saibil, Helen R
openaire +2 more sources
Mutant NPM1 in Acute Myeloid Leukemia Initiation and Maintenance
Aging and Cancer, EarlyView.NPM1 mutations drive acute myeloid leukemia by acting as neomorphic transcriptional regulators that cooperate with Menin–MLL and XPO1 to sustain HOX/MEIS1 expression and block differentiation. Targeting these mutant‐specific transcriptional dependencies provides a rational therapeutic strategy for NPM1‐mutated AML.
Yanan Jiang +3 more
wiley +1 more source
BMC Bioinformatics, 2011 Background HSPs (Heat shock proteins) are highly conserved ubiquitous proteins among species which are involved in maintaining appropriate folding and conformation of other proteins and are thus referred to as molecular chaperones.
Bisaria Virendra S +6 more
doaj +1 more source
Molecular Chaperones and Co-Chaperones in Parkinson Disease [PDF]
The Neuroscientist, 2012 Parkinson disease, a progressive neurodegenerative disorder, is caused by the pathological accumulation of proteins, including the ubiquitous presynaptic protein α-synuclein. Alterations in the metabolism of α-synuclein have clearly been linked to neurodegeneration, and early steps in the pathological sequence of this protein include the formation of ...
Hemi, Dimant +2 more
openaire +2 more sources
Advanced Healthcare Materials, EarlyView.We measure the cell‐specific responses of administering infusible ECM (iECM) in acute myocardial infarction (MI) across multiple timepoints. Using single‐nucleus RNA sequencing and spatial transcriptomics, we measure macrophage activation, fibroblast remodeling, increased vascular development, lymphangiogenesis, cardioprotection, and neurogenesis ...
Joshua M. Mesfin +18 more
wiley +1 more source
Hsp70- and Hsp90-mediated proteasomal degradation underlies TPIsugarkill pathogenesis in Drosophila
Neurobiology of Disease, 2010 Triosephosphate isomerase (TPI) deficiency is a severe glycolytic enzymopathy that causes progressive locomotor impairment and neurodegeneration, susceptibility to infection, and premature death. The recessive missense TPIsugarkill mutation in Drosophila
Stacy L. Hrizo, Michael J. Palladino
doaj +1 more source
Design of Allosteric Stimulators of the Hsp90 ATPase as New Anticancer Leads [PDF]
, 2017 Allosteric compounds that stimulate Hsp90 adenosine triphosphatase (ATPase) activity were rationally designed, showing anticancer potencies in the low micromolar to nanomolar range.
Agard, Da +10 more
core +1 more source