Results 91 to 100 of about 5,379 (199)
Acta Physiologica, Volume 242, Issue 10, October 2026.ABSTRACT Aim Repeated heat exposure may promote adaptive remodeling or cumulative tissue burden depending on thermal dose, but its graded molecular and functional consequences during recovery remain unclear. We examined whether repeated moderate (39°C) and severe (41°C) whole‐body hyperthermia produce distinct skeletal muscle trajectories involving ...
Cansu Yakin +4 more
wiley +1 more source
Insect Molecular Biology, Volume 35, Issue 5, Page 556-575, October 2026.RNA‐seq and Batelli gland proteomics of fifth‐instar Mahanarva spectabilis nymphs reveal transcripts and proteins associated with xylem feeding, foam production and environmental interaction. Functional annotation identified genes involved in osmoregulation, detoxification, chemosensation and stress responses, while proteomic analysis confirmed ...
Monique da Silva Bonjour +8 more
wiley +1 more source
Physiological Reports, Volume 14, Issue 19, October 2026.We examined the vastus lateralis (VL) muscle proteomic signature in younger and older males before and after a 10–12‐week resistance training period. Despite similar training volumes between age groups, VL hypertrophy (determined via ultrasound) was dampened in older individuals, and this coincided with an attenuated proteome plasticity response.
Dustyn T. Lewis +16 more
wiley +1 more source
, 2012 The pathogen Mycobacterium tuberculosis expresses two chaperonins, one (Cpn60.1) dispensable and one (Cpn60.2) essential. These proteins have been reported not to form oligomers despite the fact that oligomerization of chaperonins is regarded as ...
Rao, Tara +20 more
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Studies on the evolution of archaeal and eukaryotic chaperonins.
, 2001 Chaperone-assisted protein folding is a universal cellular process. The chaperonins are a class of evolutionarily related molecular chaperones that form multisubunit double-ring complexes and facilitate protein folding through the hydrolysis of ATP. This
Archibald, John M.
core +2 more sources
STRUCTURE AND FUNCTION OF THE ESKAPE PATHOGEN GROESL CHAPERONINS
, 2019 GroESL is an essential bacterial chaperone system comprising the homotetradecameric, double ring GroEL and the homoheptameric cochaperone GroES that is highly conserved from bacteria to man.
Panfilenko, Iliya Vitalievich
core +4 more sources
Myelin Pathology: Involvement of Molecular Chaperones and the Promise of Chaperonotherapy
Brain Sciences, 2019 The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins.
Federica Scalia +4 more
doaj +1 more source
Chaperonin-mediated Protein Folding [PDF]
Journal of Biological Chemistry, 2011 We have been studying chaperonins these past twenty years through an initial discovery of an action in protein folding, analysis of structure, and elucidation of mechanism. Some of the highlights of these studies were presented recently upon sharing the honor of the 2013 Herbert Tabor Award with my early collaborator, Ulrich Hartl, at the annual ...
openaire +3 more sources
Group II chaperonins: new TRiC(k)s and turns of a protein folding machine
, 1999 In the past decade, the eubacterial group I chaperonin GroEL became the paradigm of a protein folding machine. More recently, electron microscopy and X-ray crystallography offered insights into the structure of the thermosome, the archetype of the group ...
Gutsche, I. +3 more
core +1 more source
Thermal activation of the co-chaperonins GroES and gp31 probed by mass spectrometry
, 2008 Many biological active proteins are assembled in protein complexes. Understanding the (dis)assembly of such complexes is therefore of major interest. Here we use mass spectrometry to monitor the disassembly induced by thermal activation of the heptameric
Vies, S.M. van der +5 more
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