Results 101 to 110 of about 94,343 (283)
This study constructed the first spatiotemporal multi‐omics map of peach fruit and discovered a key candidate gene that synergistically regulates trichome development and drought tolerance through the jasmonic acid signaling pathway, providing insights into the coupling mechanism between development and stress resistance.
Zhixin Liu +9 more
wiley +1 more source
The Chaperonopathies - Diseases with Defective Molecular Chaperones
In the mid 1950's the Nobel Prize Laureate Christian B. Anfinsen from his research on the folding of ribonuclease A, began to concentrate on the problem of the relationship between structure and function in enzymes.
Giovanni Li Volti
doaj +1 more source
Advances in Heat Shock Proteomics: Towards a Better Understanding of the Physiology and Pathophysiology of Molecular Chaperones. [PDF]
Chaperones are a large group of unrelated protein families that stabilize unfolded proteins, unfold them for translocation across membranes or degradation, and assist in their correct folding and assembly.
Giardina, Bruno +2 more
core
Redox‐Dependent Chaperoning of GBF1 Condensates Regulates Seed Germination in Arabidopsis
In dormant seeds (low ROS), GBF1 forms liquid condensates to repress the germination gene CathB3, and the chaperone GIP1 maintains condensate liquidity and repressive activity. Upon imbibition (high ROS), ROS oxidize GIP1 during germination, impairing its chaperone function.
Yunying Wang, Xiaofeng Fang
wiley +1 more source
This study elucidates that β‐elemene promotes cellular uptake of L. gasseri‐derived lactate by enhancing the membrane translocation of MCT1 in a CD147‐dependent manner. Intracellular lactate, through the lactylation of RBBP4 at the K26 site, recruits EP300 to the promoter regions of downstream genes (POLD1/POLD3), catalyzing H3K27ac modification.
Jiancheng He +10 more
wiley +1 more source
Summary: The extracellular molecular chaperone heat shock protein 90 (eHSP90) stabilizes protease client the matrix metalloproteinase 2 (MMP2), leading to tumor cell invasion.
Alexander J. Baker-Williams +15 more
doaj +1 more source
Evolvability of Chaperonin Substrate Proteins [PDF]
Molecular chaperones ensure that their substrate proteins reach the functional native state, and prevent their aggregation. Recently, an additional function was proposed for molecular chaperones: they serve as buffers (_capacitors_) for evolution by ...
Tobias Maier +7 more
core +1 more source
Comparative genomics of Gondwana‐diverged Pila and Pomacea reveals parallel evolution of aerial oviposition. Convergent chromosomal rearrangements reshape regulatory landscapes within topologically associating domains. Lineage‐specific gene family expansions and viral‐derived perivitelline proteins (PV1) underpin desiccation resistance.
Yufei Zhou +10 more
wiley +1 more source
Disaggregases, molecular chaperones that resolubilize protein aggregates
The process of folding is a seminal event in the life of a protein, as it is essential for proper protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not only lead to loss of function, but also to the formation of ...
David Z. Mokry +2 more
doaj +1 more source
Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes [PDF]
Molecular chaperones are key components in the maintenance of cellular homeostasis and survival, not only during stress but also under optimal growth conditions.
Fraga, Jorge +4 more
core +1 more source

