Results 61 to 70 of about 34,485 (247)

Evolvability of Chaperonin Substrate Proteins [PDF]

, 2009
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 ...
Emanuele Raineri, Luis Serrano, Paolo Ribeca, Tobias Maier   +3 more
core   +1 more source

OsCPN10a, cooperating with OsCPN20 and OsHSP60‐3B negatively regulate ABA signaling and enhance seed storability in rice

Journal of Integrative Plant Biology, EarlyView.
Abscisic acid signaling homeostasis is essential for seed storability. The molecular chaperone OsCPN10a enhances rice seed storability by forming a trimeric chaperone complex with OsCPN20‐OsHSP60‐3B that attenuates abscisic acid signaling via direct interaction with OsPYL10‐OsABIL1, thereby maintaining starch integrity and offering a promising target ...
Sufeng Liao, Yidong Wei, Yongsheng Zhu, Kunyang Li, Ting Chen, Shuai Zhao, Fangxi Wu, Jinlan Wang, Pengbo Yu, Hongguang Xie, Liping Chen, Qiuhua Cai, Huaan Xie, Jianfu Zhang   +13 more
wiley   +1 more source

The Function of Different Subunits of the Molecular Chaperone CCT in the Microsporidium Nosema bombycis: NbCCTζ Interacts with NbCCTα

Journal of Fungi
Chaperonin containing tailless complex polypeptide 1 (CCT) is a molecular chaperone protein that consists of eight completely different subunits and assists in the folding of newly synthesized peptides.
Sheng Xu, Ying Chen, Jingru Qi, Runpeng Wang, Erjun Wei, Qiang Wang, Yiling Zhang, Xudong Tang, Zhongyuan Shen   +8 more
doaj   +1 more source

Heat Shock Protein 60 (HSP60) detection by QCM Biosensor and Antibody Covered Gold Nanoparticles

International Journal of Electrochemical Science, 2021
Heat Shock Protein 60 (HSP60) is a 60 kDa weighting chaperonin that is an evolutionary conserved protein occurring in a wide number of organisms. It can serve as a plasma or blood serum biomarker of serious pathologies including cancer.
Miroslav Pohanka
doaj   +1 more source

A multi‐omics investigation of sarcopenia and frailty: Integrating genomic, epigenomic and telomere length data

Experimental Physiology, EarlyView.
Abstract Sarcopenia and frailty are complex geriatric syndromes influenced by a combination of genetic and environmental factors. Recent studies suggest that specific genetic variants, DNA methylation patterns and shortened telomeres are associated with age‐related diseases and might contribute to the development of both sarcopenia and frailty. In this
Valentina Ginevičienė, Erinija Pranckevičienė, Alina Urnikytė, Laura Jurkūnaitė, Kristijona Gutauskaitė, Rūta Dadelienė, Justina Kilaitė, Ieva Eglė Jamontaitė, Asta Mastavičiūtė, Ildus I. Ahmetov, Vidmantas Alekna   +10 more
wiley   +1 more source

Traversing the effects of ploidy changes in different Eragrostis curvula genotypes through high‐throughput RNA sequencing

The Plant Genome, Volume 19, Issue 2, June 2026.
Abstract Polyploidization has played a key role in plant genome evolution. Eragrostis curvula (Schrad.) Ness, a perennial forage grass species of the Poaceae family, is an excellent model for investigating genome duplication due to its natural variation in ploidy levels.
D. F. Santoro, J. Carballo, M. C. Pasten, C. A. Gallo, E. Albertini, V. Echenique   +5 more
wiley   +1 more source

Dissecting intrinsic chaperonin activity [PDF]

Proceedings of the National Academy of Sciences, 1997
It has long been known that the linear sequence of amino acids along the polypeptide chains contains all the necessary information required to determine the correct three-dimensional structure of a protein (1). Indeed, a large number of proteins have been shown to refold spontaneously in vitro from an unfolded denatured state to the native folded state
G M, Clore, A M, Gronenborn
openaire   +2 more sources

Chaperonin Abundance Enhances Bacterial Fitness

Frontiers in Molecular Biosciences, 2021
The ability of chaperonins to buffer mutations that affect protein folding pathways suggests that their abundance should be evolutionarily advantageous. Here, we investigate the effect of chaperonin overproduction on cellular fitness in Escherichia coli.
C. M. Santosh Kumar, Kritika Chugh, Anirban Dutta, Vishnuvardhan Mahamkali, Tungadri Bose, Sharmila S. Mande, Shekhar C. Mande, Peter A. Lund   +7 more
doaj   +1 more source

Soluble oligomerization provides a beneficial fitness effect on destabilizing mutations. [PDF]

, 2011
Protein stability is widely recognized as a major evolutionary constraint. However, the relation between mutation-induced perturbations of protein stability and biological fitness has remained elusive.
Eugene Shakhnovich, Shimon Bershtein
core   +1 more source

Effects of confinement and crowding on folding of model proteins

, 2008
We perform molecular dynamics simulations for a simple coarse-grained model of crambin placed inside of a softly repulsive sphere of radius R. The confinement makes folding at the optimal temperature slower and affects the folding scenarios, but both ...
Baruah, Baukmketner, Cheung, Cieplak, Cieplak, Cieplak, Duroux, Ellis, Go, Hartl, Hoang, Honeycutt, Jewett, Kwiecinska, Luisi, M. Wojciechowski, Marek Cieplak, Matzke, Melo, Moilanen, Murtas, Rathore, Sulkowska, Sulkowska, Szymczak, Szymczak, Takagi   +26 more
core   +1 more source