Results 91 to 100 of about 37,307 (249)
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 +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
The Plant Genome, Volume 19, Issue 1, March 2026.Abstract Shade stress affects soybean yield in intercropping, but the molecular basis of cultivar‐specific tolerance is unclear. We analyzed shade‐tolerant (Guru) and sensitive (Heinong 53) soybeans under 30% and 70% shade using transcriptomic, physiological, and biochemical methods.
Fengyi Zhang +10 more
wiley +1 more source
cpnDB: A Chaperonin Sequence Database [PDF]
Genome Research, 2004 Type I chaperonins are molecular chaperones present in virtually all bacteria, some archaea and the plastids and mitochondria of eukaryotes. Sequences of cpn60 genes, encoding 60-kDa chaperonin protein subunits (CPN60, also known as GroEL or HSP60), are useful for phylogenetic studies and as targets for detection and identification of organisms ...
Hill, Janet +4 more
openaire +2 more sources
Emerging Aspects of Jumbo Bacteriophages
Infection and Drug Resistance, 2021 Amina Nazir,1,2 Azam Ali,3 Hong Qing,1 Yigang Tong2 1Key Laboratory of Molecular Medicine and Biotherapy in the Ministry of Industry and Information Technology, Department of Biology, School of Life Sciences, Beijing Institute of Technology, Beijing ...
Nazir A, Ali A, Qing H, Tong Y
doaj
A yeast two-hybrid screen reveals a strong interaction between the Legionella chaperonin Hsp60 and the host cell small heat shock protein Hsp10 [PDF]
, 2015 L. pneumophila is an intracellular bacterium that replicates inside a membrane-bound vacuole called Legionella-containing vacuole (LCV), where it plentifully liberates its HtpB chaperonin.
Nasrallah, Gheyath K.
core +1 more source
The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol
Cellular Microbiology, 2017 The malaria parasite exports numerous proteins into its host red blood cell (RBC). The trafficking of these exported effectors is complex. Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous ...
Natalie J. Spillman +4 more
semanticscholar +1 more source
New Phytologist, Volume 249, Issue 5, Page 2515-2530, March 2026.Summary Fumonisin B1 (FB1) is a mycotoxin that disrupts ceramide biosynthesis and kills plants. Prior activation with bacterial microbe‐associated molecular patterns (MAMPs), such as components of bacterial flagella, effectively suppresses FB1‐induced cell death.
Ali O. Alqarni +3 more
wiley +1 more source
Cryo-EM structure of human mitochondrial HSPD1
iScience, 2021 Summary: Chaperonins play an important role in folding newly synthesized or translocated proteins in all organisms. The bacterial chaperonin GroEL has served as a model system for the understanding of these proteins.
David P. Klebl +7 more
doaj +1 more source
Science Advances, 2018 Site-selective isotope labeling enables structural and functional investigation of a working 1-MDa chaperonin by NMR spectroscopy. Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota, and archaea, facilitating the folding of ...
Guillaume Mas +9 more
semanticscholar +1 more source