Results 61 to 70 of about 21,272 (221)
Emerging Aspects of Jumbo Bacteriophages
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
Rare‐earth ions act as multifunctional modifiers in perovskite solar cells by improving charge transport, suppressing oxygen vacancies, passivating defects, promoting grain growth, and enabling redox‐mediated stabilization. In addition, RE‐doped layers can expand spectral utilization through upconversion and downconversion, thereby enhancing light ...
Jiaqi Meng +9 more
wiley +1 more source
Structural And Functional Investigation Of Φ-El-Chaperonin Mediated Protein Folding [PDF]
Chaperonins are ubiquitous, sequence related protein complexes that aid in the folding of nascent and misfolded polypeptides in an ATP driven pathway. Recently a GroEL-like, 860 kilo Dalton chaperonin protein complex was identified and isolated from the ...
Molugu, Sudheer Kumar
core +2 more sources
Cryo-EM structure of human mitochondrial HSPD1
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
Omics‐driven drug repositioning reveals pyroxamide as a neuroprotective HDAC1 inhibitor in Parkinson's disease models. Abstract Parkinson's disease (PD) is the second most common neurodegenerative disorder mainly characterized by the degeneration of dopaminergic neurons originating in the substantia nigra (SN) pars compacta and projecting to other ...
Paz Cartas‐Cejudo +7 more
wiley +1 more source
cpnDB: A Chaperonin Sequence Database [PDF]
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
Mycobacterium tuberculosis chaperonin 10 forms stable tetrameric and heptameric structures [PDF]
The chaperonin activity of sequence-related chaperonin 10 proteins requires their aggregation into heptameric structures. We describe size-exclusion chromatography and ultracentrifugation studies that reveal that while Escherichia coli chaperonin 10 ...
Gianluca Fossati +39 more
core +1 more source
ABSTRACT Molecular chaperones play a central role in the plant proteostasis machinery by aiding the folding of nascent proteins, preventing aggregation, and repairing or degrading damaged proteins. These functions are especially essential during abiotic and biotic stress, which can destabilise cellular proteins and disrupt metabolic homoeostasis.
Mingfang Yang +10 more
wiley +1 more source
Multiple states of a Nucleotide-Bound Group 2 Chaperonin [PDF]
Chaperonin action is controlled by cycles of nucleotide binding and hydrolysis. Here, we examine the effects of nucleotide binding on an archaeal group 2 chaperonin.
Quispe, J. +9 more
core +1 more source
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 +10 more
wiley +1 more source

