Results 101 to 110 of about 21,316 (231)
BMC Genomics, 2012 Background Molecular chaperones appear to have been evolved to facilitate protein folding in the cell through entrapment of folding intermediates on the interior of a large cavity formed between GroEL and its co-chaperonin GroES.
Kumar Vipul +3 more
doaj +1 more source
Proteins: Structure, Function, and Bioinformatics, Volume 94, Issue 9, Page 1610-1627, September 2026.ABSTRACT The role of the cell envelope‐associated Rv0132c/FGD2 from Mycobacterium tuberculosis has long been a subject of debate. Importantly, FGD2 is found only in pathogenic mycobacteria, making it a potential drug target. While some suggest it functions as a glucose‐6‐phosphate dehydrogenase, others propose it acts instead as an F420‐dependent ...
Adewale V. Aderemi +12 more
wiley +1 more source
Український журнал Здоров'я жінкиМета - встановити рівні анти-HSP60 і анти-GroEL антитіл у сироватці крові вагітних із хронічною гіпертензією та накладеною прееклампсією; оцінити можливість їх використання як предикторів накладеної прееклампсії. Матеріали та методи.
O.K. Popel, D.O. Govsieiev
doaj +1 more source
Annals of Applied Biology, Volume 189, Issue 2, September 2026.Squash Silverleaf Disorder (SLD) is growing in its economic impact due to the invasive behaviour of the silverleaf whitefly (Bemisia tabaci MEAM1). In this review we summarize what is currently known about the whitefly‐squash interaction, how both the disease and the whitefly are being affected by climate change, and discuss current and novel ...
Nihal Oztolan‐Erol +4 more
wiley +1 more source
Advanced Science, Volume 13, Issue 45, 13 August 2026.ARC3 levels are controlled by cytosolic and chloroplast proteolytic systems. PUB52 mediates ARC3 precursor ubiquitination and degradation in the cytosol, while CLPC1 promotes ARC3 degradation in chloroplasts, where ARC2 protects ARC3 from excessive breakdown. Disrupting these components causes chloroplast division defects, placing them upstream of ARC3.
Yang Yuan +5 more
wiley +1 more source
Suppression of amyloid fibrils using the GroEL apical domain
Scientific Reports, 2016 In E. coli cells, rescue of non-native proteins and promotion of native state structure is assisted by the chaperonin GroEL. An important key to this activity lies in the structure of the apical domain of GroEL (GroEL-AD) (residue 191–376), which ...
B. Ojha +4 more
semanticscholar +1 more source
Protein Science, Volume 35, Issue 8, August 2026.Abstract F1‐ATPase (F1) is a rotary molecular motor that hydrolyzes adenosine triphosphate (ATP) to drive rotation of the central subunit against the surrounding stator ring. Single‐molecule rotation assays of mutated F1s have elucidated the roles of residues and regions in the chemo‐mechanical coupling mechanism, yet comprehensive mutational ...
Mai Taguchi +3 more
wiley +1 more source
Fitness Trade-Offs Determine the Role of the Molecular Chaperonin GroEL in Buffering Mutations
Molecular biology and evolution, 2015 Molecular chaperones fold many proteins and their mutated versions in a cell and can sometimes buffer the phenotypic effect of mutations that affect protein folding.
B. Sabater-Muñoz +7 more
semanticscholar +1 more source
GroEL: A Proteinaceous “Surfactant” ? [PDF]
Microscopy and Microanalysis, 2002 J. Deaton +6 more
openaire +1 more source
GroEL–Substrate Interactions [PDF]
Cell, 2000 Feltham, Joanna L, Gierasch, Lila M
openaire +1 more source