Results 11 to 20 of about 19,683 (209)

Ligands regulate GroEL thermostability [PDF]

FEBS Letters, 1997
Escherichia coli heat‐shock proteins GroEL and GroES stimulate (in an ATP‐dependent manner) the folding of various proteins. In this study scanning microcalorimetry was applied to investigate GroEL thermostability in the presence of its ligands. Mg2+ and K+ ions stabilize while ADP destabilizes the GroEL molecule against the action of temperature ...
Surin, A.K, Kotova, N.V, Kashparov, I.A, Marchenkov, V.V, Marchenkova, S.Yu, Semisotnov, G.V   +5 more
openaire   +3 more sources

Probing the dynamic process of encapsulation in Escherichia coli GroEL. [PDF]

PLoS ONE, 2013
Kinetic analyses of GroE-assisted folding provide a dynamic sequence of molecular events that underlie chaperonin function. We used stopped-flow analysis of various fluorescent GroEL mutants to obtain details regarding the sequence of events that ...
Toshifumi Mizuta, Kasumi Ando, Tatsuya Uemura, Yasushi Kawata, Tomohiro Mizobata   +4 more
doaj   +2 more sources

Structural interplay of the redox co-chaperone CnoX to GroEL/ES chaperonin [PDF]

Life Science Alliance
Cryo-EM structures reveal how the redox co-chaperone CnoX is accommodated during the GroEL reaction cycle and how GroES binding remodels the apical domains to promote CnoX release. Protein folding by the bacterial chaperonin GroEL/ES relies on ATP-driven
Junhak Kim, Mingyu Jung, Soung-Hun Roh
doaj   +2 more sources

In vivo activities of GroEL minichaperones [PDF]

Proceedings of the National Academy of Sciences, 1998
Fragments encompassing the apical domain of GroEL, called minichaperones, facilitate the refolding of several proteins in vitro without requiring GroES, ATP, or the cage-like structure of multimeric GroEL.
J, Chatellier, F, Hill, P A, Lund, A R, Fersht   +3 more
core   +6 more sources

Structural and Computational Study of the GroEL–Prion Protein Complex

Biomedicines, 2021
The molecular chaperone GroEL is designed to promote protein folding and prevent aggregation. However, the interaction between GroEL and the prion protein, PrPC, could lead to pathogenic transformation of the latter to the aggregation-prone PrPSc form ...
Aleksandra A. Mamchur, Andrei V. Moiseenko, Irina S. Panina, Igor A. Yaroshevich, Sofia S. Kudryavtseva, Evgeny B. Pichkur, Olga S. Sokolova, Vladimir I. Muronetz, Tatiana B. Stanishneva-Konovalova   +8 more
doaj   +2 more sources

Phage Display Selection and In Silico Characterization of Peptides as Potential GroEL Modulators [PDF]

Pharmaceutics
Background/Objectives. Antibiotic resistance is an escalating global health concern, highlighting the need for innovative antibacterial strategies beyond traditional drugs.
Stefania Olla, Stella Garcia Colombarolli, Chiara Siguri, Davide Murrau, Alberto Vitali   +4 more
doaj   +2 more sources

GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome [PDF]

Nature Communications
The bacterial chaperonin GroEL/ES promotes protein folding post-translation by transiently encapsulating client proteins within a central chamber. GroEL also binds translating ribosomes in vivo, implying an additional role in cotranslational folding ...
Alžběta Roeselová, Sarah L. Maslen, Jessica Zhiyun He, Gabija Jurkeviciute, Aleksandra Pajak, J. Mark Skehel, Radoslav I. Enchev, David Balchin   +7 more
doaj   +2 more sources

Mechanism of substrate recognition by the chaperonin GroEL

Biochemistry and Cell Biology, 2001
The bacterial chaperonin GroEL functions with its cofactor GroES in assisting the folding of a wide range of proteins in an ATP-dependent manner. GroEL–GroES constitute one of the main chaperone systems in the Escherichia coli cytoplasm. The chaperonin facilitates protein folding by enclosing substrate proteins in a cage defined by the GroEL cylinder ...
Walid A Houry
openaire   +3 more sources

Prospective study to estimate the role of different infertility factors in prediction of unsuccessful IVF outcome

Репродуктивная эндокринология, 2021
Research objective: in a prospective controlled study to investigate the role of HSP60, GroEl and other infertility factors as predictors of successful IVF outcome. Materials and methods.
V.O. Berestovyi, A. Mahmood, A.M. Martych, A.B. Prylutska, O.O. Berestovyi, D.O. Govsieiev   +5 more
doaj   +1 more source

Роль білків теплового шоку в прогнозуванні перебігу клімактеричного синдрому

Український журнал Здоров'я жінки, 2022
Проблема клімактерію актуальна вже протягом багатьох десятиліть. Патогенетично обґрунтованим методом лікування, враховуючи зміну гормонального фону жінки, є замісна гормональна терапія.
I.V. Sokol, D.O. Govsieiev
doaj   +1 more source