Results 201 to 210 of about 29,854 (231)
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?????????????????? ?????????????????????????????? ???????????????? GroEL ?? ?????? ???????????????????????????????? ??????????-???????????????????????? ?? Hsp60

2019
The method of obtaining and purification of recombinant chaperon GroEL (prokaryotic homolog of eukaryotic chaperon Hsp60) including the protein expression in E. coli cells, precipitation with saturated ammonium sulphate from a producent lysate, gel-filtration on Sephacryl-300 column and ion-exchange chromatography on MonoQ HR 5/5 column, is described ...
openaire   +2 more sources

Characterization of the chaperonin GroEL in Mycoplasma gallisepticum

Archives of Microbiology, 2014
Mycoplasma gallisepticum (MG) is a common and widespread cause of chronic respiratory disease in poultry. In this study, antigenic proteins were identified from MG membrane using two-dimensional gel electrophoresis (2-DE) analysis followed by Western blot and matrix-assisted desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS ...
Lei, Tan   +9 more
openaire   +2 more sources

Oxidized GroEL can function as a chaperonin

Frontiers in Bioscience, 2004
Here, we report on the facilitated reactivation (85%) of oxidatively inactivated rhodanese by an oxidized form of the molecular chaperone GroEL (ox-GroEL). Reactivation by ox-GroEL required a reductant, and the enzyme substrate, sodium thiosulfate.
Girish C, Melkani   +2 more
openaire   +2 more sources

Immunodetection of the recombinant GroEL by the Nanobody NbBruc02

World Journal of Microbiology and Biotechnology, 2012
Brucella has a great impact on health and economy in Syria, thus much effort is being placed on the development of diagnostics and vaccines. In this context, a wide Nanobody "immune" library was previously established, from which several Brucella-specific binders were isolated.
Lubna, Abo Assali   +3 more
openaire   +2 more sources

A biochemical screen for GroEL/GroES inhibitors

Bioorganic & Medicinal Chemistry Letters, 2014
High-throughput screening of 700,000 small molecules has identified 235 inhibitors of the GroEL/GroES-mediated refolding cycle. Dose-response analysis of a subset of these hits revealed that 21 compounds are potent inhibitors of GroEL/GroES-mediated refolding (IC50
Steven M, Johnson   +8 more
openaire   +2 more sources

Refolding of Denatured Trichosanthin in the Presence of GroEL

Biochemical and Biophysical Research Communications, 1998
The stability of trichosanthin (TCS), a 27-kDa ribosome-inactivating protein, was investigated in the presence of guanidinium chloride (GdnHCl). The process of unfolding was monitored by CD and fluorescence spectroscopy. Both methods show the presence of partially folded intermediates. Unfolding of TCS is attained in 6M GdnHCl, but the inactive species
C K, Lau, R N, Wong, S C, Lo, F, Kwok
openaire   +2 more sources

Basis of Substrate Binding by the Chaperonin GroEL

Biochemistry, 1999
The molecular chaperonins are essential proteins involved in protein folding, complex assembly, and polypeptide translocation. While there is abundant structural information about the machinery and the mechanistic details of its action are well studied, it is yet unresolved how chaperonins recognize a large number of structurally unrelated polypeptides
Z, Wang   +4 more
openaire   +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 ...
openaire   +2 more sources

Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL

MBio, 2021
Jared Sivinski   +2 more
exaly  

Lactobacillus stress protein GroEL prevents colonic inflammation

Journal of Gastroenterology, 2021
François Hermetet   +2 more
exaly  

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