Results 191 to 200 of about 18,538 (219)

Identification of in vivo substrates of the chaperonin GroEL

Nature, 1999
The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that GroEL interacts strongly with a well-defined set of approximately 300 newly translated polypeptides, including essential components of the transcription/translation machinery and metabolic enzymes.
W A, Houry, D, Frishman, C, Eckerskorn, F, Lottspeich, F U, Hartl   +4 more
openaire   +2 more sources

Sublingual Vaccine with GroEL Attenuates Atherosclerosis

Journal of Dental Research, 2014
Autoimmune responses to heat-shock protein 60 (HSP60) contribute to the progression of atherosclerosis, whereas immunization with HSP60 may induce atheroprotective responses. We assessed the capacity of an atheroprotective vaccine that targeted a recombinant HSP60 from Porphyromonas gingivalis (rGroEL) to induce a protective ...
M, Hagiwara, T, Kurita-Ochiai, R, Kobayashi, T, Hashizume-Takizawa, K, Yamazaki, M, Yamamoto   +5 more
openaire   +2 more sources

Chaperonin GroEL: Structure and Reaction Cycle

Current Protein & Peptide Science, 2007
The structure of Escherichia coli chaperonin GroEL was studied using various experimental tools. Such studies produced information about its structure with increasing details. Moreover, remarkable advances in experimental methods provided a step forward in understanding the reaction cycle involved in GroEL-mediated protein folding.
K Ananda, Krishna, G Venkateswara, Rao, K R S Sambasiva, Rao   +2 more
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Asymmetric binding of membrane proteins to GroEL

Archives of Biochemistry and Biophysics, 2005
The interaction of GroEL with non-native soluble proteins has been studied intensively and structure-function relationships have been established in considerable detail. Recently, we found that GroEL is also able to bind membrane proteins in the absence of detergents and deliver them to liposomes in a biologically active state.
Jingchuan, Sun, Christos G, Savva, John, Deaton, H Ronald, Kaback, Maja, Svrakic, Ry, Young, Andreas, Holzenburg   +6 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, Gustavo, Zardeneta, Jose A, Mendoza   +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, Ayman, Al-Mariri, Ebtisam, Hamad, Abdul Qader, Abbady   +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, Orzala, Sharif, Puiying Annie, Mak, Hsiao-Ting, Wang, Ingo H, Engels, Achim, Brinker, Peter G, Schultz, Arthur L, Horwich, Eli, Chapman   +8 more
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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, Meirong, Hu, Shengqing, Yu, Xin, Wang, Feng, Lu, Fang, Liu, Xusheng, Qiu, Cuiping, Song, Yingjie, Sun, Chan, Ding   +9 more
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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, H p, Feng, S J, Landry, J, Maxwell, L M, Gierasch   +4 more
openaire   +2 more sources