Results 101 to 110 of about 18,538 (219)

GroEL: More than Just a Folding Cage

open access: yes, 2006
The chaperonin GroEL has been thought of as an important but passive player in protein folding, providing an encapsulated environment that allows folding to proceed unimpaired by aggregation. In this issue, Tang et al.
Radford, Sheena E.
core   +1 more source

GroEL/ES mediated the in vivo recovery of TRAIL inclusion bodies in Escherichia coli

open access: yesScientific Reports, 2018
Inclusion body (IB) formation generates substantial bio-waste in the pharmaceutical industry and remains a major challenge for heterologous protein expression.
Zhanqing Wang   +6 more
doaj   +1 more source

Seleção, caracterização e clonagem dos genes fljB e groEL agonistas dos receptores de reconhecimento de padrão do sistema imune inato das aves

open access: yesPesquisa Veterinária Brasileira, 2014
A produção recombinante de agonistas dos receptores do reconhecimento de padrão do sistema imune inato tem fornecido uma nova ferramenta para a produção de imunoestimulantes para animais.
Bruno A. Soares   +7 more
doaj   +1 more source

Chaperomics: In Vivo GroEL Function Defined [PDF]

open access: yesCurrent Biology, 2005
A recent proteome analysis of protein folding inside cells of Escherichia coli predicts that only 84 of the approximately 2400 cytosolic proteins expressed in minimal media depend absolutely on the GroEL/GroES chaperone system to avoid aggregation. These proteins are enriched in alpha/beta domains and 13 are essential for growth.
openaire   +2 more sources

Single-Ring GroEL: An Expanded View

open access: yes, 2006
A remarkable structure of an 86 kDa substrate encapsulated in a single-ring GroEL/GroES chaperonin complex is revealed by cryo-electron microscopy in this issue of Structure (Chen et al., 2006).
Wolf, Sharon Grayer
core   +1 more source

GroEL (Hsp60) of Clostridium difficile is involved in cell adherence.

open access: yes, 2001
International audiencePrevious results have demonstrated that adherence of Clostridium difficile to tissue culture cells is augmented by various stresses; this study focussed on whether the GroEL heat shock protein is implicated in this process. The 1940
Porcheray, Fabrice   +6 more
core   +1 more source

Interaction of β-lactoglobulin with chaperonin GroEL [PDF]

open access: yes
Sakai, Kazuko, Hoshino, Masaru and Goto, Yuji "Interaction of β-lactoglobulin with chaperonin GroEL", Proceedings of the Indian National Science Academy, 68, 4A, 341-347, Indian National Science Academy, 2002The roles of electrostatic and hydrophobic ...
Sakai, Kazuko   +2 more
core  

GroEL channels the folding of thioredoxin along one kinetic route

open access: yes, 2001
Many proteins display complex folding kinetics, which represent multiple parallel folding pathways emanating from multiple unfolded forms and converging to the unique native form.
Bhutani, Nidhi, Udgaonkar, Jayant B.
core   +1 more source

groEL encodes a highly antigenic protein in Burkholderia pseudomallei

open access: yes, 2001
No recombinant protein is available for serodiagnosis of melioidosis. In this study, we report the cloning of the groEL gene, which encodes an immunogenic protein of Burkholderia pseudomallei.
Woo, PCY   +4 more
core   +1 more source

Refolding of denatured MDH by GroEL and Pf-cpn20.

open access: yes, 2013
Urea-denatured malate dehydrogenase was refolded by GroEL with the help of Pf-cpn20, using At-cpn20 and GroES as control co-chaperonins. A) Refolding yields as a function of the co-chaperonin/GroEL protomer ratio.
Gal Zizelski (104051)   +6 more
core   +1 more source

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