Results 101 to 110 of about 19,683 (209)
GroEL/ES mediated the in vivo recovery of TRAIL inclusion bodies in Escherichia coli
Scientific 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
Pesquisa 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
DEVELOPING A NEW MODEL OF THE GROEL FUNCTIONAL CYCLE AND ITS IMPLICATIONS FOR THE GROEL-OPTIMIZED SUBSTRATE PROTEIN REFOLDING [PDF]
, 2014 Despite years of research work, many aspects of the fundamentally important GroEL functional cycle are still in dispute. The work of this dissertation mainly focuses on three major disputes in the field: the identity of the rate determining step (RDS ...
Ye, Xiang
core +1 more source
Interaction of β-lactoglobulin with chaperonin GroEL [PDF]
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 +1 more source
Electron Micrographs of GroEL CP376-RW.
, 2013 Samples were stained with 1% uranyl acetate. The scale bar in each figure indicates 100 nm. Magnification was x 60,000. Wild Type denotes wild type GroEL, R231W indicates GroEL R231W.
Kazuhiro Isaji (341697) +5 more
core +1 more source
An expanded protein folding cage in the GroEL-gp31 complex
, 2006 Bacteriophage T4 produces a GroES analogue, gp31, which cooperates with the Escherichia coli GroEL to fold its major coat protein gp23. We have used cryo-electron microscopy and image processing to obtain three-dimensional structures of the E.
Heerikhuizen, H. van +6 more
core +1 more source
A single molecule study of the GroEL active cage mechanism [PDF]
, 2015 The cylindrical chaperonin GroEL and its lid-shaped cofactor GroES of Escherichia coli perform an essential role in assisting protein folding by transiently encapsulating non-native substrate in an ATP-regulated mechanism.
Gupta, Amit Jean
core +1 more source
GroEL–Substrate Interactions [PDF]
Cell, 2000 Feltham, Joanna L, Gierasch, Lila M
openaire +1 more source
GroEL Stability and Function [PDF]
Journal of Biological Chemistry, 2003 Begoña Sot +3 more
openaire +1 more source