Results 111 to 120 of about 30,272 (208)
Characterisation of the effects of salicylidene acylhydrazide compounds on type three secretion in Escherichia coli O157:H7 [PDF]
, 2009 Recent work has highlighted a number of compounds that target bacterial virulence by affecting gene regulation. In this work, we show that small-molecule inhibitors affect the expression of the type III secretion system (T3SS) of <i>Escherichia ...
Elofsson, M. +9 more
core +3 more sources
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
An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes. [PDF]
, 2018 Mass spectrometry (MS) has become a crucial technique for the analysis of protein complexes. Native MS has traditionally examined protein subunit arrangements, while proteomics MS has focused on sequence identification.
Campuzano, Iain DG +4 more
core +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
GroEL–Substrate Interactions [PDF]
Cell, 2000 Feltham, Joanna L, Gierasch, Lila M
openaire +1 more source
GroEL: More than Just a Folding Cage [PDF]
Cell, 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. (2006) redesign the GroEL central cavity and show that the chaperonin cage can alter the rate of folding and, for some proteins, could ...
openaire +2 more sources
A major T cell antigen of Mycobacterium leprae is a 10-kD heat-shock cognate protein. [PDF]
, 1992 Several mycobacterial antigens, identified by monoclonal antibodies and patient sera, have been found to be homologous to stress or heat-shock proteins (hsp) defined in Escherichia coli and yeast.
Alland, D +9 more
core
Stability of Recombinant Proteins in Escherichia coli: The Effect of Co-Expression of Five Different Chaperone Sets [PDF]
Journal of Sciences, Islamic Republic of Iran, 2009 Chaperones are produced by prokaryotic, yeast and higher eukaryotic cells for various purposes. Over-expression of each chaperone or sets of them affect the production level of a recombinant protein in the cell.
H. Mirzahoseini
doaj