Results 111 to 120 of about 29,598 (207)
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
Shiga toxin production and translocation during microaerobic human colonic infection with Shiga toxin-producing E. coli O157:H7 and O104:H4 [PDF]
, 2014 Haemolytic uraemic syndrome caused by Shiga toxin-producing E. coli (STEC) is dependent on release of Shiga toxins (Stxs) during intestinal infection and subsequent absorption into the bloodstream.
Billoud, Lucile +4 more
core +2 more sources
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
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
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
, 2020 The ATP-dependent Hsp70 chaperones (DnaK in E. coli) mediate protein folding in cooperation with J proteins and nucleotide exchange factors (E. coli DnaJ and GrpE, respectively). The Hsp70 system prevents protein aggregation and increases folding yields.
Balchin, D. +3 more
core +1 more source
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
Dose, exposure time, and resolution in Serial X-ray Crystallography
, 2007 The resolution of X-ray diffraction microscopy is limited by the maximum dose that can be delivered prior to sample damage. In the proposed Serial Crystallography method, the damage problem is addressed by distributing the total dose over many identical ...
Chapman, H. N. +10 more
core +1 more source