Results 181 to 190 of about 30,272 (208)

Biofilm-associated molecular patterns: BAMPs. [PDF]

open access: yesInfect Immun
Østrup Jensen P   +2 more
europepmc   +1 more source

Chaperone-mediated thermotolerance in hyperthermophilic composting: Molecular-Level protein remodeling of microbial communities. [PDF]

open access: yesEnviron Sci Ecotechnol
Li X   +11 more
europepmc   +1 more source

Variety of Bacterial Pathogens in Ticks Removed from Humans, Northeastern China. [PDF]

open access: yesMicroorganisms
Su XL   +11 more
europepmc   +1 more source

GroEL−GroES-Mediated Protein Folding

Chemical Reviews, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Arthur L, Horwich   +2 more
openaire   +3 more sources

Groel crystal growth and characterization

Biosystems, 2008
Single crystals of ribosomal proteins obtained for the first time by Langmuir-Blodgett (LB) nanotemplate confirm earlier findings (Pechkova et al., 2008), pointing to a new generation of bionanomaterials of unique structure-function relationship. The ribosomal protein phage GroEL was overexpressed in E. coli.
PESHKOVA, EVGENIYA   +3 more
openaire   +3 more sources

Transmission Electron Microscopy of GroEL, GroES, and the Symmetrical GroEL/ES Complex

Journal of Structural Biology, 1994
Two new 2-D crystal forms of the Escherichia coli chaperone GroEL (cpn60) 2 x 7-mer have been produced using the negative staining-carbon film (NS-CF) technique. These 2-D crystals, which contain the cylindrical GroEL in side-on and end-on orientations, both possess p21 symmetry, with two molecules in the respective unit cells. The crystallographically
J R, Harris, A, Plückthun, R, Zahn
openaire   +2 more sources

Insertion mutagenesis of Escherichiacoli GroEL

Biochemical and Biophysical Research Communications, 2003
To gain insights into the in vivo folding and assembly of bacterial chaperonins, groEL was subjected to insertion mutagenesis using transposon ISlacZ/in. Four GroEL-LacZ fusions and the corresponding insertion mutants were obtained after residues 34, 90, 291, and 367. Apical domain insertion mutants GroEL291 and GroEL367 were degraded into monomeric 30-
Danielle, Amatore, François, Baneyx
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 mucosal immune response ...
M, Hagiwara   +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   +2 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy