Results 181 to 190 of about 29,598 (207)
Genetic and structural insights into the functional importance of the conserved gly-met-rich C-terminal tails in bacterial chaperonins. [PDF]
Commun BiolKumar CMS, Mai AM, Mande SC, Lund PA.
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Laboratory strategies for the identification of Burkholderia species: From classical phenotyping to advanced genomic and proteomic approaches. [PDF]
Antonie Van LeeuwenhoekSilva-Santana G +2 more
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Co-purification of the GroEL chaperone during outer membrane vesicle purification: insights from <i>Aeromonas salmonicida</i> subsp. <i>salmonicida</i>. [PDF]
Microbiology (Reading)Paquet MF, Charette SJ.
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GroEL−GroES-Mediated Protein Folding
Chemical Reviews, 2006AbstractChemInform 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
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Groel crystal growth and characterization
Biosystems, 2008Single 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
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Transmission Electron Microscopy of GroEL, GroES, and the Symmetrical GroEL/ES Complex
Journal of Structural Biology, 1994Two 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
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Insertion mutagenesis of Escherichiacoli GroEL
Biochemical and Biophysical Research Communications, 2003To 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
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Sublingual Vaccine with GroEL Attenuates Atherosclerosis
Journal of Dental Research, 2014Autoimmune 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
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Chaperonin GroEL: Structure and Reaction Cycle
Current Protein & Peptide Science, 2007The 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
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1994
Abstract Both Groel and GroES are essential for growth of E. coli at all temperatures4 Temperature-sensitive, conditional lethal mutants isolated on the basis of blocking phage λgrowth show impaired DNA and RNA synthesis5, a block in cell division that results in formation of long filaments without septa at the non-permissive ...
J Martin, F -U Hartl
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Abstract Both Groel and GroES are essential for growth of E. coli at all temperatures4 Temperature-sensitive, conditional lethal mutants isolated on the basis of blocking phage λgrowth show impaired DNA and RNA synthesis5, a block in cell division that results in formation of long filaments without septa at the non-permissive ...
J Martin, F -U Hartl
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