Results 161 to 170 of about 8,357 (212)

Phage Display Selection and In Silico Characterization of Peptides as Potential GroEL Modulators. [PDF]

Pharmaceutics
Olla S, Colombarolli SG, Siguri C, Murrau D, Vitali A.   +4 more
europepmc   +1 more source

Limited Diversity of Thermal Adaptation to a Critical Temperature in <i>Zymomonas mobilis</i>: Evidence from Multiple-Parallel Laboratory Evolution Experiments. [PDF]

Int J Mol Sci
Pattanakittivorakul S, Kato S, Kuga T, Kosaka T, Matsutani M, Murata M, Ishikawa M, Charoenpunthuwong K, Thanonkeo P, Yamada M.   +9 more
europepmc   +1 more source

Genus-targeted markers for the taxonomic identification and monitoring of coagulase-positive and coagulase-negative Staphylococcus species. [PDF]

World J Microbiol Biotechnol
Jiménez-Velásquez S, Pacheco-Montealegre ME, Torres-Higuera L, Uribe-Gutiérrez L, Burbano-David D, Dávila-Mora LL, Renjifo-Ibáñez C, Caro-Quintero A.   +7 more
europepmc   +1 more source

The -10 region adjacent to open reading frames is a common expression pattern in <i>Deinococcus-Thermus</i>. [PDF]

Life Sci Alliance
Zhong S, Wang L, Song S, Wang L, Hua Y, Lu H.   +5 more
europepmc   +1 more source

Integration of strain and process optimization to increase autotrophic growth of engineered Komagataella phaffii

Baumschabl M, Lutz L, Jecmenica M, Ata Ö, Mattanovich D.   +4 more
europepmc   +1 more source

GroES and the chaperonin-assisted protein folding cycle: GroES has no affinity for nucleotides [PDF]

FEBS Letters, 1995
The E. coli chaperonin proteins, GroEL and GroES, assist in folding newly synthesized proteins. GroES is necessary for GroEL‐assisted folding under conditions where the substrate protein cannot spontaneously fold. On the basis of photolabelling of GroES with 8‐azido‐ATP, a role for nucleotide binding to GroES in chaperonin function was suggested ...
Matthew J Todd, Ernesto Freire, George H Lorimer   +2 more
exaly   +5 more sources

Role of the amino terminal domain in GroES oligomerization [PDF]

BBA - Proteins and Proteomics, 1997
Digestions of the GroES oligomer with trypsin, chymotrypsin and Glu-C protease from Staphylococcus aureus V8 (V8) have helped to locate three regions in the GroES sequence that are sensitive to limited proteolysis and have provided information of the GroES domains involved in monomer-monomer and GroEL interaction.
OSCAR Llorca, JOSÉ L Carrascosa, Enrique Méndez   +2 more
exaly   +5 more sources

The structural stability of the co-chaperonin GroES

Journal of Molecular Biology, 1997
The structural stability of the co-chaperonin GroES has been studied by high sensitivity differential scanning calorimetry and circular dichroism under different solvent conditions. The thermal folding/unfolding of GroES is a spontaneous reversible process involving a highly cooperative transition between folded heptamers and unfolded monomers.
Olga Boudker, Matthew J Todd, Ernesto Freire   +2 more
exaly   +3 more sources

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A biochemical screen for GroEL/GroES inhibitors

Bioorganic and Medicinal Chemistry Letters, 2014
High-throughput screening of 700,000 small molecules has identified 235 inhibitors of the GroEL/GroES-mediated refolding cycle. Dose-response analysis of a subset of these hits revealed that 21 compounds are potent inhibitors of GroEL/GroES-mediated refolding (IC50
Steven M Johnson, Ingo H Engels, Achim Brinker   +2 more
exaly   +3 more sources