Results 231 to 240 of about 27,570 (293)

Low-temperature features of the psychrophilic chaperonin from Pseudoalteromonas haloplanktis. [PDF]

Arch Microbiol
Hertle E, Ursinus A, Martin J.
europepmc   +1 more source

Insights Into the Mechanism of Action of Chlorhexidine on <i>Porphyromonas gingivalis</i>. [PDF]

Int J Dent
Mejía K, Rodríguez-Hernández AP, Martínez-Hernández M.   +2 more
europepmc   +1 more source

Rubisco is slow across the tree of life. [PDF]

Proc Natl Acad Sci U S A
de Pins B, Malbranke C, Jabłońska J, Shmuel A, Sharon I, Bitbol AF, Mueller-Cajar O, Noor E, Milo R.   +8 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

Ex ante and ex post analysis of great infrastructure investment projects - the case of the fixed Oresund link [PDF]

Jensen-Butler, Christopher, Madsen, Bjarne   +1 more
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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, Peter G Schultz, Arthur L Horwich   +2 more
exaly   +4 more sources

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
exaly   +4 more sources

GroEL and the GroEL-GroES Complex

Sub-cellular biochemistry, 2017
Chaperonin is categorized as a molecular chaperone and mediates the formation of the native conformation of proteins by first preventing folding during synthesis or membrane translocation and subsequently by mediating the step-wise ATP-dependent release that result in proper folding.
N. Ishii
openaire   +3 more sources

NMR analysis of a 900K GroEL–GroES complex

Nature, 2002
Biomacromolecular structures with a relative molecular mass (M(r)) of 50,000 to 100,000 (50K 100K) have been generally considered to be inaccessible to analysis by solution NMR spectroscopy. Here we report spectra recorded from bacterial chaperonin complexes ten times this size limit (up to M(r) 900K) using the techniques of transverse relaxation ...
Jocelyne, Fiaux, Eric B, Bertelsen, Arthur L, Horwich, Kurt, Wüthrich   +3 more
openaire   +3 more sources