Results 181 to 190 of about 29,854 (231)

The <i>Leptospira interrogans</i> CdaA protein is a functional diadenylate cyclase. [PDF]

Infect Immun
Schuler EJA, Patel DT, Moylan AD, Miller DP, Marconi RT.   +4 more
europepmc   +1 more source

Development of a Novel Sandwich ELISA Test for the Detection of Antibodies Against Rickettsia. [PDF]

Pathogens
Quevedo-Diaz M, Kaliukanov S, Csicsay F, Hopkova D, Skultety L.   +4 more
europepmc   +1 more source

Detection and genetic diversity of Neoehrlichia mikurensis in rodents from central and southern Shanxi, China. [PDF]

Sci Rep
Cheng H, Niu J, Liu Y, Ren F, Zhao C, Cui J, Bai Y, Chen Y, Yu J, Rao H.   +9 more
europepmc   +1 more source

Detection of Tick-Borne Microorganisms, Anaplasmataceae and Piroplasmida, in <i>Sorex</i> spp. in Hokkaido, Japan. [PDF]

Microorganisms
Zamoto-Niikura A, Terui S, Sasaki M, Nakao M, Taira M, Hanaki KI.   +5 more
europepmc   +1 more source

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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

Structure and Allostery of the Chaperonin GroEL

Journal of Molecular Biology, 2013
Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of subunits presenting end cavities lined with hydrophobic binding sites for nonnative polypeptides. Once bound, substrates are subjected to forceful, concerted movements that result in their ejection from the binding surface and simultaneous encapsulation inside a ...
Helen R, Saibil, Wayne A, Fenton, Daniel K, Clare, Arthur L, Horwich   +3 more
openaire   +2 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, TRIPATHI S, SPERA, ROSANNA, NICOLINI, CLAUDIO   +3 more
openaire   +3 more sources

GroEL/ES inhibitors as potential antibiotics [PDF]

Bioorganic and Medicinal Chemistry Letters, 2016
We recently reported results from a high-throughput screening effort that identified 235 inhibitors of the Escherichia coli GroEL/ES chaperonin system [Bioorg. Med. Chem. Lett.2014, 24, 786]. As the GroEL/ES chaperonin system is essential for growth under all conditions, we reasoned that targeting GroEL/ES with small molecule inhibitors could be a ...
Andrew J Ambrose, Gregory G Anderson, Peter G Schultz   +2 more
exaly   +3 more sources

Purification and Handling of the Chaperonin GroEL

2021
GroEL is an important model molecular chaperone. Despite being extensively studied, several critical aspects of its functionality are still in dispute due partly to difficulties in obtaining protein samples of consistent purity. Here I describe an easy-to-carry-out purification protocol that can reliably produce highly purified and fully functional ...
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