Results 241 to 250 of about 27,570 (293)

Activation of Wheat Defense Response by Buchnera aphidicola-Derived Small Chaperone Protein GroES in Wheat Aphid Saliva.

Journal of Agricultural and Food Chemistry, 2022
Salivary proteins secreted by aphids during feeding play an important role in regulating the plant defense response. We used mass spectrometry to identify 155 proteins from the wheat aphid, Sitobion miscanthi, among which 44 proteins were derived from ...
Qian Li, Yu Fu, Xiaobei Liu, Jingxuan Sun, M. Hou, Yong Zhang, Julian Chen   +6 more
semanticscholar   +1 more source

The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex

Nature, 1997
Arthur L Horwich
exaly   +2 more sources

The GroEL–GroES Chaperonin Machine: A Nano-Cage for Protein Folding

Trends in Biochemical Sciences, 2016
Manajit Hayer-Hartl, Andreas Bracher, F Ulrich Hartl   +2 more
exaly   +2 more sources

GroE structures galore

Nature Structural Biology, 1996
The stuctures of the co-chaperonin GroES and of the GroEL•ATPγS complex raise a host of tantalizing questions and whet the appetite for even more challenging structures, the various GroEL•nucleotide•GroES complexes which facilitate folding.
George H. Lorimer, Matthew J. Todd
openaire   +1 more source

THE UNIVERSALLY CONSERVED GroE (Hsp60) CHAPERONINS

Annual Review of Microbiology, 1991
INTRODUCTION . . . . . . . . . . . . . . . . . . . . . . .. . . . . . . . . .. . . .. . . .. . . . . ... ...... . . . . . . . . . . . . . . . . ... . . . . . . . . . . 301 THE groE OPERON . . . . . . . . . . . .... . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
J, Zeilstra-Ryalls, O, Fayet, C, Georgopoulos   +2 more
openaire   +3 more sources

GroES Promotes the T to R Transition of the GroEL Ring Distal to GroES in the GroEL−GroES Complex^†

Biochemistry, 1997
Curves of initial rates of ATP hydrolysis by GroEL as a function of ATP concentration, in the presence of fixed concentrations of GroES, were found to deviate from sigmoidal kinetics. Instead of the lag phase typical of sigmoidal curves, a linear phase is observed at low ATP concentrations.
E, Inbar, A, Horovitz
openaire   +2 more sources

Lord of the Rings: GroES Structure

Science, 1996
The crystal structure of the chaparonin GroES, which together with GroEL assists in the folding of many proteins in Escherichia coli , is reported in this issue of Science by Mande et al . ( p. 203 ). In this Perspective, M. Mayhew and F.
M, Mayhew, F U, Hartl
openaire   +2 more sources

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

Nature, 1996
Samuel J Landry, Lila M Gierasch
exaly   +2 more sources

Bis-sulfonamido-2-phenylbenzoxazoles Validate the GroES/EL Chaperone System as a Viable Antibiotic Target.

Journal of the American Chemical Society
We recently reported on small-molecule inhibitors of the GroES/GroEL chaperone system as potential antibiotics against Escherichia coli and the ESKAPE pathogens but were unable to establish GroES/GroEL as the cellular target, leading to cell death.
Jack Godek, J. Sivinski, Edmond R Watson, Felicidad Lebario, Wenli Xu, Mckayla Stevens, Christopher J. Zerio, Andrew J Ambrose, Xiaoyi Zhu, Carlee A Trindl, Donna D Zhang, Steven M Johnson, Gabriel C. Lander, Eli Chapman   +13 more
semanticscholar   +1 more source

GroEL and GroES

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
openaire   +1 more source