Results 151 to 160 of about 5,066 (183)

Mass spectrometry and split luciferase complementation assays reveal the MecA protein interactome of Streptococcus mutans. [PDF]

Microbiol Spectr
Qin H, Anderson D, Zou Z, Higashi D, Borland C, Kreth J, Merritt J.   +6 more
europepmc   +1 more source

Developmentally-regulated proteolysis by MdfA and ClpCP mediates metabolic differentiation duringBacillus subtilissporulation

Riley EP, Lyda JA, Reyes-Matte O, Sugie J, Kasu IR, Enustun E, Armbruster E, Ravishankar S, Isaacson RL, Camp AH, Lopez-Garrido J, Pogliano K.   +11 more
europepmc   +1 more source

Horizontal Gene Transfer of a key Translation Factor and its Role in Polyproline Proteome Evolution. [PDF]

Mol Biol Evol
Brewer TE, Wagner A.
europepmc   +1 more source

Faculty Opinions recommendation of MecA, an adaptor protein necessary for ClpC chaperone activity.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, 2003
openaire   +2 more sources

ClpP2 proteasomes and SpxA1 determine Listeria monocytogenes tartrolon B hyper-resistance. [PDF]

PLoS Genet
Engelgeh T, Wamp S, Rothe P, Herrmann J, Fischer MA, Müller R, Halbedel S.   +6 more
europepmc   +1 more source

MecA, an adaptor protein necessary for ClpC chaperone activity [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2003
ClpC of Bacillus subtilis is an ATP-dependent HSP100/Clp protein involved in general stress survival. A complex of ClpC with the protease ClpP and the adaptor protein MecA also controls competence development by regulated proteolysis of the transcription factor ComK. We investigated the
Axel Mogk, Bernd Bukau, Kürşad Turgay
exaly   +4 more sources

Adaptor protein controlled oligomerization activates the AAA+ protein ClpC [PDF]

EMBO Journal, 2006
The AAA+ protein ClpC is not only involved in the removal of misfolded and aggregated proteins but also controls, through regulated proteolysis, key steps of several developmental processes in the Gram-positive bacterium Bacillus subtilis. In contrast to other AAA+ proteins, ClpC is unable to mediate these processes without an adaptor protein like MecA.
Janine Kirstein, Axel Mogk, Bernd Bukau
exaly   +3 more sources

Structural Dynamics of the MecA-ClpC Complex [PDF]

Journal of Biological Chemistry, 2013
Ningning Li, Yigong Shi, Feng Wang
exaly   +2 more sources

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Structure and mechanism of the hexameric MecA–ClpC molecular machine

Nature, 2011
Regulated proteolysis by ATP-dependent proteases is universal in all living cells. Bacterial ClpC, a member of the Clp/Hsp100 family of AAA+ proteins (ATPases associated with diverse cellular activities) with two nucleotide-binding domains (D1 and D2), requires the adaptor protein MecA for activation and substrate targeting.
Feng Wang, Qi Hu, Jiawei Wang
exaly   +3 more sources

Interaction of In^IIIClPc and Tl^IIIClPc phthalocyanines with deprotonated porphyrin HTPP− anions. Metal-centred reduction of Tl^IIIClPc

Journal of Porphyrins and Phthalocyanines, 2021
Reactions of InIIIClPc or TlIIIClPc phthalocyanines with monodeprotonated tetraphenylporphyrin HTPP[Formula: see text] anions have been studied under reduction or in the presence of [Formula: see text]-methylimidazole ([Formula: see text]-MeIm). Formation of salt {InIII[Formula: see text]-MeIm)2(TPP[Formula: see text]}[Formula: see text]{InIII(Pc ...
Nikita R. Romanenko, Maxim A. Faraonov, Salavat S. Khasanov, Evgeniya I. Yudanova, Dmitri V. Konarev   +4 more
openaire   +1 more source