Results 161 to 170 of about 5,066 (183)

ClpC-Mediated Sporulation Regulation at Engulfment Stage in Bacillus anthracis

Indian Journal of Microbiology, 2021
Bacterial sporulation is a conserved process utilized by members of Bacillus genus and Clostridium in response to stress such as nutrient or temperature. Sporulation initiation is triggered by stress signals perceived by bacterial cell that leads to shutdown of metabolic pathways of bacterial cells.
Nishant Kumar, Aakriti Gangwal, Nitika Sangwan, Neha Dhasmana, Chetkar Chandra Keshavam, Ekta Tyagi, Yogendra Singh   +6 more
openaire   +2 more sources

Sequestration of Ni (II), Pb (II), and Zn (II) utilizing biogenic synthesized Fe3O4/CLPC NCs and modified Fe3O4/CLPC@CS NCs: Process optimization, simulation modeling, and feasibility study

Environmental Science and Pollution Research, 2023
The present study reports low-cost novel biogenic magnetite Citrus limetta peels carbon (Fe3O4/CLPC) nanocomposites and modified Fe3O4/CLPC@CS nanocomposites cross-linked with glutaraldehyde and subsequently employed in batch mode sequestration of heavy metals ions.
Subhash Chander, Asha Gupta, Sangita Yadav   +2 more
exaly   +3 more sources

Pneumococcal proteins ClpC and UvrC as novel host plasminogen binding factors

Microbiology and Immunology, 2022
AbstractTwo plasminogen binding proteins were identified from a mouse infected with Streptococcus pneumoniae. The pneumococcal proteins were annotated as ATP‐dependent Clp protease ATP‐binding subunit (ClpC) and excinuclease ABC subunit C (UvrC) using the isobaric tags for relative and absolute quantification (iTRAQ) method.
Satoru Hirayama, Yoshihito Yasui, Karin Sasagawa, Hisanori Domon, Yutaka Terao   +4 more
openaire   +2 more sources

Expression and functional characterisation of the ClpC gene of Mycobacterium leprae: ClpC protein elicits human antibody response

Gene, 1996
This paper reports the expression of a previously described gene [Nath and Laal, Nucleic Acids Res. 18 (1990) 4935], currently identified as the clpC gene of Mycobacterium leprae, using an in vitro rabbit reticulocyte lysate-coupled transcription/translation system. The produced protein moved as a 95-kDa band on SDS-PAGE.
N, Misra, S, Habib, A, Ranjan, S E, Hasnain, I, Nath   +4 more
openaire   +2 more sources

Phylogenetic analysis predicts structural divergence for proteobacterial ClpC proteins

Journal of Structural Biology, 2018
Regulated proteolysis is required in all organisms for the removal of misfolded or degradation-tagged protein substrates in cellular quality control pathways. The molecular machines that catalyze this process are known as ATP-dependent proteases with examples that include ClpAP and ClpCP.
Justin M, Miller, Hamza, Chaudhary, Justin D, Marsee   +2 more
openaire   +2 more sources

Trapping and Identification of Cellular Substrates of the Staphylococcus aureus ClpC Chaperone [PDF]

Journal of Bacteriology, 2013
ABSTRACT ClpC is an ATP-dependent Hsp100/Clp chaperone involved in protein quality control in low-GC Gram-positive bacteria. Previously, we found that ClpC affected the expression of a large number of genes, including capsule genes in Staphylococcus aureus .
Chia Y Lee
exaly   +4 more sources

ChemInform Abstract: METAL PHTHALOCYANINE COMPLEXES. 1. SYNTHESIS AND PROPERTIES OF (RU(CLPC)(PY)2).CNTDOT.4PY AND (RU(CLPC)(PPH3)2)

Chemischer Informationsdienst, 1980
AbstractEine Mischung von festem o‐Dicyanobenzol und Ru(III)‐chlorid‐trihydrat wird bei 280°C 4 h erhitzt und dann mit siedendem Wasser und anschließend mit MeOH extrahiert.
L. J. BOUCHER, P. RIVERA
openaire   +1 more source

Structural and Motional Contributions of the Bacillus subtilis ClpC N-Domain to Adaptor Protein Interactions [PDF]

Journal of Molecular Biology, 2009
The AAA(+) (ATPases associated with a variety of cellular activities) superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. As part of a large oligomeric complex, ClpC controls an array of cellular processes by recognizing, unfolding, and providing misfolded and aggregated proteins as substrates for the ClpP peptidase ...
Douglas J Kojetin, John Cavanagh, Mark Rance   +2 more
exaly   +3 more sources

NMR assignment of the N-terminal repeat domain of Bacillus subtilis ClpC

Biomolecular NMR Assignments, 2007
The HSP100/AAA+ superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. We present here the backbone and side-chain assignments of the N-terminal repeat domain (residues 1-145) of ClpC from Bacillus subtilis.
Douglas J, Kojetin, Patrick D, McLaughlin, Richele J, Thompson, Ronald A, Venters, Mark, Rance, John, Cavanagh   +5 more
openaire   +2 more sources

Stress induction of clpC in Bacillus subtilis and its involvement in stress tolerance [PDF]

Journal of Bacteriology, 1994
A member of the clpC subfamily of stress response-related Clp ATPases was cloned from Bacillus subtilis. The B. subtilis clpC gene was induced in response to various stresses, including heat shock. Its product was identified as a general stress protein (Gsp12) described previously.
E, Krüger, U, Völker, M, Hecker
exaly   +3 more sources