Results 31 to 40 of about 30,272 (208)

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES

Frontiers in Microbiology, 2017
Chaperonin GroEL (Cpn60) requires cofactor GroES (Cpn10) for protein refolding in bacteria that possess single groEL and groES genes in a bicistronic groESL operon.
Yue-zhong Li, Li Zhuo, Yan Wang, Yan Wang, Zheng Zhang, Jian Li, Xiao-Hua Zhang   +6 more
doaj   +1 more source

Bartonella infections in fleas (Siphonaptera : Pulicidae) and lack of Bartonellae in ticks (Acari : Ixodidae) from Hungary [PDF]

, 2006
Fleas (95 Pulex irritans, 50 Ctenocephalides felis, 45 Ctenocephalides canis) and ixodid ticks (223 Ixodes ricinus, 231 Dermacentor reticulatus, 204 Haemaphysalis concinna) were collected in Hungary and tested, in assays based on PCR, for Bartonella ...
Márialigeti, Károly, Sréter, Tamás, Sréter-Lancz, Z., Széll, Z., Tornyai, K.   +4 more
core   +1 more source

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction [PDF]

Scientific Reports, 2017
AbstractChaperonin and cochaperonin, represented by E. coli GroEL and GroES, are essential molecular chaperones for protein folding. The double-ring assembly of GroEL is required to function with GroES, and a single-ring GroEL variant GroELSR forms a stable complex with GroES, arresting the chaperoning reaction cycle.
Illingworth, Melissa, Ellis, Holly, Chen, Lingling   +2 more
openaire   +2 more sources

The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues

Biomolecules, 2021
Group I chaperonins are a highly conserved family of essential proteins that self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins in bacteria and organelles.
Karla N. Valenzuela-Valderas, Gabriel Moreno-Hagelsieb, John R. Rohde, Rafael A. Garduño   +3 more
doaj   +1 more source

GroEL is an immunodominant surface-exposed antigen of Rickettsia typhi

PLoS ONE, 2021
Rickettsioses are neglected and emerging potentially fatal febrile diseases that are caused by obligate intracellular bacteria, rickettsiae. Rickettsia (R.) typhi and R.
Jessica Rauch, Jessica Barton, Marcel Kwiatkowski, Malte Wunderlich, Pascal Steffen, Kristin Moderzynski, Stefanie Papp, Katharina Höhn, Hella Schwanke, Susanne Witt, Ulricke Richardt, Ute Mehlhoop, Hartmut Schlüter, Verena Pianka, Bernhard Fleischer, Dennis Tappe, Anke Osterloh   +16 more
doaj   +2 more sources

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution

Biomolecules, 2020
The main events in chaperone-assisted protein folding are the binding and ligand-induced release of substrate proteins. Here, we studied the location of denatured proteins previously bound to the GroEL chaperonin resulting from the action of the GroES co-
Victor Marchenkov, Andrey Gorokhovatsky, Natalia Marchenko, Tanya Ivashina, Gennady Semisotnov   +4 more
doaj   +1 more source

Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622. [PDF]

PLoS Genetics, 2013
The gene encoding the GroEL chaperonin is duplicated in nearly 30% of bacterial genomes; and although duplicated groEL genes have been comprehensively determined to have distinct physiological functions in different species, the mechanisms involved have ...
Yan Wang, Wen-yan Zhang, Zheng Zhang, Jian Li, Zhi-feng Li, Zai-gao Tan, Tian-tian Zhang, Zhi-hong Wu, Hong Liu, Yue-zhong Li   +9 more
doaj   +1 more source

In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution

Frontiers in Molecular Biosciences, 2023
Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating ...
Hideki Taguchi, Ayumi Koike-Takeshita
doaj   +1 more source

Diverse tick-borne microorganisms identified in free-living ungulates in Slovakia [PDF]

, 2018
Background: Free-living ungulates are hosts of ixodid ticks and reservoirs of tick-borne microorganisms in central Europe and many regions around the world.
A Alberti, A Mysterud, A Nahayo, A Obiegala, A Ohlson, A Ortuňo, A Pereira, A Pereira, A Rizzoli, A Zintl, AO Michel, AS Faria, B Flaisz, B Skotarczak, B Víchová, BL Herwaldt, C Billinis, C Huhn, C Kiffner, C Kiffner, C Martin, C Silaghi, C Silaghi, C Silaghi, CA Becker, D Duh, D González-Barrio, D Hulinska, D Hulínská, D Žele, E Dorko, E Overzier, E Overzier, E Špitalská, E Špitalská, Elena Kocianová, Eva Špitalská, F Strle, F Veronesi, FCA Pacilly, H Polin, H Sprong, H Sprong, H-P Fuehrer, Hein Sprong, HK Hinaidy, HS Ginsberg, I Baráková, I Baráková, J García-Sanmartín, J Gray, J Hapunik, J Michalik, J Michalik, J Nosek, J Stańczak, J Řeháček, J Řeháček, JM Medlock, JM Rijks, JS Liz, JW Courtney, K Häselbarth, K Kurtenbach, K Reiterová, K Siuda, K Stefanidesova, K Strasek Smrdel, K Tamura, K Štefanidesová, KT Friedhoff, L Berthová, L Gilbert, L Lempereur, L Lempereur, L Malandrin, L Minichová, L Qviller, L Tomassone, Lenka Mahríková, Lenka Minichová, Leonhard Schnittger, M Adamska, M Battilani, M Derdáková, M Di Domenico, M Jouglin, M Kauffmann, M Kazimírová, M Maurin, M Petrovec, M Petrovec, M Pfäffle, M Salman, M Sawczuk, M Sawczuk, Manoj Fonville, MJ Yabsley, MO Andersson, MP Tampieri, Mária Kazimírová, N Saitou, NS Alexander, O Rosef, P Heyman, P Zeman, R Cézanne, R Galuppi, R Welc-Falęciak, Radoslav Caban, RC Galindo, RF Massung, RL Regnery, S Casati, S Hornok, S Hornok, S Hornok, S Jahfari, S Jahfari, S Kumar, S Schorn, S Stuen, S Stuen, S Stuen, S Zanet, SE Randolph, SE Randolph, T Dugat, T Dugat, T Kiss, T Vor, TR Hofmeester, U Mackenstedt, V Tagliapietra, V Černý, VV Ebani, VV Ebani, VV Ebani, VV Ebani, W Scharf, Z Hamšíková, Z Hamšíková, Z Hamšíková Svitálková, Z Woldehiwet, Zuzana Hamšíková, Ø Hammer, Ø Øines   +146 more
core   +4 more sources

Crystal Structure of Wild-type Chaperonin GroEL [PDF]

Journal of Molecular Biology, 2005
The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and represents the reference structure, facilitating the study of structural and functional differences observed in GroEL variants. Until now the crystal structure of the mutant Arg13Gly, Ala126Val GroEL was used for this purpose.
Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H   +4 more
openaire   +10 more sources