Results 81 to 90 of about 29,854 (231)

Epitopes of Immunoreactive Proteins of Streptococcus Agalactiae: Enolase, Inosine 5′-Monophosphate Dehydrogenase and Molecular Chaperone GroEL

Frontiers in Cellular and Infection Microbiology, 2018
Three Streptococcus agalactiae (group B streptococci, GBS) immunoreactive proteins: enolase (47.4 kDa), inosine 5′-monophosphate dehydrogenase (IMPDH) (53 kDa) and molecular chaperone GroEL (57 kDa) were subjected to investigation.
Anna Dobrut, Ewa Brzozowska, Sabina Górska, Marcelina Pyclik, Andrzej Gamian, Małgorzata Bulanda, Elzbieta Majewska, Monika Brzychczy-Włoch   +7 more
doaj   +1 more source

Fungal, not insect: Revisiting a misidentified Bemisia tabaci protein interacting with a begomovirus coat protein

Insect Molecular Biology, EarlyView.
A small heat‐shock protein (HSP16) previously reported as insect‐derived in Bemisia tabaci actually originates from a fungal species of the genus Wallemia. BLAST, genome survey and phylogenetic analyses support the fungal origin and clarify persistent misattribution in the literature.
Jesús Navas‐Castillo, Elvira Fiallo‐Olivé   +1 more
wiley   +1 more source

GroEL/GroES Mechanism of Action and Formation of Complexes During Reaction Cycle: A Matter of Debate [PDF]

Journal of Stress Physiology & Biochemistry
The bacterial chaperonin GroEL alongwith its cochaperonin GroES is the paradigmatic molecular chaperone machine for protein folding. Most bacterial proteins require the GroEL chaperonin for proper folding.
Sutrisha Kundu, Vivek Raychaudhuri, Sudipa Saha   +2 more
doaj  

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

The Hydrophobic Nature of GroEL-Substrate Binding [PDF]

Journal of Biological Chemistry, 1995
The molecular chaperone GroEl from Escherichia coli is a member of the highly conserved Hsp60 family of proteins that facilitates protein folding. A central question regarding the mechanism of GroEL-assisted refolding of proteins concerns its broad substrate specificity.
Z, Lin, F P, Schwartz, E, Eisenstein
openaire   +2 more sources

Autoimmunity and Periodontitis

Journal of Periodontal Research, EarlyView.
In a microbe‐driven inflammatory environment, peptidyl‐arginine deiminase (PAD) enzymes from neutrophils and Porphyromonas gingivalis citrullinate both microbial and self‐antigens. B cell presentation of citrullinated or self‐mimicking epitopes activates T cells that assist B cells in antibody isotype switching, affinity maturation, epitope spreading ...
Massimo Costalonga, Vivek Thumbigere‐Math, Mark C. Herzberg   +2 more
wiley   +1 more source

DnaK Functions as a Central Hub in the E. coli Chaperone Network

Cell Reports, 2012
Cellular chaperone networks prevent potentially toxic protein aggregation and ensure proteome integrity. Here, we used Escherichia coli as a model to understand the organization of these networks, focusing on the cooperation of the DnaK system with the ...
Giulia Calloni, Taotao Chen, Sonya M. Schermann, Hung-chun Chang, Pierre Genevaux, Federico Agostini, Gian Gaetano Tartaglia, Manajit Hayer-Hartl, F. Ulrich Hartl   +8 more
doaj   +1 more source

Immunization using GroEL decreases Clostridium difficile intestinal colonization. [PDF]

PLoS ONE, 2013
Clostridium difficile is a pathogen which is responsible for diarrhea and colitis, particularly after treatment with antibiotics. Clinical signs are mainly due to two toxins, TcdA and TcdB.
Séverine Péchiné, Claire Hennequin, Céline Boursier, Sandra Hoys, Anne Collignon   +4 more
doaj   +1 more source

High prevalence of a host‐associated Anaplasma lineage in wild coatis (Nasua nasua) from the Brazilian Atlantic Forest

Medical and Veterinary Entomology, EarlyView.
Anaplasma sp. DNA was detected in 47.9% of free‐ranging coatis (Nasua nasua) sampled in Iguaçu National Park, southern Brazil. Molecular analyses revealed a genetically distinct Anaplasma lineage infecting coatis, differing from Anaplasma strains detected in associated tick populations.
Matheus Dias Cordeiro, Paulo César Magalhães‐Matos, Isadora dos Santos Dias, Jônathan David Ribas Chagas, Olívia Zen Gianfrancisco, Ellen Meireles Brandão, Claudia Bezerra da Silva, Bruna de Azevedo Baêta   +7 more
wiley   +1 more source

The metabolic enzyme AdhE controls the virulence of Escherichia coli O157:H7 [PDF]

, 2014
Classical studies have focused on the role that individual regulators play in controlling virulence gene expression. An emerging theme, however, is that bacterial metabolism also plays a key role in this process.
Abernathy, Anders, Baumler, Bergman, Boehm, Booth, Campellone, Chevance, Clark, Coburn, Creek, Echave, Elliott, Emmerson, Frankel, Fukuda, Fukuda, Hansen, Hartland, Hayashi, Hu, Hu, Hueck, Iyoda, Kendall, Kuhn, Mahajan, Massé, Minato, Nataro, Naylor, Noris, Paul, Porter, Rietsch, Rietsch, Ritchie, Ritchie, Roe, Roe, Scheltema, Shevchenko, Smith, Soutourina, Sullivan, Sánchez-Sanmarti, Thao, Tobe, Tree, Turner, Vytvytska, Wang, Wang, Weinert, Wolfe, Wolfe, Wolfe, Zhang, Zhao, Zumbrun   +59 more
core   +2 more sources