Results 51 to 60 of about 30,272 (208)

Evolvability of Chaperonin Substrate Proteins [PDF]

, 2009
Molecular chaperones ensure that their substrate proteins reach the functional native state, and prevent their aggregation. Recently, an additional function was proposed for molecular chaperones: they serve as buffers (_capacitors_) for evolution by ...
Emanuele Raineri, Luis Serrano, Paolo Ribeca, Tobias Maier   +3 more
core   +1 more source

Latent Neoehrlichia mikurensis Infections May Be Reactivated in Patients With B‐Cell Lymphomas Treated With Rituximab

Immunology, EarlyView.
Eight percent of this cohort of patients had a latent Neoehrlichia mikurensis infection. It was only the latently infected patients who had N. mikurensis‐specific T cells, not the matched B‐cell lymphoma patients without the infection. The T‐cell responses of latently infected patients included perforin‐expressing Th1 and CD8+ T cells that upregulated ...
Linda Wass, Catharina Lewerin, Daniel Jaén‐Luchoro, Christine Lingblom, Christine Wennerås   +4 more
wiley   +1 more source

The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms

Frontiers in Molecular Biosciences, 2018
The nucleotide-free chaperonin GroEL is capable of capturing transient unfolded or partially unfolded states that flicker in and out of existence due to large-scale protein dynamic vibrational modes.
Pierce T. O'Neil, Alexandra J. Machen, Benjamin C. Deatherage, Caleb Trecazzi, Alexander Tischer, Venkata R. Machha, Matthew T. Auton, Michael R. Baldwin, Tommi A. White, Tommi A. White, Mark T. Fisher   +10 more
doaj   +1 more source

Capturing the essence of folding and functions of biomolecules using Coarse-Grained Models

, 2011
The distances over which biological molecules and their complexes can function range from a few nanometres, in the case of folded structures, to millimetres, for example during chromosome organization. Describing phenomena that cover such diverse length,
A Dhar, A Elcock, A Elcock, A Grosberg, A Grosberg, A Minton, A Pisliakov, A Podtelezhnikov, A Rychkova, A Savelyev, A Vologodskii, AA Podtelezhnikov, B Messer, BJ Alder, C Bustamante, C Clementi, C Hyeon, C Hyeon, C Hyeon, C Hyeon, C Hyeon, C Hyeon, C Hyeon, C Hyeon, C Hyeon, C Hyeon, D Thirumalai, D Thirumalai, D Thirumalai, D Thirumalai, D Thirumalai, E Koculi, E Lieberman-Aiden, E O'Brien, E Shakhnovich, EP O'Brien, F Valle, G Lorimer, G Papoian, G Ziv, H Liu, H Ma, HX Zhou, I Tinoco Jr., J Chen, J Harms, J Karanicolas, J Straub, JD Honeycutt, JM Fernandez, JN Onuchic, KA Dill, M Levitt, M Mickler, M Strajbl, M Takano, ME Fisher, MJ Todd, MS Cheung, N Hirokawa, N Koga, N Toan, OK Dudko, P Weinkam, PB Moore, PC Whitford, Q Du, R Russell, R Tehver, R Tehver, RD Vale, RD Vale, RI Dima, RW Pastor, S Jun, S Jun, S Jun, S Kamerlin, S Kirkpatrick, S Moghaddam, SB Smith, SJ Chen, SJ Marrink, T Cloutier, T Cremer, T Kirkpatrick, T Veitshans, V Lubchenko, Z Liu, Z Xu   +89 more
core   +1 more source

RomA, A Periplasmic Protein Involved in the Synthesis of the Lipopolysaccharide, Tunes Down the Inflammatory Response Triggered by Brucella [PDF]

, 2018
Brucellaceae are stealthy pathogens with the ability to survive and replicate in the host in the context of a strong immune response. This capacity relies on several virulence factors that are able to modulate the immune system and in their structural ...
Altabe, Silvia Graciela, Casabuono, Adriana Cristina, Cassataro, Juliana, Couto, Alicia Susana, Czibener, Cecilia, Fulgenzi, Fabiana Rosa, Guaimas, Francisco Fernando, Pasquevich, Karina Alejandra, Spera, Juan Manuel, Ugalde, Juan Esteban, Valguarnera, Pablo Ezequiel   +10 more
core   +1 more source

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

Novel cryo-EM structure of an ADP-bound GroEL–GroES complex

Scientific Reports, 2021
The GroEL–GroES chaperonin complex is a bacterial protein folding system, functioning in an ATP-dependent manner. Upon ATP binding and hydrolysis, it undergoes multiple stages linked to substrate protein binding, folding and release.
Sofia S. Kudryavtseva, Evgeny B. Pichkur, Igor A. Yaroshevich, Aleksandra A. Mamchur, Irina S. Panina, Andrei V. Moiseenko, Olga S. Sokolova, Vladimir I. Muronetz, Tatiana B. Stanishneva-Konovalova   +8 more
doaj   +1 more source

Allo-network drugs: Extension of the allosteric drug concept to protein-protein interaction and signaling networks [PDF]

, 2013
Allosteric drugs are usually more specific and have fewer side effects than orthosteric drugs targeting the same protein. Here, we overview the current knowledge on allosteric signal transmission from the network point of view, and show that most ...
Csermely, Péter, Nussinov, Ruth, Szilágyi, András   +2 more
core   +2 more sources

Porphyromonas gingivalis GroEL exacerbates orthotopic allograft transplantation vasculopathy via impairment of endothelial cell function

Molecular Oral Microbiology, EarlyView.
Abstract Orthotopic allograft transplantation (OAT) is a significant approach to addressing organ failure. However, persistent immune responses to the allograft affect chronic rejection, which induces OAT vasculopathy (OATV) and organ failure. Porphyromonas gingivalis can infiltrate remote organs via the bloodstream, thereby intensifying the severity ...
Chien‐Sung Tsai, Chun‐Yao Huang, Yi‐Ting Tsai, Chun‐Ming Shih, Ze‐Hao Lai, Chen‐Wei Liu, Yi‐Wen Lin, Feng‐Yen Lin   +7 more
wiley   +1 more source

Dataset concerning GroEL chaperonin interaction with proteins

Data in Brief, 2016
GroEL chaperonin is well-known to interact with a wide variety of polypeptide chains. Here we show the data related to our previous work (http://dx.doi.org/10.1016/j.pep.2015.11.020 [1]), and concerning the interaction of GroEL with native (lysozyme, α ...
V.V. Marchenkov, N.Yu. Marchenko, A.L. Kaysheva, N.V. Kotova, I.A. Kashparov, G.V. Semisotnov   +5 more
doaj   +1 more source