Results 61 to 70 of about 8,357 (212)

Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes [PDF]

, 1995
The Escherichia coli chaperonin GroEL and its regulator GroES are thought to mediate adenosine triphosphate-dependent protein folding as an asymmetrical complex, with substrate protein bound within the GroEL cylinder.
Dasilva, A. C. R., Hegerl, R., Hayerhartl, M. K., Baumeister, W., Dasilva, A., Engel, A., Pfeifer, G., Hayerhartl, M., Muller, S., Goldie, K. N., da Silva, A. C., Hayer-Hartl, M. K., Goldie, K., Hartl, F. U., Hartl, F.   +14 more
core   +1 more source

Investigating cytokine responses in rats: Genetic immunization against tuberculosis using five Mycobacterium tuberculosis-specific genes

Pakistan Journal of Pharmaceutical Sciences
Tuberculosis, being an infectious disease, is unchecked and still hard to wipe out in the underdeveloped countries. Despite ongoing efforts, no new TB vaccine has been successfully developed in the past century beyond BCG, although DNA-based vaccines ...
Muhammad Mohsin Zaman, Mirza Imran Shahzad, Gildardo Rivera, Aeman Jilani, Mexico   +4 more
doaj   +1 more source

Functional and structural insights into cyanobacterial CO2 concentrating mechanisms: from compartmentalization to regulation

The Plant Journal, Volume 126, Issue 5, June 2026.
Significance Statement Life on Earth depends on photosynthetic CO2 fixation via the Calvin–Benson–Bassham cycle to form organic carbon. This process evolved first in cyanobacteria and was later conveyed to eukaryotes, giving rise to plastids in algae and plants. To cope with low atmospheric CO2 concentrations that developed over the course of evolution,
Erik Zimmer, Carolin Poppitz, Stephan Klähn, Khaled A. Selim   +3 more
wiley   +1 more source

Proteomic analysis reveals metabolic and regulatory systems involved the syntrophic and axenic lifestyle of Syntrophomonas wolfei.

Frontiers in Microbiology, 2015
Microbial syntrophy is a vital metabolic interaction necessary for the complete oxidation of organic biomass to methane in all-anaerobic ecosystems.
Jessica Rhea Sieber, Jessica Rhea Sieber, Bryan Regis Crable, Bryan Regis Crable, Cody Springer Sheik, Cody Springer Sheik, Gregory B. Hurst, Lars eRohlin, Lars eRohlin, Robert P. Gunsalus, Michael Joseph McInerney   +10 more
doaj   +1 more source

Multi-scale simulations provide supporting evidence for the hypothesis of intramolecular protein translocation in GroEL/GroES complexes. [PDF]

PLoS Computational Biology, 2008
The biological function of chaperone complexes is to assist the folding of non-native proteins. The widely studied GroEL chaperonin is a double-barreled complex that can trap non-native proteins in one of its two barrels.
Ivan Coluzza, Alfonso De Simone, Franca Fraternali, Daan Frenkel   +3 more
doaj   +1 more source

Review: A Structural View of the GroE Chaperone Cycle [PDF]

Journal of Structural Biology, 2001
The GroE chaperone system consists of two ring-shaped oligomeric components whose association creates different functional states. The most remarkable property of the GroE system is the ability to fold proteins under conditions where spontaneous folding cannot occur. To achieve this, a fully functional system consisting of GroEL, the cochaperone GroES,
H, Grallert, J, Buchner
openaire   +2 more sources

Outer Membrane Vesicles Mediate the Secretion and Nuclear Trafficking of a Bacterial Nucleomodulin

Journal of Extracellular Vesicles, Volume 15, Issue 5, May 2026.
(A) We propose that Helicobacter pylori secretes a nucleomodulin, Tumour Necrosis Factor‐α‐inducing protein (Tipα), predominantly via extracellular vesicles (EVs), also known as outer membrane vesicles, rather than as free protein. (B) EVs carrying Tipα enter eukaryotic cells by endocytosis and independently of surface‐expressed nucleolin, then traffic
Jack K. Emery, Variya Nemidkanam, Nina Colon, Kate R. J. Friesen, Lena H. M. Le, Angus R. Cramond, Maxine Yap, Mônica S. Barbosa, Georgie Wray‐McCann, David J. McGee, Natalia Castaño‐Rodríguez, Dongmei Tong, Caroline Skene, Laurent Terradot, Richard L. Ferrero   +14 more
wiley   +1 more source

Putting a lid on protein folding: structure and function of the co-chaperonin, GroES [PDF]

, 1996
The co-chaperonin GroES is an essential partner in protein folding mediated by the chaperonin, GroEL. Two recent crystal structures of GroES provide a structural basis to understand how GroES forms the lid on the folding-active cis ternary complex, and ...
Horwich, Arthur L., Weissman, Jonathan S., Fenton, Wayne A.   +2 more
core   +1 more source

P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coli. [PDF]

PLoS ONE, 2013
Human malaria is among the most ubiquitous and destructive tropical, parasitic diseases in the world today. The causative agent, Plasmodium falciparum, contains an unusual, essential organelle known as the apicoplast.
Anna Vitlin Gruber, Shahar Nisemblat, Gal Zizelski, Avital Parnas, Ron Dzikowski, Abdussalam Azem, Celeste Weiss   +6 more
doaj   +1 more source

Phosphate Limitation Modulates Vibrio Cholerae Outer Membrane Vesicle Formation, Composition and Toxicity

Journal of Extracellular Biology, Volume 5, Issue 5, May 2026.
ABSTRACT Vibrio cholerae inhabits phosphorus‐poor aquatic environments and host intestine, where it expresses genes regulated by the PhoB/PhoR two‐component system in response to inorganic phosphate (Pi) limitation. Like other Gram‐negative bacteria, V.
Matheus Luchetta da Fonseca, Livia Carvalho Barbosa, Beatriz Ferreira de Carvalho Patricio, Wellington da Silva Ferreira, Carolina Neumann Keim, Cedric Delporte, Pierre van Antwerpen, Jean‐Marie Ruysschaert, Paulo Mascarello Bisch, Wanda Maria Almeida von Kruger   +9 more
wiley   +1 more source