Results 41 to 50 of about 21,272 (221)

Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition

Biomolecules, 2014
Chaperonin GroEL is a complex oligomeric heat shock protein (Hsp60) assisting the correct folding and assembly of other proteins in the cell. An intriguing question is how GroEL folds itself.
Nataliya Ryabova, Victor Marchenkov, Nina Kotova, Gennady Semisotnov   +3 more
doaj   +1 more source

ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking. [PDF]

PLoS ONE, 2013
Group II chaperonins play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea. These proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner.
Hiroshi Sekiguchi, Ayumi Nakagawa, Kazuki Moriya, Koki Makabe, Kouhei Ichiyanagi, Shunsuke Nozawa, Tokushi Sato, Shin-ichi Adachi, Kunihiro Kuwajima, Masafumi Yohda, Yuji C Sasaki   +10 more
doaj   +1 more source

The effect of three acid-resistant isolated proteins from Lactobacillus casei on lipid and carbohydrate metabolism pathway-related genes: An In vitro study

Biomedical and Biotechnology Research Journal, 2021
Background: The role of Lactobacillus casei on human health is well documented. However, little is known about their protein effects on food digestion. Therefore, in the present study, we aimed to investigate the efficacy of three proteins of L. casei on
Golgis Karimi, Mina Saadat, Shivasadat Gheflat, Bahram Kazemi, Mojgan Bandehpour   +4 more
doaj   +1 more source

Murine Factor H Co-Produced in Yeast With Protein Disulfide Isomerase Ameliorated C3 Dysregulation in Factor H-Deficient Mice

Frontiers in Immunology, 2021
Recombinant human factor H (hFH) has potential for treating diseases linked to aberrant complement regulation including C3 glomerulopathy (C3G) and dry age-related macular degeneration.
Heather Kerr, Heather Kerr, Andrew P. Herbert, Elisavet Makou, Dariusz Abramczyk, Talat H. Malik, Hannah Lomax-Browne, Yi Yang, Yi Yang, Isabel Y. Pappworth, Isabel Y. Pappworth, Harriet Denton, Harriet Denton, Anna Richards, Kevin J. Marchbank, Kevin J. Marchbank, Matthew C. Pickering, Paul N. Barlow, Paul N. Barlow   +18 more
doaj   +1 more source

Explicit solvent molecular dynamics simulations of chaperonin-assisted rhodanese folding

, 2009
Chaperonins are known to facilitate the productive folding of numerous misfolded proteins. Despite their established importance, the mechanism of chaperonin-assisted protein folding remains unknown.
Li, Jinghai, Gao, J, Ying Ren, Ge, Wei, Wei Ge, Jian Gao, Ren, Ying, Jinghai Li, Ji Xu, Gao, Jian, Xu, Ji   +10 more
core   +1 more source

Comparative Genomics and Pathogenicity Analysis of Two Bacterial Symbionts of Entomopathogenic Nematodes: The Role of the GroEL Protein in Virulence

Microorganisms, 2022
Bacteria of the genera Xenorhabdus and Photorhabdus are symbionts of entomopathogenic nematodes. Despite their close phylogenetic relationship, they show differences in their pathogenicity and virulence mechanisms in target insects.
Abraham Rivera-Ramírez, Rosalba Salgado-Morales, Alfredo Jiménez-Pérez, Rebeca Pérez-Martínez, Blanca Inés García-Gómez, Edgar Dantán-González   +5 more
doaj   +1 more source

Heterotropic regulation and negative homotropic cooperativity

FEBS Open Bio, EarlyView.
We identified a structural module common to some proteins that couple negative cooperativity with heterotropic regulation, two features that rarely coexist. These proteins are ring‐like and present an ordered asymmetry whereby noncontacting subunits are symmetric, and their tertiary structure differs from that of contacting subunits.
Veronica Morea, Francesco Angelucci, Federica Arnesano, Gianmarco Pascarella, Patrizio Di Micco, Andrea Bellelli   +5 more
wiley   +1 more source

Chaperonin-Catalyzed Rescue of Kinetically Trapped States in Protein Folding [PDF]

, 2010
SummaryGroEL and GroES form a chaperonin nano-cage for single protein molecules to fold in isolation. The folding properties that render a protein chaperonin dependent are not yet understood.
Shi, Q. Y., Chakraborty, K., Qiaoyun Shi, Poschner, B. C., Sikor, M., Jiang, G. X., Manajit Hayer-Hartl, Guoxin Jiang, Sikor, Martin, Chakraborty, Kausik, F. Ulrich Hartl, Hayer-Hartl, M., Hayer-Hartl, Manajit, Poschner, Bernhard C., Chatila, Manal, Sinha, J., Chatila, M., Hartl, F. U., Sinha, Jyoti, Bernhard C. Poschner, Hartl, F. Ulrich, Kausik Chakraborty, Martin Sikor, Jiang, Guoxin, Lamb, Don C., Don C. Lamb, Lamb, D. C., Jyoti Sinha, Manal Chatila, Shi, Qiaoyun   +29 more
core   +1 more source

A minimal cellulosome‐like system in Cellulosilyticum lentocellum

FEBS Open Bio, EarlyView.
Cellulose‐degrading bacteria typically use cellulosomes, large multi‐enzyme complexes on a scaffold protein. In Cellulosilyticum lentocellum, we characterise a far smaller arrangement, a single scaffold bound to one cellulase through a single cohesin‐dockerin interaction.
John Allan, Amias Alstrom‐Moore, Gary W Black   +2 more
wiley   +1 more source

Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins

, 2016
Stabilizing the folded state of metastable and/or aggregation-prone proteins through exogenous ligand binding is an appealing strategy for decreasing disease pathologies caused by protein folding defects or deleterious kinetic transitions.
Subhashchandra Naik (1911184), Wesley McGinn-Straub (3040995), Mark T. Fisher (1911193), Alexandra J. Machen (3040980), Wendy A. Lea (2044258), Joshua R. Burns (3040992), Pierce T. O’Neil (3040986), Matthew T. Auton (3040989), Karen R. Khar (446747), John Karanicolas (386959), Tapan Chaudhri (3040983), Michael R. Baldwin (2267239), Alexander Tischer (2929434)   +12 more
core   +1 more source