Results 51 to 60 of about 18,538 (219)
GroEL Binds to and Unfolds Rhodanese Posttranslationally [PDF]
Journal of Biological Chemistry, 1996 The Escherichia coli chaperone GroEL is a member of a class of molecular chaperones that possesses a stacked double ring structure containing seven subunits per ring, with approximately 60-kDa subunits. It has been suggested that newly synthesized proteins may interact with a eukaryotic homolog of GroEL co-translationally, thereby sequestering the ...
B G, Reid, G C, Flynn
openaire +2 more sources
Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]
, 2006 In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, T., Maier, Tobias
core
Food Chemistry International, EarlyView.Enterocin‐producing Enterococcus faecium RSCUDR7 from camel milk exhibited strong probiotic and antimicrobial properties, along with stability in skim milk. Its suitability as a safe and effective dairy starter highlights its potential for developing functional probiotic dairy products.
Rahul Singhal +4 more
wiley +1 more source
Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones [PDF]
, 2011 Folding of newly synthesized proteins is an essential part of protein biosynthesis and misfolding can result in protein aggregation which can also lead to several severe diseases.
Sikor, Martin
core
Bacterial Heat Shock Protein GroEL (Hsp64) Exerts Immunoregulatory Effects on T Cells by Utilizing Apoptosis. [PDF]
PLoS ONE, 2016 Aggregatibacter actinomycetemcomitans (Aa) expresses a 64-kDa GroEL protein belonging to the heat shock family of proteins. This protein has been shown to influence human host cells, but the apoptotic capacity of the GroEL protein regarding T cells is ...
Ayten Nalbant, Melis Kant
doaj +1 more source
First 20 Years of Orbitrap Mass Spectrometry as the Mainstream Analytical Technique
Mass Spectrometry Reviews, EarlyView.ABSTRACT This review traces the first 20 years of Orbitrap mass spectrometry as a mainstream high‑resolution and accurate‑mass (HR/AM) technology. It outlines the historical development of the Orbitrap analyzer, the evolution of major instrument families, and the key technological innovations that enabled its widespread adoption. Particular emphasis is
Alexander Makarov
wiley +1 more source
ROLE OF SALT BRIDGES IN GROEL ALLOSTERY [PDF]
, 2014 Chaperonin GroEL facilitates protein folding with two stacked back-to-back, identical rings and the "lid", co-chaperonin GroES. The mis-folded/unfolded substrate protein (SP) adjusts the chaperonin cycling from an asymmetric to a symmetric cycle by ...
Yang, Dong
core +1 more source
BMC Microbiology, 2021 Background Leptospirosis is a zoonotic disease caused by infection with spirochetes from Leptospira genus. It has been classified into at least 17 pathogenic species, with more than 250 serologic variants.
Joana Dias Ho +8 more
doaj +1 more source
Mass Spectrometry Reviews, EarlyView.ABSTRACT Top‐down proteomics (TDP) characterizes proteoforms in cells, tissues, and biofluids, in discovery mode and on a global scale, requiring analytical tools with high peak capacity for proteoform separation and high sensitivity for proteoform detection, given the extremely high proteoform complexity and wide proteoform concentration dynamic range.
Guijie Zhu +5 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 +8 more
doaj +1 more source