Results 61 to 70 of about 29,854 (231)
The refolding of recombinant human liver methylmalonyl-CoA mutase from inclusion bodies produced in Escherichia coli : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Biochemistry at Massey University [PDF]
Human methylmalonyl-CoA mutase (hMCM) is an adenosylcobalamin-dependent enzyme that catalyses the structural rearrangement of (R)-methylmalonyl-CoA to succinyl-CoA as pan of the catabolism of the branched chain amino acids valine, leucine and isoleucine,
Hayes, Michelle Marie
core
GroEL Binds to and Unfolds Rhodanese Posttranslationally [PDF]
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
While several oncogenic pathogens cause site‐specific cancers, uncertainties remain about many other chronic infections and combined pathogen effects, especially in non‐Western populations. Using a large case–cohort study nested within the China Kadoorie Biobank, the authors found that co‐infection was common, with a mean of 10 pathogens per individual.
Ling Yang +212 more
wiley +1 more source
Synergistic effects of microplastic and Vibrio harveyi co‐exposure on big‐belly seahorse (Hippocampus abdominalis). Seahorses were exposed to microplastics (50 beads/L of 0.2 μm SMP and 1.0 μm LMP) and injected with V. harveyi (1 × 103 CFU/mL).
Jin A Kim +4 more
wiley +1 more source
In vivo activities of GroEL minichaperones [PDF]
Fragments encompassing the apical domain of GroEL, called minichaperones, facilitate the refolding of several proteins in vitro without requiring GroES, ATP, or the cage-like structure of multimeric GroEL. We have identified the smallest minichaperone that is active in vitro in chaperoning ...
J, Chatellier +3 more
openaire +4 more sources
Reducing Campylobacter jejuni colonization in broiler chickens by in-feed supplementation with hyperimmune egg yolk antibodies [PDF]
Campylobacter infections sourced mainly to poultry products, are the most important bacterial foodborne zoonoses worldwide. No effective measures to control these infections in broiler production exist to date.
Canessa, Stefano +8 more
core +1 more source
First 20 Years of Orbitrap Mass Spectrometry as the Mainstream Analytical Technique
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
Dataset concerning GroEL chaperonin interaction with proteins
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 +5 more
doaj +1 more source
Environmental stress responses in Lactococcus lactis [PDF]
Bacteria can encounter a variety of physical conditions during their life. Bacterial cells are able to survive these (often adverse) conditions by the induction of specific or general protection mechanisms. The lactic acid bacterium Lactococcus lactis is
Kok, Jan, +2 more
core +3 more sources
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

