Results 71 to 80 of about 19,683 (209)
The Hydrophobic Nature of GroEL-Substrate Binding [PDF]
The molecular chaperone GroEl from Escherichia coli is a member of the highly conserved Hsp60 family of proteins that facilitates protein folding. A central question regarding the mechanism of GroEL-assisted refolding of proteins concerns its broad substrate specificity.
Z, Lin, F P, Schwartz, E, Eisenstein
openaire +2 more sources
Background/Purpose: Accurate identification is important for effective treatment because Enterococcus species have talents to cope with various antibiotics either by intrinsic resistance or by acquisition of mobile genetic elements.
Wei-Wen Hung +5 more
doaj +1 more source
Abstract Infection is a known cause of abdominal aortic aneurysm (AAA), and matrix metalloproteases‐2 (MMP‐2) secreted by vascular smooth muscle cells (SMCs) plays a key role in the structural disruption of the middle layer of the arteries during AAA progression.
Yi‐Wen Lin +6 more
wiley +1 more source
Summary: Protein-based stable isotope probing (protein-SIP) can link microbial taxa to substrate assimilation. Traditionally, protein-SIP requires a sample-specific metagenome-derived database for samples with unknown composition. Here, we describe GroEL-
Simon Klaes +4 more
doaj +1 more source
A recent survey in Germany revealed the wide presence of ‘Candidatus Phytoplasma ulmi’ in native elm stands. Accessions were studied for their genetic variability and phylogenetic relationship based on the conserved groEL and the variable imp gene. While
B. Schneider +3 more
doaj +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
Three Streptococcus agalactiae (group B streptococci, GBS) immunoreactive proteins: enolase (47.4 kDa), inosine 5′-monophosphate dehydrogenase (IMPDH) (53 kDa) and molecular chaperone GroEL (57 kDa) were subjected to investigation.
Anna Dobrut +7 more
doaj +1 more source
Immunization using GroEL decreases Clostridium difficile intestinal colonization. [PDF]
Clostridium difficile is a pathogen which is responsible for diarrhea and colitis, particularly after treatment with antibiotics. Clinical signs are mainly due to two toxins, TcdA and TcdB.
Séverine Péchiné +4 more
doaj +1 more source
Extracellular vesicles (EVs) derived from C. butyricum can enter intestinal epithelial cells and mediate the anti‐lipid absorption effects by delivering miRNA‐like RNAs (milRNAs), particularly milRNA‐3020179, which primarily targeted host genes majorly including PPARα. Deletion of milRNA‐3020179 in C. butyricum abolished its effects on lipid deposition
Hong Hu +9 more
wiley +1 more source
학위논문(박사) - 한국과학기술원 : 생물공학과, 1991.8, [ x, 136 p. ]Several proteins were overproduced by the powerful T7 expression system, and their solubility and enzyme activity were detemined.
김한복, Kim, Han-Bok
core +1 more source

