Results 51 to 60 of about 29,854 (231)
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
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, 2019 Arbuscular mycorrhizal fungi (AMF) form symbioses with approximately 80% of plant species and potentially benefit their hosts (e.g. nutrient acquisition) and the soil environment (e.g. soil aggregation).
Johnston, P. +4 more
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cDNA-RNA subtractive hybridization reveals increased expression of mycocerosic acid synthase in intracellular Mycobacterium bovis BCG. [PDF]
, 2001 Identifying genes that are differentially expressed by Mycobacterium bovis BCG after phagocytosis by macrophages will facilitate the understanding of the molecular mechanisms of host cell-intracellular pathogen interactions. To identify such genes a cDNA-
Centre Gunnels Wood +7 more
core +3 more sources
Animal Research and One Health, EarlyView.Heat stress disrupts gut microbial balance in poultry, impairing nutrient absorption and immunity. This review outlines the interplay between thermal stress and microbiome dynamics and discusses integrative mitigation strategies, probiotics, phytogenics, cooling systems, and genetic adaptation to enhance poultry resilience.
O. E. Oke +9 more
wiley +1 more source
The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms
Frontiers in Molecular Biosciences, 2018 The nucleotide-free chaperonin GroEL is capable of capturing transient unfolded or partially unfolded states that flicker in and out of existence due to large-scale protein dynamic vibrational modes.
Pierce T. O'Neil +10 more
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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
Evolvability of Chaperonin Substrate Proteins [PDF]
, 2009 Molecular chaperones ensure that their substrate proteins reach the functional native state, and prevent their aggregation. Recently, an additional function was proposed for molecular chaperones: they serve as buffers (_capacitors_) for evolution by ...
Emanuele Raineri +3 more
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An Adaptation To Life In Acid Through A Novel Mevalonate Pathway. [PDF]
, 2016 Extreme acidophiles are capable of growth at pH values near zero. Sustaining life in acidic environments requires extensive adaptations of membranes, proton pumps, and DNA repair mechanisms.
Bowie, James U +3 more
core +1 more source
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
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