Results 91 to 100 of about 1,339,271 (291)

Infection control in the brain and the eye

open access: yesActa Ophthalmologica, EarlyView.
Abstract The Central Nervous System (CNS), comprising the brain and the eye, is considered to have a ‘privileged’ mechanism for dealing with immunological challenge (immune privilege, IP). CNS IP has been revealed through experiments using foreign protein antigens and cell and tissue alloantigens (grafts), but evidence for a role for IP in modulating ...
John V. Forrester   +2 more
wiley   +1 more source

The cloning , expression and characterisation of bacterial chitin-binding proteins from pseudomonas aeruginosa , serratia marcescens, photorhabdus luminescens and photorhabdus asymbiotica. [PDF]

open access: yes, 2011
It is well recognised that most proteins are subject to post translational modifications and that these modifications can have specific effects on the biological properties and functions of these proteins.
Larragy, Ruth
core  

Radioimmunochemical determination of cellular retinol- and cellular retinoic acid-binding proteins in cytosols of rat tissues.

open access: yesJournal of Biological Chemistry, 1982
Radioimmunoassays have been developed for cellular retinol-binding protein and cellular retinoic acid-binding protein, postulated mediators of vitamin A action in nonvisual functions.
D. Ong, J. Crow, F. Chytil
semanticscholar   +1 more source

Pharmacological activation of NO‐cGMP signalling attenuates metabolic dysfunction‐associated steatohepatitis

open access: yesBritish Journal of Pharmacology, EarlyView.
Background and Purpose Metabolic dysfunction‐associated steatohepatitis (MASH) is linked to activation of hepatic stellate cells (HSCs) to α‐smooth muscle actin–positive myofibroblasts that produce collagen and proinflammatory cytokines. Quiescent HSCs express the NO‐cGMP signalling axis.
Krithika Rajeeth   +14 more
wiley   +1 more source

Critical role of HMGA proteins in regulation of ATM expression and in cellular response to DNA damage

open access: yes, 2009
MGA proteins are a family of chromatin remodelers involved in many cellular processes including regulation of gene expression, apoptosis and cell proliferation.
Palmieri, Dario
core  

14-3-3 Proteins Interact with a Hybrid Prenyl-Phosphorylation Motif to Inhibit G Proteins [PDF]

open access: yes, 2013
Signaling through G proteins normally involves conformational switching between GTP- and GDP-bound states. Several Rho GTPases are also regulated by RhoGDI binding and sequestering in the cytosol.
Riou, P   +62 more
core   +1 more source

Ginsenoside CK and retinol on UVA-induced photoaging exert the synergistic effect through antioxidant and antiapoptotic mechanisms

open access: yesScientific Reports
Retinol and retinoids can effectively intervene skin aging process, but usually induce skin intolerance. In this study, we aimed to determine the synergistic anti-aging effects of retinol and two retinol derivatives-hydroxypinacolone retinoate (HPR) and ...
Jingyin Zhang   +4 more
doaj   +1 more source

Hepatic retinol metabolism. Distribution of retinoids, enzymes, and binding proteins in isolated rat liver cells.

open access: yesJournal of Biological Chemistry, 1985
The main retinoids and some binding proteins and enzymes involved in retinol metabolism have been quantified in different types of rat liver cells. Hepatic perisinusoidal stellate cells contained 28-34 nmol of retinoids/10(6) cells, and parenchymal liver
R. Blomhoff   +9 more
semanticscholar   +1 more source

Retinoic Acid Signalling Regulates Zebrafish Tooth Germ Repair Following Injury

open access: yesCell Proliferation, EarlyView.
Retinoic acid signalling may regulate the repair processes in a tooth germ injury model using Tg(scpp5:Dendra2‐NTR) zebrafish and the nitroreductase (NTR)/metronidazole (MTZ) system. ABSTRACT Although the role of retinoic acid (RA) signalling in odontogenesis is well established, its involvement in the repair of injured tooth germs remains unclear.
Qiqi Liu   +4 more
wiley   +1 more source

Mapping of the ligand-binding site on the b ' domain of human PDI: interaction with peptide ligands and the x-linker region [PDF]

open access: yes, 2009
PDI (protein disulfide-isomerase) catalyses the formation of native disulfide bonds of secretory proteins in the endoplasmic reticulum. PDI consists of four thioredoxin-like domains, of which two contain redox-active catalytic sites (a and a'), and two ...
Freedman, R. B.   +15 more
core   +1 more source

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