Results 71 to 80 of about 641,669 (159)

Scotty: lattice coincidences in the Protein Data Bank

open access: yesActa Crystallographica Section D, Volume 82, Issue 7, Page 824-835, July 2026.
Scotty supports crystallographic comparisons of lattice coincidences, the interpretation of oligomeric assemblies and paracrystallinity.The application Scotty, implemented within the Phasertng codebase, was used to perform a PDB‐wide analysis of lattice coincidences.
Airlie J. McCoy   +3 more
wiley   +1 more source

Microbial Metabolite‐Stimulated Bitter Taste Receptor T2R14 Signaling Is Modulated by CFTR Interactions

open access: yesThe FASEB Journal, Volume 40, Issue 11, 15 June 2026.
Bitter taste receptors (T2Rs) play an important role in physiological and cellular responses. Bitter tasting chemicals and microbial metabolites can bind to T2R14, which enables interactions between T2R14 and specific intracellular domains of the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel.
Tejas Gupte   +8 more
wiley   +1 more source

Calcium Binding to TAT Rhodopsin

open access: yes, 2022
Rhodopsin is a large family of retinal-binding photoreceptive proteins found in animals and microbes. The retinal chromophore is normally positively charged by protonation of the Schiff base linkage, which is stabilized by the negatively charged ...
Hideki Kandori (534378)   +5 more
core   +1 more source

Nature’s toolkit for microbial rhodopsin ion pumps [PDF]

open access: yesProceedings of the National Academy of Sciences, 2014
Microbial rhodopsins function as light-driven (retinal-based) ion pumps, cation channels, or light sensors in various microorganisms [see Heberle et al.’s Retinal Proteins—You can teach an old dog new tricks (1)], are found in all three domains of life (2⇓–4), and were recently reported in viruses as well (5, 6).
Béjà, Oded, Lanyi, Janos K
openaire   +4 more sources

Protein dynamics of a light-driven Na+ pump rhodopsin probed using a tryptophan residue near the retinal chromophore

open access: yesBiophysics and Physicobiology, 2023
Direct observation of protein structural changes during ion transport in ion pumps provides valuable insights into the mechanism of ion transport. In this study, we examined structural changes in the light-driven sodium ion (Na+) pump rhodopsin KR2 on ...
Akihiro Otomo   +4 more
doaj   +1 more source

Efficacy of omega‐3 fatty acids as a functional food: a multifaceted approach to health reinforcement

open access: yesJournal of the Science of Food and Agriculture, Volume 106, Issue 8, Page 4521-4549, June 2026.
Abstract Omega‐3 fatty acids (omega‐3s) are polyunsaturated fatty acids linked with numerous health benefits. Omega‐3s exhibit multifaceted activities through various mechanisms. Eicosapentaenoic acid (EPA) alleviates oxidative stress by lowering reactive oxygen species and improving oxidative stress in brain tissues and acts against neurodegenerative ...
Md Faruque Ahmad   +12 more
wiley   +1 more source

Prediction of Structure, Function, and Spectroscopic Properties of G-Protein-Coupled Receptors: Methods and Applications [PDF]

open access: yes, 2004
G-protein-coupled receptors are of great pharmaceutical interest, comprising the majority of targets for currently marketed drugs. The theme of my thesis is the development of the structure prediction method, MembStruk, for the superfamily of G-protein ...
Trabanino, Rene Jouvanni
core   +1 more source

Photoisomerization detected in a fully wavelength‐tunable rhodopsin mimic system

open access: yesActa Crystallographica Section D, Volume 82, Issue 6, Page 664-671, June 2026.
The mechanism of retinal photoswitching is illuminated in a designed rhodopsin mimic. Two mechanisms, a conventional cis–trans isomerization and an unprecedented `photodehydration', are observed at atomic resolution in single crystals.We describe the photoisomerization of the retinylidene protonated Schiff base in human retinol‐binding protein II ...
Nona Ehyaei   +10 more
wiley   +1 more source

Mimicking Microbial Rhodopsin Isomerization in a Single Crystal

open access: yes, 2019
Bacteriorhodopsin represents the simplest, and possibly most abundant, phototropic system requiring only a retinal-bound transmembrane protein to convert photons of light to an energy-generating proton gradient.
Babak Borhan (1336584)   +7 more
core   +1 more source

Microbial rhodopsins on leaf surfaces of terrestrial plants [PDF]

open access: yesEnvironmental Microbiology, 2011
Summary The above‐ground surfaces of terrestrial plants, the phyllosphere, comprise the main interface between the terrestrial biosphere and solar radiation. It is estimated to host up to 10 26 microbial cells that may intercept part of the photon flux impinging on the ...
Atamna-Ismaeel, N   +11 more
openaire   +4 more sources

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