Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Rachel J Service"'
Autor:
Thalia H. Bajakian, Silvia A. Cervantes, Maria A. Soria, Maïwenn Beaugrand, Ji Yun Kim, Rachel J. Service, Ansgar B. Siemer
Publikováno v:
Biomolecules, Vol 7, Iss 3, p 57 (2017)
The cytoplasmic polyadenylation element binding protein (CPEB) homologue Orb2 is a functional amyloid that plays a key regulatory role for long-term memory in Drosophila. Orb2 has a glutamine, histidine-rich (Q/H-rich) domain that resembles the Q/H-r
Externí odkaz:
https://doaj.org/article/fcc347b1ff524cf0a01e0e017891eead
Autor:
Silvia A. Cervantes, Thalia H. Bajakian, Maria A. Soria, Alexander S. Falk, Rachel J. Service, Ralf Langen, Ansgar B. Siemer
Publikováno v:
Scientific Reports
Orb2 is a functional amyloid that plays a key role in Drosophila long-term memory formation. Orb2 has two isoforms that differ in their N-termini. The N-terminus of the A isoform (Orb2A) that precedes its Q-rich prion-like domain has been shown to be
Autor:
Rachel J. Service, Junko Yano, Preston L. Dilbeck, Robert L. Burnap, Warwick Hillier, Richard J. Debus
Publikováno v:
Biochemistry. 52:8452-8464
In the 1.9 A structural model of photosystem II (PDB: 3ARC), the amino acid residue Glu333 of the D1 polypeptide coordinates to the oxygen-evolving Mn4CaO5 cluster. This residue appears to be highly significant in that it bridges the two Mn ions (MnB
Publikováno v:
Biochemistry. 52:4758-4773
The role of chloride in photosystem II (PSII) is unclear. Using structural information from PSII and a careful comparison with other chloride-activated enzymes, we proposed a role for chloride at the D2-K317 site in PSII [Pokhrel, R., et al. (2011) B
Autor:
Melodie A Strickler, Hong Jin Hwang, Robert L Burnap, Junko Yano, Lee M Walker, Rachel J Service, R. David Britt, Warwick Hillier, Richard J Debus
Publikováno v:
Philosophical Transactions of the Royal Society B: Biological Sciences. 363:1179-1188
In the recent X-ray crystallographic structural models of photosystem II, Glu354 of the CP43 polypeptide is assigned as a ligand of the O2-evolving Mn4Ca cluster. In this communication, a preliminary characterization of the CP43-Glu354Gln mutant of t
Multifrequency electron spin-echo envelope modulation (ESEEM) spectroscopy is used to ascertain the nature of the bonding interactions of various active site amino acids with the Mn ions that compose the oxygen-evolving cluster (OEC) in photosystem I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b19d1be3c0b79e8ba4fba6792573f197
https://europepmc.org/articles/PMC3418060/
https://europepmc.org/articles/PMC3418060/
Autor:
Junko Yano, Lee M. Walker, Melodie A. Strickler, Rachel J. Service, Vittal K. Yachandra, Richard J. Debus
The effect of replacing a histidine ligand on the properties of the oxygen-evolving complex (OEC) and the structure of the Mn(4)Ca cluster in Photosystem II (PSII) is studied by x-ray absorption spectroscopy using PSII core complexes from the Synecho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05a378a9ed68d4355a3c7588d4b5f0ce
https://europepmc.org/articles/PMC3059017/
https://europepmc.org/articles/PMC3059017/
Autor:
Jamie A. Stull, Troy A. Stich, Rachel J. Service, Richard J. Debus, Sanjay K. Mandal, William H. Armstrong, R. David Britt
Publikováno v:
Journal of the American Chemical Society. 132(2)
Antiferromagnetically coupled Mn(III)Mn(IV) dimers have been commonly used to study biological systems that exhibit complex exchange interactions. Such is the case for the oxygen evolving complex (OEC) in photosystem II (PSII), where we have studied