Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Richard S, Swanwick"'
Autor:
Andrew S.C. Rice, Kersti Karu, David L.H. Bennett, Ana Antunes-Martins, Benjamin Thomas, Min Fang, Richard S. Swanwick, William A. Foster, Eiji Yoshimi, Stephen B. McMahon, Amparo Novejarque-Gadea, Kenji Okuse
Publikováno v:
Journal of Proteome Research. 19:1592-1619
Pain and emotional distress have a reciprocal relation. The amygdala has been implicated in emotional processing. The central nucleus of the amygdala (CeA) receives nociceptive information from the dorsal horn of spinal cord and is responsible for th
Autor:
Richard S. Swanwick, Rudolf Konrad Allemann, E. Joel Loveridge, Lai-Hock Tey, Sabine L. Flitsch
Publikováno v:
FEBS Journal. 277:2171-2179
Post-translational glycosylation is one of the most abundant forms of covalent protein modification in eukaryotic cells. It plays an important role in determining the properties of proteins, and stabilizes many proteins against thermal denaturation.
Autor:
Rudolf Konrad Allemann, Lai-Hock Tey, Sabine L. Flitsch, Alison M. Daines, Richard S. Swanwick
Publikováno v:
ChemBioChem. 6:1338-1340
Heat protection. The native conformation of many proteins can be stabilised against thermal denaturation by glycosylation. Here we show that the thermal stability of the naturally nonglycosylated enzyme, dihydrofolate reductase, can be increased sign
Autor:
Ya-Chun, Chen, Alessandro, Pristerá, Mahmood, Ayub, Richard S, Swanwick, Kersti, Karu, Yosuke, Hamada, Andrew S C, Rice, Kenji, Okuse
Publikováno v:
The Journal of Biological Chemistry
Background: VGF is a neuropeptide involved in chronic pain. Results: VGF-derived peptide TLQP-21 activates macrophages. We identified gC1qR as a receptor for TLQP-21. Conclusion: TLQP-21 and gC1qR are involved in chronic pain pathways. Significance:
Publikováno v:
The FEBS journal. 277(9)
Post-translational glycosylation is one of the most abundant forms of covalent protein modification in eukaryotic cells. It plays an important role in determining the properties of proteins, and stabilizes many proteins against thermal denaturation.
Autor:
Paul J. Shrimpton, Rudolf Konrad Allemann, Richard S. Swanwick, Jiayun Pang, Giovanni Maglia, Robert J. Rodriguez, Rhiannon M. Evans, Lai-Hock Tey
Publikováno v:
Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 361(1472)
Dihydrofolate reductase (DHFR) maintains the intracellular pool of tetrahydrofolate through catalysis of hydrogen transfer from reduced nicotinamide adenine dinucleotide to 7,8-dihydrofolate. We report results for pre-steady-state kinetic studies of
Publikováno v:
The Biochemical journal. 394(Pt 1)
The enzyme DHFR (dihydrofolate reductase) catalyses hydride transfer from NADPH to, and protonation of, dihydrofolate. The physical basis of the hydride transfer step catalysed by DHFR from Escherichia coli has been Studied through the measurement of
Publikováno v:
Organicbiomolecular chemistry. 3(4)
Apparently homogenous glycoproteins can be synthesised in good yield by a combination of site directed mutagenesis, a highly flexible but selective chemical derivatisation and efficient purification through the use of glycosyl thiosulfonates such as
Publikováno v:
Journal of the American Chemical Society. 131:6926-6927
We report here solvent kinetic isotope effects for two dihydrofolate reductases, namely the monomeric, mesophilic enzyme from E. coli (EcDHFR) and the dimeric, thermophilic enzyme from Thermotoga maritima (TmDHFR). Multiple isotope effects reveal mec
Autor:
Rudolf K. Allemann, Rhiannon M. Evans, Lai-hock Tey, Giovanni Maglia, Jiayun Pang, Robert Rodriguez, Paul J. Shrimpton, Richard S. Swanwick
Publikováno v:
Philosophical Transactions of the Royal Society B: Biological Sciences; Aug2006, Vol. 361 Issue 1472, p1317-1321, 5p