Zobrazeno 1 - 10
of 69
pro vyhledávání: '"N M Green"'
Autor:
D. B. Larkman, R. Patel, Simon Brewster, D. Blundell, P. Burke, N. M. Green, S. Richardson, R. G. Kenny, James M. A. Turner, Robert Kee, Richard Pearson
Publikováno v:
SAE International Journal of Engines. 3:938-955
The paper describes the principal features of Omnivore, a spark-ignition-based research engine designed to investigate the possibility of true wide-range HCCI operation on a variety of fossil and renewable liquid fuels. The engine project is part-fun
Publikováno v:
Journal of Biological Chemistry. 272:28815-28818
Autor:
David H. MacLennan, Tullio Pozzan, M. De Mattei, J Meldolesi, Antonello Villa, Susan Treves, N. M. Green, M Landfredi
Publikováno v:
Biochemical Journal. 271:473-480
In a search for the non-muscle equivalent of calsequestrin (the low-affinity high-capacity Ca2(+)-binding protein responsible for Ca2+ storage within the terminal cisternae of the sarcoplasmic reticulum), acidic proteins were extracted from rat liver
Autor:
David H. MacLennan, Kinya Otsu, F A Lai, Michael A. Phillips, Gerhard Meissner, Junichi Fujii, Francesco Zorzato, N M Green
Publikováno v:
Journal of Biological Chemistry. 265:2244-2256
We have cloned cDNAs encoding the rabbit and human forms of the Ca2+ release channel of sarcoplasmic reticulum. The human cDNA encodes a protein of 5032 amino acids, with a molecular weight of 563,584, which is made without an NH2-terminal signal seq
Publikováno v:
Biochemical Society Transactions. 18:841-843
Publikováno v:
Acta physiologica Scandinavica. Supplementum. 643
Alanine-scanning mutagenesis of all amino acids in transmembrane helices M4, M5, M6 and M8, which contain known Ca2+ binding residues in the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum, revealed patches of mutation-sensitivity in M4, M5 a
Autor:
N. M. Green
Publikováno v:
The Sodium Pump ISBN: 9783642725135
For several years we have been analysing the sequences of P-type ion pumps in order to obtain structural information to provide a basis for understanding the mechanism of their action. There are now over one hundred sequences in the data banks, about
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd6bd38888eb8f0b7ddf165eeb8db297
https://doi.org/10.1007/978-3-642-72511-1_21
https://doi.org/10.1007/978-3-642-72511-1_21
Publikováno v:
The Sodium Pump ISBN: 9783642725135
The Ca2+-ATPase from sarcoplasmic reticulum (SR) is exceedingly well characterized in terms of kinetics, ligand binding and amino acid sequence. For example, particular events in the reaction cycle have been assigned to specific amino acid residues b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b737a2676f84f5f65040ca0c2ad53b59
https://doi.org/10.1007/978-3-642-72511-1_22
https://doi.org/10.1007/978-3-642-72511-1_22
Autor:
N M, Green, D L, Stokes
Publikováno v:
Acta physiologica Scandinavica. Supplementum. 607
Over forty sequences of P-type ion pumps have been determined. They fall into five families showing between 20% and 50% identity in sequence. The conserved residues are concentrated in several regions which are found in all the pumps. All the defined
Publikováno v:
The Journal of biological chemistry. 265(23)
We have cloned and sequenced cDNA encoding the Ca2+ release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum. The cDNA, 16,532 base pairs in length, encodes a protein of 4,969 amino acids with a Mr of 564,711. The deduced