Results 331 to 340 of about 1,612,762 (345)
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Protein Phosphorylation In Prokaryotes
Annual Review of Microbiology, 1988xxx
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2015
Synthetic methods for phosphoryl compounds are described. The methods cover 75 classes of compounds. These include dialkyl/diaryl phosphoryl substances of general structure: ROP(O)Cl2, ArOP(O)Cl2, ROP(O)F2, ArOP(O)F2, ROP(O)(NR2)2, ROP(O)(NHNHR)2, ROP(O)(NCO)2, ROP(O)(NCS)2, ROP(O)(OH)2, ROP(O)(SR)2, RO(RS)P(O)Cl, RO(R2N)P(O)Cl, RS(R2N)P(O)Cl, (RS)2P(O)
Renard, Pierre-Yves +2 more
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Synthetic methods for phosphoryl compounds are described. The methods cover 75 classes of compounds. These include dialkyl/diaryl phosphoryl substances of general structure: ROP(O)Cl2, ArOP(O)Cl2, ROP(O)F2, ArOP(O)F2, ROP(O)(NR2)2, ROP(O)(NHNHR)2, ROP(O)(NCO)2, ROP(O)(NCS)2, ROP(O)(OH)2, ROP(O)(SR)2, RO(RS)P(O)Cl, RO(R2N)P(O)Cl, RS(R2N)P(O)Cl, (RS)2P(O)
Renard, Pierre-Yves +2 more
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2017
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene were discovered in 2004 and have been found to be the most frequently mutated gene in Parkinson's disease. LRRK2 is a large multi-domain protein with a functional GTPase and kinase domain. The signal transduction pathways in which LRRK2 is dysfunctional in the disease state are only now being ...
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Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene were discovered in 2004 and have been found to be the most frequently mutated gene in Parkinson's disease. LRRK2 is a large multi-domain protein with a functional GTPase and kinase domain. The signal transduction pathways in which LRRK2 is dysfunctional in the disease state are only now being ...
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Evidence for a phosphorylated intermediate in oxidative phosphorylation
Biochemical and Biophysical Research Communications, 1962D.E. Griffiths, R.A. Chaplain
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Exhaustion of the Phosphorylation
Acta Medica Scandinavica, 1949György Gábor +2 more
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[21] Estimation of phosphorylation stoichiometry by separation of phosphorylated isoforms
1991Publisher Summary This chapter discusses the estimation of phosphorylation stoichiometry by separation of phosphorylated isoforms. The stoichiometry of phosphorylation of a protein is of central importance in assessing the possible significance of the phosphorylation. Although it is theoretically possible that enzymatic function could be regulated by
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