Results 281 to 290 of about 1,594,903 (314)
Some of the next articles are maybe not open access.
N→S phosphoryl migration in phosphoryl glutathion
International Journal of Peptide and Protein Research, 1993It was found that in the case of N‐(diisopropylphosphoryl) glutathion (reduced form), 2, N→ S phosphoryl migration took place, but not for N,N‐bis(diisopropylphosphoryl) glutathion (oxidized form) or N‐diisopropylphosphoryl cysteine. These results were deduced by 31P‐NMR tracing experiments.
H J, Yang, J, Liu, Y F, Zhao
openaire +2 more sources
N-Phosphoryl oxazolidinones as effective phosphorylating agents
Tetrahedron Letters, 2004AbstractFor Abstract see ChemInform Abstract in Full Text.
Simon Jones, Chaiwat Smanmoo
openaire +1 more source
Evidence of a phosphorylated intermediate in mitochondrial oxidative phosphorylation
Biochemical and Biophysical Research Communications, 1970Abstract The effects of aurovertin and oligomycin on the rates of oxidative phosphorylation and arsenate-stimulated respiration have been studied over a wide range of concentrations. It has been found that both arsenate and phosphate can react with an energy-rich intermediate of oxidative phosphorylation even when reaction with ADP is prevented by ...
R L, Cross, J H, Wang
openaire +2 more sources
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 ...
openaire +2 more sources
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 ...
openaire +2 more sources
Phosphorylation of rhodopsin: Most rhodopsin molecules are not phosphorylated
Biochemical and Biophysical Research Communications, 1974Abstract Phosphorylation of rod membrane proteins is a light-dependent reaction. Most rhodopsin molecules, however, are not phosphorylated. The protein that is highly phosphorylated (>3 moles phosphate per mole phosphorylated protein) appears to be a rhodopsin species that is different from the rest or is located in different parts of the rod ...
H, Shichi, R L, Somers, P J, O'Brien
openaire +2 more sources
The thymidine phosphorylating kinases
Biochimica et Biophysica Acta, 1961Abstract The pattern of the phosphorylation reactions when supernatant fractions from leukaemic spleen and lymph nodes of mice are incubated with an ATP regenerating system and [2- 14 C]thymidine has been studied. The results indicate that TDP is not an intermediate in the formation of TTP, the latter compound being formed by pyrophosphate addition ...
P A, BIANCHI +3 more
openaire +2 more sources
Phosphorylation of 19S Thyroglobulin
1988Thyroglobulin (TG), one of the largest known eukaryotic proteins (Mr 660.000, sedimentation coefficient 19S), plays a central role in thyroid hormonogenesis. TG presents several characteristics of special interest: (i) it represents the major biosynthetic product of thyroid follicular cell1; (ii) under denaturing conditions it can be dissociated into ...
Tassi V. +3 more
openaire +3 more sources
Evidence for a phosphorylated intermediate in oxidative phosphorylation
Biochemical and Biophysical Research Communications, 1962D E, GRIFFITHS, R A, CHAPLAIN
openaire +2 more sources
Protein Phosphorylation In Prokaryotes
Annual Review of Microbiology, 1988xxx
openaire +3 more sources