Zobrazeno 1 - 5
of 5
pro vyhledávání: '"W J, Rocque"'
Publikováno v:
Journal of Biological Chemistry. 268:9964-9971
Human myristoyl-CoA:protein N-myristoyltransferase (hNmt) catalyzes the transfer of myristate from CoA to the amino-terminal Gly residue of a number of cellular proteins involved in signal transduction pathways, to structural and nonstructural protei
Publikováno v:
The Journal of biological chemistry. 268(14)
Human myristoyl-CoA:protein N-myristoyltransferase (hNmt) catalyzes the transfer of myristate from CoA to the amino-terminal Gly residue of a number of cellular proteins involved in signal transduction pathways, to structural and nonstructural protei
Publikováno v:
The Journal of biological chemistry. 266(15)
The mechanism of catalysis of Escherichia coli-derived Saccharomyces cerevisiae myristoyl-CoA: protein N-myristoyltransferase (NMT) has been characterized. Previous studies indicated that a high affinity reaction intermediate forms between NMT and my
Lipopolysaccharide (LPS) bound to isolated porin was detected on polyacrylamide gels by using a carbohydrate-specific silver stain and on Western blots by using anti-lipid A monoclonal antibodies. Porin was isolated from Escherichia coli JF733 (Ra ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21cea9868f14169fb500d8ebbb1c01fe
https://europepmc.org/articles/PMC213700/
https://europepmc.org/articles/PMC213700/
Publikováno v:
Antimicrobial agents and chemotherapy. 32(3)
Lipopolysaccharide (LPS) samples isolated from a parent and two antibiotic-hypersusceptible mutant strains of Escherichia coli were analyzed for polycation affinity and level of binding. Purified salts of the LPSs from the parent strain, UB1005, and