l homocysteine/karijes

Veza se sprema u međuspremnik

ČlanciKliničkim ispitivanjimaPatenti

Odaberite vrstu sortiranja

10 rezultati

Engineered extrahelical base destabilization enhances sequence discrimination of DNA methyltransferase M.HhaI.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

Improved sequence specificity of the DNA cytosine methyltransferase HhaI was achieved by disrupting interactions at a hydrophobic interface between the active site of the enzyme and a highly conserved flexible loop. Transient fluorescence experiments show that mutations disrupting this interface

Specific reactions of S-nitrosothiols with cysteine hydrolases: A comparative study between dimethylargininase-1 and CTP synthetase.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

S-Transnitrosation is an important bioregulatory process whereby NO(+) equivalents are transferred between S-nitrosothiols and Cys of target proteins. This reaction proceeds through a common intermediate R-S-N(O(-))-S-R' and it has been proposed that products different from S-nitrosothiols may be

Crystal structure of Rv2258c from Mycobacterium tuberculosis H37Rv, an S-adenosyl-l-methionine-dependent methyltransferase.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

The Mycobacterium tuberculosis Rv2258c protein is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase (MTase). Here, we have determined its crystal structure in three forms: a ligand-unbound form, a binary complex with sinefungin (SFG), and a binary complex with S-adenosyl-L-homocysteine

Crystal structures of NodS N-methyltransferase from Bradyrhizobium japonicum in ligand-free form and as SAH complex.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

NodS is an S-adenosyl-L-methionine (SAM)-dependent N-methyltransferase that is involved in the biosynthesis of Nod factor (NF) in rhizobia, which are bacterial symbionts of legume plants. NF is a modified chitooligosaccharide (COS) signal molecule that is recognized by the legume host, where it

Crystal structure of YecO from Haemophilus influenzae (HI0319) reveals a methyltransferase fold and a bound S-adenosylhomocysteine.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

The crystal structure of YecO from Haemophilus influenzae (HI0319), a protein annotated in the sequence databases as hypothetical, and that has not been assigned a function, has been determined at 2.2-A resolution. The structure reveals a fold typical of S-adenosyl-L-methionine-dependent (AdoMet)

Structural basis for CARM1 inhibition by indole and pyrazole inhibitors.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

CARM1 (co-activator-associated arginine methyltransferase 1) is a PRMT (protein arginine N-methyltransferase) family member that catalyses the transfer of methyl groups from SAM (S-adenosylmethionine) to the side chain of specific arginine residues of substrate proteins. This post-translational

Characterization of human S-adenosyl-homocysteine hydrolase in vitro and identification of its potential inhibitors.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

Human S-adenosyl-homocysteine hydrolase (SAHH, E.C.3.3.1.1) has been considered to be an attractive target for the design of medicines to treat human disease, because of its important role in regulating biological methylation reactions to catalyse the reversible hydrolysis of S-adenosylhomocysteine

Crystal structure of Thermus thermophilus tRNA m1A58 methyltransferase and biophysical characterization of its interaction with tRNA.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

Methyltransferases from the m(1)A(58) tRNA methyltransferase (TrmI) family catalyze the S-adenosyl-l-methionine-dependent N(1)-methylation of tRNA adenosine 58. The crystal structure of Thermus thermophilus TrmI, in complex with S-adenosyl-l-homocysteine, was determined at 1.7 A resolution. This

Structural insight into binding mode of inhibitor with SAHH of Plasmodium and human: interaction of curcumin with anti-malarial drug targets.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

S-adenosyl-L-homocysteine hydrolase of Plasmodium falciparum (PfSAHH) is a potential drug target against malaria, and selective inhibition of PfSAHH is the excellent strategy to prevent the growth of parasite inside the host. Therefore, a comparative analysis of human S-adenosyl-L-homocysteine

Docking and in silico ADMET studies of noraristeromycin, curcumin and its derivatives with Plasmodium falciparum SAH hydrolase: a molecular drug target against malaria.

Samo registrirani korisnici mogu prevoditi članke

Prijavite se / prijavite se

The Plasmodium falciparum S-adenosyl-L-homocysteine hydrolase (pfSAHH) enzyme has been considered as a potential chemotherapeutic target against malaria due to the amino acid differences found on binding sites of pfSAHH related to human SAHH. It has been reported that noraristeromycin and some

Pridružite se našoj
facebook stranici

Herbal & Natural Medicine

Najkompletnija baza ljekovitog bilja potpomognuta naukom

Radi na 55 jezika
Biljni lijekovi potpomognuti naukom
Prepoznavanje biljaka po slici
Interaktivna GPS karta - označite bilje na lokaciji (uskoro)
Pročitajte naučne publikacije povezane sa vašom pretragom
Pretražite ljekovito bilje po učincima
Organizirajte svoja interesovanja i budite u toku sa istraživanjem vijesti, kliničkim ispitivanjima i patentima

Upišite simptom ili bolest i pročitajte o biljkama koje bi mogle pomoći, unesite travu i pogledajte bolesti i simptome protiv kojih se koristi.
* Sve informacije temelje se na objavljenim naučnim istraživanjima