Retraction of Mechanistic Basis for Epstein–Barr Virus Ribonucleotide

Retraction of Mechanistic Basis for EpsteinâBarr Virus Ribonucleotide

Jul 23, 2012 - Retraction of âPreorganized Chromophores Facilitate Triplet Energy Migration, Annihilation and Upconverted Singlet Energy Collectionâ.

Peptidomimetic Inhibitors of Herpes Simplex Virus Ribonucleotide

Publication Date (Web): October 11, 1996 ... 1357, a significantly more potent antiviral compound than our previously published best compound, BILD 1263.

Mechanistic Basis for Suicide Inactivation of Porphobilinogen

Institute for Cancer Research, Fox Chase Cancer Center, 7701 Burholme AVenue, Philadelphia, PennsylVania 19111, ... Its contents are solely the responsibility.


4,7-Dioxosebacic acid (4,7-DOSA) is an active site-directed irreversible inhibitor of porphobilinogen synthase (PBGS). PBGS catalyzes the first common step in ...


Mechanistic Basis for Suicide Inactivation of Porphobilinogen Synthase by. 4,7-Dioxosebacic Acid, an Inhibitor That Shows Dramatic Species Selectivityâ .


Mechanistic Basis for Suicide Inactivation of Porphobilinogen Synthase by .... (Î²ME) from Fluka (Buchs, Switzerland) was vacuum- distilled prior to use.

Structural and mechanistic basis for anaerobic ergothioneine

independent reaction.11 The sulfoxide synthase EgtB from Mycobacterium thermoresistibile catalyzes oxygen-dependent sulfurization of TMH.12 This second.

Structural and Mechanistic Basis for Anaerobic Ergothioneine

Apr 3, 2019 - The central and C-terminal domains form a dimer with pseudo-C2 symmetry (Figure 2C). The active site, as identified by the location of a ...

Mechanistic Basis for Ribosomal Peptide ... - ACS Publications

Feb 8, 2019 - act as a general base surrogate, or at an elevated pH to ensure deprotonation of the Cys thiol to the more .... Satish K. Nair: 0000-0003-1790-1334 ... by funding from the National Institutes of Health (GM097142 to D.A.M., and ...

Structural and mechanistic basis for anaerobic ergothioneine

5 days ago - ... Catalyzed by NosN, a Class C Radical S-Adenosylmethionine Methylase Involved in the Biosynthesis of the Nosiheptide Side-Ring System.

Retraction of Mechanistic Basis for Epstein–Barr Virus Ribonucleotide

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