Results 131 to 140 of about 9,490,238 (346)
Annual Report - Marine Biological Laboratory, 1942
Annual report of the Marine Biological Laboratory in Woods Hole. 1942.
Marine Biological Laboratory (Woods Hole MA)
core
Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav +2 more
wiley +1 more source
Chestnut is a valuable species that grows widely throughout the Italian peninsula. It is susceptible to different diseases and among them chestnut blight caused by Cryphonectria parasitica is the most devastating one.
Stefania Mirela Mang +7 more
doaj +1 more source
Discovery of Guanfacine as a Novel TAAR1 Agonist: A Combination Strategy through Molecular Modeling Studies and Biological Assays. [PDF]
Cichero E +10 more
europepmc +1 more source
Annual Report - Marine Biological Laboratory, 1894
Annual report of the Marine Biological Laboratory in Woods Hole. 1894.
Marine Biological Laboratory (Woods Hole MA)
core
How do genomes gain new functional parts? In eukaryotes, which tend to evolve under weak selection, much of the genome is junk. Palazzo and Qiu borrow the logic of Markov chains to show how non‐functional DNA becomes functional through the appearance of intermediate states, which arise due to epistasis, buffering, and biochemical messiness, allowing ...
Alexander F. Palazzo, Yi Qiu
wiley +1 more source
Evaluation of a serological reference panel for Lassa virus
E. Bentley +8 more
doaj +1 more source
Curcumin-loaded mesoporous silica nanoparticles for drug delivery: synthesis, biological assays and therapeutic potential - a review. [PDF]
Iranshahy M +8 more
europepmc +1 more source
Annual Report - Marine Biological Laboratory, 1934
Annual report of the Marine Biological Laboratory in Woods Hole. 1934.
Marine Biological Laboratory (Woods Hole MA)
core
The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge +6 more
wiley +1 more source

