Results 161 to 170 of about 5,256,148 (309)

The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

open access: yesFEBS Letters, EarlyView.
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

Annual Report - Marine Biological Laboratory, 1957

open access: yes, 1957
Annual report of the Marine Biological Laboratory in Woods Hole. 1957.
Marine Biological Laboratory (Woods Hole MA)
core  

Chiral separation of chloroalkanes with the chromatographic column onboard Martian rovers

open access: yesFEBS Letters, EarlyView.
Computer image of the Rosalind Franklin Rover of ESA's ExoMars mission. ExoMars is scheduled to land on planet Mars in Oxia Planum in 2029. This area represents an interesting spot to look for biosignatures. Investigations of ExoMars include measurement on molecular chirality. We show that chiral chloroalkanes, that have been identified on Mars, can be
Asma Merzougui   +4 more
wiley   +1 more source

Annual Report - Marine Biological Laboratory, 1896-1902

open access: yes, 1902
Annual report of the Marine Biological Laboratory in Woods Hole for the years 1896-1899.
Marine Biological Laboratory (Woods Hole MA)
core  

Prospecting the protein design landscape

open access: yesFEBS Letters, EarlyView.
This review outlines the current state of various protein design approaches. We discuss the current possibilities enabled by recently released tools, highlight future avenues to pursue in protein design, and underscore the crucial role of key databases and resources for successful protein design workflows.
Jakob R. Riccabona   +4 more
wiley   +1 more source

Annual Report - Marine Biological Laboratory, 1967

open access: yes, 1968
Annual report of the Marine Biological Laboratory in Woods Hole. 1967.
Marine Biological Laboratory (Woods Hole MA)
core  

L‐aspartate oxidase provides new insights into fumarate reduction in anaerobic darkness in Synechocystis sp. PCC6803

open access: yesFEBS Letters, EarlyView.
Synechocystis strains deficient in succinate dehydrogenase (SDH) secrete more succinate than the WT under dark anaerobic conditions, supporting that SDH then primarily acts as SDH, not as a fumarate reductase. L‐aspartate oxidase (Laspo) from Synechocystis is functional under anaerobic conditions, reducing fumarate to succinate.
Kateryna Kukil   +3 more
wiley   +1 more source

Annual Report - Marine Biological Laboratory, 1926

open access: yes, 1927
Annual report of the Marine Biological Laboratory in Woods Hole. 1926.
Marine Biological Laboratory (Woods Hole MA)
core  

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