Results 131 to 140 of about 26,374,058 (266)

Structures of mycobacterial 3‐methylcrotonyl‐CoA carboxylase reveal carrier‐domain translocation between catalytic sites

FEBS Letters, EarlyView.
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, Bogdan I. Florea, Sebastian Geibel   +2 more
wiley   +1 more source

Innovative humanitarian finance: examining the promises and realities of impact bonds in humanitarian and refugee response. [PDF]

Disasters
Zulkaphil L.
europepmc   +1 more source

From junk to function — How weak selection in eukaryotes builds new parts and drives genomic complexity

FEBS Letters, EarlyView.
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

Discussing Future Treatment and Care in the ICU: Perspectives From Patients. [PDF]

Acta Anaesthesiol Scand
Smith MA, Zwisler AD, Nissen A, Michelsen J, Olsen HT, Wichmann S, Hansen PM, Walther LH, Le Greves S, Westergaard B, Jensen HI, Nystrup KB.   +11 more
europepmc   +1 more source

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

FEBS 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, Vivian Pogenberg, Alexander Baumgart, Bente Siebels, Hartmut Schlüter, Michael Hecht‐Bucher, Aymelt Itzen   +6 more
wiley   +1 more source

New Tocopherol Dimers. [PDF]

Acta Chemica Scandinavica, 1968
J. Lars G. Nilsson, G. Doyle Daves, Jr., Karl Folkers, Salo Gronowitz, Harald Christiansen, Ulf Rosén   +5 more
openaire   +2 more sources

Prospecting the protein design landscape

FEBS 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, Katharina T. Stonig, Jens Meiler, Clara T. Schoeder, Monica L. Fernández‐Quintero   +4 more
wiley   +1 more source

TIMS Techniques for Measuring Strontium Isotope Ratios in Apatite Grains and Application to Igneous Rock Petrology. [PDF]

Rapid Commun Mass Spectrom
Neto C, de Morisson Valeriano C, Paravidini G, Bruno H, Carvalho M, Almeida R, Peixoto C, Bersan S, Carvalho M, Heilbron M.   +9 more
europepmc   +1 more source

Labdarības loma psihiatriskās aprūpes tapšanā Latvijā: Aleksandra Augstumiem – 180

Acta Medico-Historica Rigensia, 2005
Kuzņecovs, Vladimirs
doaj   +1 more source

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

FEBS 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, Jeffrey A. Hawkes, Cecilia Blikstad, Pia Lindberg   +3 more
wiley   +1 more source