Results 221 to 230 of about 15,014,800 (402)

Open Access – What’s New in the Social Sciences?

open access: yes, 2015
Learn about some of the newest open access publications and platforms designed to support the open sharing of social science research. Join a discussion with librarian liaisons to social science and interdisciplinary departments about how Gettysburg ...
Scholarly Communications,
core  

Open for Science

open access: yes, 2021
"Open for Science" is a presentation by Dr Kevin Moerman and is aimed at informing academics about the benefits of open science and how to be an open scientist. This talk was presented as part of a symposium for the SFI research centre LERO, as well as for the PERFORM training network.
openaire   +1 more source

Modifications in FLAP's second cytosolic loop influence 5‐LOX interaction, inhibitor binding, and leukotriene formation

open access: yesFEBS Letters, EarlyView.
The enzyme 5‐lipoxygenase (5‐LOX) catalyzes the first step in the biosynthesis of leukotrienes (LTs) involved in inflammatory pathophysiology. After cellular stimulation, 5‐LOX translocates to the nucleus, interacting with the 5‐LOX‐activating protein (FLAP) to form LTA4 from arachidonic acid (AA).
Erik Romp   +5 more
wiley   +1 more source

Trusted CI Experiences in Cybersecurity and Service to Open Science

open access: yes, 2019
This article describes experiences and lessons learned from the Trusted CI project, funded by the US National Science Foundation to serve the community as the NSF Cybersecurity Center of Excellence.
Adams, Andrew   +18 more
core   +1 more source

Brucella NyxA and NyxB dimerization enhances effector function during infection

open access: yesFEBS Letters, EarlyView.
Brucella abortus thrives inside cells thanks to the translocation of effector proteins that fine‐tune cellular functions. NyxA and NyxB are two effectors that destabilize the nucleolar localization of their host target, SENP3. We show that the Nyx proteins directly interact with each other and that their dimerization is essential for their function ...
Lison Cancade‐Veyre   +4 more
wiley   +1 more source

The carboxylate “gripper” of the substrate is critical for C‐4 stereo‐inversion by UDP‐glucuronic acid 4‐epimerase

open access: yesFEBS Letters, EarlyView.
UDP‐glucuronic acid 4‐epimerase (UGAepi) catalyzes NAD+‐dependent interconversion of UDP‐glucuronic acid (UDP‐GlcA) and UDP‐galacturonic acid (UDP‐GalA) via C4‐oxidation, 4‐keto‐intermediate rotation, and C4‐reduction. Here, Borg et al. examined the role of the substrate's carboxylate group in the enzymic mechanism by analyzing NADH‐dependent reduction
Annika J. E. Borg   +2 more
wiley   +1 more source

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