Results 61 to 70 of about 1,927,178 (242)

Animal Experimentation Ethics Committee A

open access: yes, 2016
This record was harvested from a previous catalogue system and will be withdrawn in 2025. Information in this record may be superseded or incomplete.
University of Melbourne. Animal Experimentation Ethics Committee
core  

Structural and biochemical analysis of a B12 superbinder

open access: yesFEBS Letters, EarlyView.
BtuG proteins are vitamin B12 scavengers in Bacteroides thetaiotaomicron, a dominant human gut bacterium. We present crystal structures of three BtuG homologs bound to cobalamin and its precursor cobinamide, revealing picomolar binding affinities, among the highest known for any natural protein.
Jose M. Martinez Felices   +3 more
wiley   +1 more source

Animal experimentation-Part II: In periodontal research

open access: yesJournal of International Clinical Dental Research Organization, 2015
Animals contribute to the development of medical and dental sciences by being sacrificed in the hands of scientists. The experimental design demands a specific type of animal to be used for experimentation.
T K Pal
doaj   +1 more source

UNIVERSITY OFMELBOURNE ANIMAL EXPERIMENTATION ETHICS COMMITTEE WORKING PARTY ON ANIMAL FACILITES

open access: yes, 1991
This record was harvested from a previous catalogue system and will be withdrawn in 2025. Information in this record may be superseded or incomplete.
University of Melbourne. Animal Experimentation Ethics Committee
core  

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

MINUTE BOOKS OF THE ANIMAL EXPERIMENTATION COMMITTEE / ANIMAL EXPERIMENTATION ETHICS COMMITTEE

open access: yes, 1991
This record was harvested from a previous catalogue system and will be withdrawn in 2025. Information in this record may be superseded or incomplete. Visit this record in UMA's new catalogue at: https://archives.library.unimelb.edu.au/nodes/view/71226The
University of Melbourne. Animal Experimentation Ethics Committee
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

Improving the transparency of animal experiments: valuable lessons learned from a systematic analysis of registration protocols

open access: yesBMC Veterinary Research
Purpose To comprehensively analyze the epidemiological characteristics of research protocols on international animal experiment registration platforms, explore potential factors influencing protocol publication, and offer recommendations to improve ...
Shaowei Yi   +12 more
doaj   +1 more source

Animal experimentation

open access: yes, 2007
Why consider opposing viewpoints? -- Introduction -- Ch. 1: Do animals have rights? -- Chapter preface -- 1. Animals have rights / Tom Regan -- 2. Animals do not have rights / Ilana Mercer -- 3.
Henig, Robin, M.
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

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