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Redox partner exchanges between spatially confined complexes control the coupling effect of cytochrome b<sub>5</sub> on P450 CYP3A4. [PDF]
Urban P, Perret A, Pompon D.
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Structural basis for no retinal binding in flotillin-associated rhodopsins
Kovalev K+10 more
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Cofactor squelching: Artifact or fact?
BioEssays, 2016Cofactor squelching is the term used to describe competition between transcription factors (TFs) for a limited amount of cofactors in a cell with the functional consequence that TFs in a given cell interfere with the activity of each other. Since cofactor squelching was proposed based primarily on reporter assays some 30 years ago, it has remained ...
Søren Fisker Schmidt+2 more
exaly +6 more sources
Towards complete cofactor arrangement in the 3.0 Å resolution structure of photosystem II
Nature, 2005Bernhard Loll, Jan Kern, Athina Zouni
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Round, round we go - strategies for enzymatic cofactor regeneration.
Natural product reports (Print), 2020Covering: up to the beginning of 2020Enzymes depending on cofactors are essential in many biosynthetic pathways of natural products. They are often involved in key steps: catalytic conversions that are difficult to achieve purely with synthetic organic ...
Silja Mordhorst, J. Andexer
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A mystery of bacterial chromosome segregation is explained by a nucleotide ...
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Advanced Functional Materials, 2019
Over the past decade, the catalytic activity of nanozymes has been greatly enhanced, but their selectivity is still low and considered a critical issue to overcome. Herein, Fe–N4 single site embedded graphene (Fe–N‐rGO), which resembles the heme cofactor
M. Kim+9 more
semanticscholar +1 more source
Over the past decade, the catalytic activity of nanozymes has been greatly enhanced, but their selectivity is still low and considered a critical issue to overcome. Herein, Fe–N4 single site embedded graphene (Fe–N‐rGO), which resembles the heme cofactor
M. Kim+9 more
semanticscholar +1 more source