Results 211 to 220 of about 286,710 (351)

Enzymatic degradation of biopolymers in amorphous and molten states: mechanisms and applications

open access: yesFEBS Open Bio, EarlyView.
This review explains how polymer morphology and thermal state shape enzymatic degradation pathways, comparing amorphous and molten biopolymer structures. By integrating structure–reactivity principles with insights from thermodynamics and enzyme engineering, it highlights mechanisms that enable efficient polymer breakdown.
Anđela Pustak, Aleksandra Maršavelski
wiley   +1 more source

Identification of three new ultraluminous X-ray sources in NGC 4631 and NGC 1097: Evidence for stellar-mass black holes

open access: diamond
Sinan Allak   +4 more
openalex   +1 more source

Understanding bio‐based polymers: A study of origins, properties, biodegradation and their impact on health and the environment

open access: yesFEBS Open Bio, EarlyView.
This review provides an overview of bio‐based polymer sources, their unique functional properties and their environmental impact, and addresses their role as sustainable alternatives. It discusses end‐of‐life options, including composting and anaerobic digestion for renewable energy.
Sabina Kolbl Repinc   +8 more
wiley   +1 more source

Multi‐omics and low‐input proteomics profiling reveals dynamic regulation driving pluripotency initiation in early mouse embryos

open access: yesFEBS Open Bio, EarlyView.
Mouse pre‐implantation development involves a transition from totipotency to pluripotency. Integrating transcriptomics, epigenetic profiling, low‐input proteomics and functional assays, we show that eight‐cell embryos retain residual totipotency features, whereas cytoskeletal remodeling regulated by the ubiquitin‐proteasome system drives progression ...
Wanqiong Li   +8 more
wiley   +1 more source

A young progenitor for the most common planetary systems in the Galaxy. [PDF]

open access: yesNature
Livingston JH   +41 more
europepmc   +1 more source

C2α‐carbanion‐protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2‐hydroxyacyl‐CoA lyase

open access: yesFEBS Open Bio, EarlyView.
Enzymes of the 2‐hydroxyacyl‐CoA lyase group catalyze the condensation of formyl‐CoA with aldehydes or ketones. Thus, by structural adaptation of active sites, practically any pharmaceutically and industrially important 2‐hydroxyacid could be biotechnologically synthesized. Combining crystal structure analysis, active site mutations and kinetic assays,
Michael Zahn   +4 more
wiley   +1 more source

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