Results 51 to 60 of about 850,147 (309)

The newfound relationship between extrachromosomal DNAs and excised signal circles

open access: yesFEBS Letters, EarlyView.
Extrachromosomal DNAs (ecDNAs) contribute to the progression of many human cancers. In addition, circular DNA by‐products of V(D)J recombination, excised signal circles (ESCs), have roles in cancer progression but have largely been overlooked. In this Review, we explore the roles of ecDNAs and ESCs in cancer development, and highlight why these ...
Dylan Casey, Zeqian Gao, Joan Boyes
wiley   +1 more source

Microbial (E)-4-hydroxy-3-methylbut-2-enyl pyrophosphate reductase (IspH) and its biotechnological potential: A mini review

open access: yesFrontiers in Bioengineering and Biotechnology, 2022
(E)-4-hydroxy-3-methylbut-2-enyl pyrophosphate (HMBPP) reductase (IspH) is a [4Fe-4S] cluster-containing enzyme, involved in isoprenoid biosynthesis as the final enzyme of the methylerythritol phosphate (MEP) pathway found in many bacteria and malaria ...
Shiyong Huang   +4 more
doaj   +1 more source

Boron carboxylate catalysis of homoallylboration. [PDF]

open access: yes, 2014
Boron tris(trifluoroacetate) is identified as the first effective catalyst for the homoallyl- and homocrotylboration of aldehydes by cyclopropylcarbinylboronates.
Dugas, Gabrielle J   +3 more
core  

Numerical Study of Heterogeneous Reactions in an SOFC Anode with Oxygen Addition [PDF]

open access: yes, 2007
Previous experimental studies have shown that addition of small amounts of oxygen to a hydrocarbon fuel stream can control coking in the anode, while relatively large amounts of oxygen are present in the fuel stream in single-chamber solid oxide fuel ...
Goodwin, David G., Hao, Yong
core   +2 more sources

The catalytic mechanism of galactose mutarotase [PDF]

open access: yesProtein Science, 2003
AbstractGalactose mutarotase catalyzes the first step in normal galactose metabolism by catalyzing the conversion of β‐d‐galactose to α‐d‐galactose. The structure of the enzyme from Lactococcus lactis was recently solved in this laboratory and shown to be topologically similar to domain 5 of β‐galactosidase. From this initial X‐ray analysis, four amino
James B, Thoden   +3 more
openaire   +2 more sources

Cell wall target fragment discovery using a low‐cost, minimal fragment library

open access: yesFEBS Letters, EarlyView.
LoCoFrag100 is a fragment library made up of 100 different compounds. Similarity between the fragments is minimized and 10 different fragments are mixed into a single cocktail, which is soaked to protein crystals. These crystals are analysed by X‐ray crystallography, revealing the binding modes of the bound fragment ligands.
Kaizhou Yan   +5 more
wiley   +1 more source

Metal-organic frameworks as selective or chiral oxidation catalysts [PDF]

open access: yes, 2014
Since the discovery of Metal Organic Frameworks (MOFs) in the early 1990s, the amount of new structures has grown exponentially. A MOF typically consists of inorganic nodes that are connected by organic linkers to form crystalline, highly porous ...
Leus, Karen   +2 more
core   +1 more source

The (Glg)ABCs of cyanobacteria: modelling of glycogen synthesis and functional divergence of glycogen synthases in Synechocystis sp. PCC 6803

open access: yesFEBS Letters, EarlyView.
We reconstituted Synechocystis glycogen synthesis in vitro from purified enzymes and showed that two GlgA isoenzymes produce glycogen with different architectures: GlgA1 yields denser, highly branched glycogen, whereas GlgA2 synthesizes longer, less‐branched chains.
Kenric Lee   +3 more
wiley   +1 more source

Structural biology of ferritin nanocages

open access: yesFEBS Letters, EarlyView.
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley   +1 more source

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

open access: yesFEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes   +4 more
wiley   +1 more source

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