Carboxymethyl starch as a reducing and capping agent in the hydrothermal synthesis of selenium nanostructures for use with three-dimensional-printed hydrogel carriers

Autor: Vishakha Vishakha, A. M. Abdel-Mohsen, Jan Michalicka, Paul B. White, Petr Lepcio, Lizeth Katherine Tinoco Navarro, Josef Jančář

Publikováno v: Royal Society Open Science, Vol 10, Iss 10 (2023)

The hydrothermal method is a cost-effective and eco-friendly route for preparing various nanomaterials. It can use a capping agent, such as a polysaccharide, to govern and define the nanoparticle morphology. Elemental selenium nanostructures (spheres

Externí odkaz: https://doaj.org/article/b50913d78366410195ae6926e83e314a

Paramagnetic relaxation enhancement NMR as a tool to probe guest binding and exchange in metallohosts

Autor: Anne Swartjes, Paul B. White, Jeroen P. J. Bruekers, Johannes A. A. W. Elemans, Roeland J. M. Nolte

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-8 (2022)

Paramagnetic metallohost systems are difficult to characterize. Here the authors report that the paramagnetic relaxation enhancement effect can be used to prove by nuclear magnetic resonance experiments that Mn(III) porphyrin cage compounds can bind

Externí odkaz: https://doaj.org/article/2f1f56e026464d5f843a00faeea91453

Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases

Autor: Abbas H. K. Al Temimi, Jona Merx, Christian J. van Noortwijk, Giordano Proietti, Romano Buijs, Paul B. White, Floris P. J. T. Rutjes, Thomas J. Boltje, Jasmin Mecinović

Publikováno v: Scientific Reports, Vol 10, Iss 1, Pp 1-12 (2020)

Abstract Histone lysine methyltransferases (KMTs) play an important role in epigenetic gene regulation and have emerged as promising targets for drug discovery. However, the scope and limitation of KMT catalysis on substrates possessing substituted l

Externí odkaz: https://doaj.org/article/d597a3d415a940e1a621ac071eda0bb4

Amide-derived lysine analogues as substrates and inhibitors of histone lysine methyltransferases and acetyltransferases

Autor: Jasmin Mecinović, Thomas J. Boltje, Paul B. White, Sabine G H A Langens, Jordi C. J. Hintzen, Jona Merx, Marijn N. Maas

Publikováno v: Organic & Biomolecular Chemistry, 20, pp. 173-181
Organic & Biomolecular Chemistry, 20, 173-181
Hintzen, J C J, Merx, J, Maas, M N, Langens, S G H A, White, P B, Boltje, T J & Mecinović, J 2022, ' Amide-derived lysine analogues as substrates and inhibitors of histone lysine methyltransferases and acetyltransferases ', Organic & Biomolecular Chemistry, vol. 20, no. 1, pp. 173-181 . https://doi.org/10.1039/D1OB02191E

Histone lysine methyltransferases and acetyltransferases are two classes of epigenetic enzymes that play pivotal roles in human gene regulation. Although they both recognise and posttranslationally modify lysine residues in histone proteins, their di

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87241cab85a70f6f85b3dc91d045d05b
https://doi.org/10.1039/d1ob02191e

Mechanism of biomolecular recognition of trimethyllysine by the fluorinated aromatic cage of KDM5A PHD3 finger

Autor: Thijs Beuming, F. Matthias Bickelhaupt, Maud H. M. Wuts, Ger J. M. Pruijn, Jos J. A. G. Kamps, Jasmin Mecinović, Bas J. G. E. Pieters, Jordi Poater, Woody Sherman, Robert S. Paton, Kiran Kumar, Paul B. White

Publikováno v: Pieters, B J G E, Wuts, M H M, Poater, J, Kumar, K, White, P B, Kamps, J J A G, Sherman, W, Pruijn, G J M, Paton, R S, Beuming, T, Bickelhaupt, F M & Mecinović, J 2020, ' Mechanism of biomolecular recognition of trimethyllysine by the fluorinated aromatic cage of KDM5A PHD3 finger ', Communications Chemistry, vol. 3, no. 1, 69, pp. 1-12 . https://doi.org/10.1038/s42004-020-0313-2
Communications Chemistry, 3
Pieters, B J G E, Wuts, M H M, Poater, J, Kumar, K, White, P B, Kamps, J J A G, Sherman, W, Pruijn, G J M, Paton, R S, Beuming, T, Bickelhaupt, F M & Mecinović, J 2020, ' Mechanism of biomolecular recognition of trimethyllysine by the fluorinated aromatic cage of KDM5A PHD3 finger ', Communications Chemistry, vol. 3, 69 . https://doi.org/10.1038/s42004-020-0313-2
Communications Chemistry, 3(1):69, 1-12. Springer Nature
Communications Chemistry
Communications Chemistry, 3, 1
Communications Chemistry, Vol 3, Iss 1, Pp 1-12 (2020)

The understanding of biomolecular recognition of posttranslationally modified histone proteins is centrally important to the histone code hypothesis. Despite extensive binding and structural studies on the readout of histones, the molecular language

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10178b367b5719086ad0d3aa769b5e24
http://www.scopus.com/inward/record.url?scp=85085870921&partnerID=8YFLogxK