Structures of human DPP7 reveal the molecular basis of specific inhibition and the architectural diversity of proline-specific peptidases.

Autor: Gustavo Arruda Bezerra, Elena Dobrovetsky, Aiping Dong, Almagul Seitova, Lissete Crombett, Lisa M Shewchuk, Annie M Hassell, Sharon M Sweitzer, Thomas D Sweitzer, Patrick J McDevitt, Kyung O Johanson, Karen M Kennedy-Wilson, Doug Cossar, Alexey Bochkarev, Karl Gruber, Sirano Dhe-Paganon

Publikováno v: PLoS ONE, Vol 7, Iss 8, p e43019 (2012)

Proline-specific dipeptidyl peptidases (DPPs) are emerging targets for drug development. DPP4 inhibitors are approved in many countries, and other dipeptidyl peptidases are often referred to as DPP4 activity- and/or structure-homologues (DASH). Membe

Externí odkaz: https://doaj.org/article/9376f8c95b9b47d38a60f33aab898172

Identification and characterization of the first fragment hits for SETDB1 Tudor domain

Autor: Steven Kennedy, Sean K. Liew, Matthieu Schapira, Masoud Vedadi, Abdellah Allali-Hassani, Cheryl H. Arrowsmith, Scott Houliston, Andrei K. Yudin, Jinrong Min, Diego B. Diaz, P. Mader, Hong Wu, Aman Iqbal, Aiping Dong, Vijayaratnam Santhakumar, Rodrigo Mendoza-Sanchez, Renato Ferreira de Freitas, Victoria B. Corless, David Smil, Peter Brown, Ludmila Dombrovski, Elena Dobrovetsky, Carlo C. dela Seña

Publikováno v: Bioorganicmedicinal chemistry. 27(17)

SET domain bifurcated protein 1 (SETDB1) is a human histone-lysine methyltransferase, which is amplified in human cancers and was shown to be crucial in the growth of non-small and small cell lung carcinoma. In addition to its catalytic domain, SETDB

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::279b1b546c4df6dc0f23953355372074
https://pubmed.ncbi.nlm.nih.gov/31327677

An Allosteric Inhibitor of Protein Arginine Methyltransferase 3

Autor: Richard Marcellus, Alena Siarheyeva, Rima Al-awar, Jian Jin, Jinrong Min, Ahmed Aman, Matthieu Schapira, Taraneh Hajian, Hong Wu, Guillermo Senisterra, Gregory A. Wasney, Peter Loppnau, Ilia Korboukh, Peter Brown, Elena Dobrovetsky, Masoud Vedadi, Feng Liu, Carly Griffin, Hong Zeng, David Smil, Abdellah Allali-Hassani, Yuri Bolshan, Cheryl H. Arrowsmith, Irene Chau, Aiping Dong, Gennadiy Poda

Publikováno v: Structure. 20(8):1425-1435

Summary PRMT3, a protein arginine methyltransferase, has been shown to influence ribosomal biosynthesis by catalyzing the dimethylation of the 40S ribosomal protein S2. Although PRMT3 has been reported to be a cytosolic protein, it has been shown to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0b0b20a7d69bbb9c94306601b8ccd88

Streamlining the Pipeline for Generation of Recombinant Affinity Reagents by Integrating the Affinity Maturation Step

Autor: Susanne Gräslund, Chris R. Vinci, Kevin T. Gorman, Renhua Huang, Brian K. Kay, Elena Dobrovetsky

Publikováno v: International Journal of Molecular Sciences
Volume 16
Issue 10
Pages 23587-23603
International Journal of Molecular Sciences, Vol 16, Iss 10, Pp 23587-23603 (2015)

Often when generating recombinant affinity reagents to a target, one singles out an individual binder, constructs a secondary library of variants, and affinity selects a tighter or more specific binder. To enhance the throughput of this general appro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02d14f99f9ca0c32394e9fa0b62b05f0

Crystal structure of the CorA Mg2+ transporter

Autor: Elena Dobrovetsky, Rongguang Zhang, Alexey Bochkarev, Andrzej Joachimiak, Vladimir V. Lunin, Galina Khutoreskaya, Aled M. Edwards, Declan A. Doyle, Christopher M. Koth, Michael E. Maguire

Publikováno v: Nature. 440:833-837

The magnesium ion, Mg2+, is essential for myriad biochemical processes and remains the only major biological ion whose transport mechanisms remain unknown. The CorA family of magnesium transporters is the primary Mg2+ uptake system of most prokaryote

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d615fe14e4b94293335197047e294bf5
https://doi.org/10.1038/nature04642