A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1.

Autor: Matthew C Clifton, David M Dranow, Alison Leed, Ben Fulroth, James W Fairman, Jan Abendroth, Kateri A Atkins, Ellen Wallace, Dazhong Fan, Guoping Xu, Z J Ni, Doug Daniels, John Van Drie, Guo Wei, Alex B Burgin, Todd R Golub, Brian K Hubbard, Michael H Serrano-Wu

Publikováno v: PLoS ONE, Vol 10, Iss 4, p e0125010 (2015)

Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advan

Externí odkaz: https://doaj.org/article/1fecc03a2b9c44169e845be5165ab56e

Phenotypic Characterization of a Comprehensive Set of MAPK1/ERK2 Missense Mutants

Autor: Lisa Brenan, Aleksandr Andreev, Ofir Cohen, Sasha Pantel, Atanas Kamburov, Davide Cacchiarelli, Nicole S. Persky, Cong Zhu, Mukta Bagul, Eva M. Goetz, Alex B. Burgin, Levi A. Garraway, Gad Getz, Tarjei S. Mikkelsen, Federica Piccioni, David E. Root, Cory M. Johannessen

Publikováno v: Cell Reports, Vol 17, Iss 4, Pp 1171-1183 (2016)

Tumor-specific genomic information has the potential to guide therapeutic strategies and revolutionize patient treatment. Currently, this approach is limited by an abundance of disease-associated mutants whose biological functions and impacts on ther

Externí odkaz: https://doaj.org/article/57cdb9a4187d4248b7ec2fc37e170d43

Structural model of the dimeric Parkinson’s protein LRRK2 reveals a compact architecture involving distant interdomain contacts

Autor: Wim Versées, Zhenyu Yue, Giambattista Guaitoli, Alex B. Burgin, Christian Johannes Gloeckner, Egon Deyaert, Felix von Zweydorf, Francesco Raimondi, Fabiana Renzi, Pravin Kumar Ankush Jagtap, Arjan Kortholt, Katja Gotthardt, Adam Schaffner, Karsten Boldt, Xianting Li, Iban Ubarretxena-Belandia, Yacob Gomez-Llorente, Donald D. Lorimer, Nebojsa Janjic, Bernd K Gilsbach, Michael Sattler, Marius Ueffing

Publikováno v: 'Proceedings of the National Academy of Sciences of the USA ', vol: 113, pages: E4357-E4366 (2016)
Proceedings of the National Academy of Sciences of the United States of America, 113(30), E4357-E4366. NATL ACAD SCIENCES
Proceedings of the National Academy of Sciences of the United States of America 113(30), E4357-E4366 (2016). doi:10.1073/pnas.1523708113

Leucine-rich repeat kinase 2 (LRRK2) is a large, multidomain protein containing two catalytic domains: a Ras of complex proteins (Roc) G-domain and a kinase domain. Mutations associated with familial and sporadic Parkinson's disease (PD) have been id

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::874400366e144c61561b4b1271088eaa
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:44933

Challenging the state of the art in protein structure prediction: Highlights of experimental target structures for the 10th Critical Assessment of Techniques for Protein Structure Prediction Experiment CASP10

Autor: Donald D. Lorimer, Andriy Kryshtafovych, Hartmut Luecke, Torsten Schwede, Rhiju Das, Mark J. van Raaij, Carmela Garcia-Doval, Xiaolei Ma, Patrick M. Bales, Kornelius Zeth, Deborah Fass, Alex B. Burgin, Frank V. Cochran, Marco Biasini, Victor Seguritan, Daniel C. Nelson, Osnat Herzberg, Anca M. Segall, Chen Chen, J. Fernando Bazan, Timothy K. Craig, Forest Rohwer, John Moult

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 82:26-42

For the last two decades, CASP has assessed the state of the art in techniques for protein structure prediction and identified areas which required further development. CASP would not have been possible without the prediction targets provided by the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f2cfc91e8732a246339929403e2e99a0
https://doi.org/10.1002/prot.24489

Functional analysis of the C-terminal domains of the site-specific recombinases XerC and XerD

Autor: Ben Butler-Cole, David J. Sherratt, Henrique Ferreira, Rachel Baker, Lidia K. Arciszewska, Alex B. Burgin

The tyrosine family site-specific recombinases XerC and XerD convert dimers of the Escherichia coli chromosome and many natural plasmids to monomers. The heterotetrameric recombination complex contains two molecules of XerC and two of XerD, with each

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7def1a4ddac46d619b8d220ef40dc528
https://doi.org/10.1016/s0022-2836(03)00558-8