Zobrazeno 1 - 10
of 187
pro vyhledávání: '"Thomas Szyperski"'
Autor:
Carlos Alvarado, Erik Stahl, Karissa Koessel, Andrew Rivera, Brian R. Cherry, Surya V.S.R.K. Pulavarti, Thomas Szyperski, William Cance, Timothy Marlowe
Publikováno v:
Molecules, Vol 24, Iss 18, p 3352 (2019)
The Focal Adhesion Targeting (FAT) domain of Focal Adhesion Kinase (FAK) is a promising drug target since FAK is overexpressed in many malignancies and promotes cancer cell metastasis. The FAT domain serves as a scaffolding protein, and its interacti
Externí odkaz:
https://doaj.org/article/300dbdafadb04c4f8d2a207909d511c0
Publikováno v:
PLoS ONE, Vol 9, Iss 5, p e96521 (2014)
A high-quality NMR solution structure is presented for protein hMcl-1(171-327) which comprises residues 171-327 of the human anti-apoptotic protein Mcl-1 (hMcl-1). Since this construct contains the three Bcl-2 homology (BH) sequence motifs which part
Externí odkaz:
https://doaj.org/article/2a723afad5f94aeaa20f834a25dddf2a
Autor:
Alexander Eletsky, Karolina Michalska, Scott Houliston, Qi Zhang, Michael D Daily, Xiaohui Xu, Hong Cui, Adelinda Yee, Alexander Lemak, Bin Wu, Maite Garcia, Meagan C Burnet, Kristen M Meyer, Uma K Aryal, Octavio Sanchez, Charles Ansong, Rong Xiao, Thomas B Acton, Joshua N Adkins, Gaetano T Montelione, Andrzej Joachimiak, Cheryl H Arrowsmith, Alexei Savchenko, Thomas Szyperski, John R Cort
Publikováno v:
PLoS ONE, Vol 9, Iss 7, p e101787 (2014)
Bacterial species in the Enterobacteriaceae typically contain multiple paralogues of a small domain of unknown function (DUF1471) from a family of conserved proteins also known as YhcN or BhsA/McbA. Proteins containing DUF1471 may have a single or th
Externí odkaz:
https://doaj.org/article/86d6bee1feac4e90bbb12b0e86a9a3f7
Autor:
Yibing Wu, Marco Punta, Rong Xiao, Thomas B Acton, Bharathwaj Sathyamoorthy, Fabian Dey, Markus Fischer, Arne Skerra, Burkhard Rost, Gaetano T Montelione, Thomas Szyperski
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e37404 (2012)
The soluble monomeric domain of lipoprotein YxeF from the Gram positive bacterium B. subtilis was selected by the Northeast Structural Genomics Consortium (NESG) as a target of a biomedical theme project focusing on the structure determination of the
Externí odkaz:
https://doaj.org/article/75854a80aed04bf4a7b9adb71cf253d4
Autor:
Sharon L. Guffy, Surya V. S. R. K. Pulavarti, Joseph Harrison, Drew Fleming, Thomas Szyperski, Brian Kuhlman
Publikováno v:
Biochemistry. 62:770-781
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7365b234cd94ac8109763d6c44791ecf
https://doi.org/10.1021/acs.biochem.2c00595
https://doi.org/10.1021/acs.biochem.2c00595
Autor:
Thomas Szyperski
Publikováno v:
The journal of physical chemistry. A. 126(45)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da549bf98dbfeeaf5f95f5c07bb75af9
https://pubmed.ncbi.nlm.nih.gov/36326642
https://pubmed.ncbi.nlm.nih.gov/36326642
Autor:
Yaohui Li, Rongzhen Zhang, Chi Wang, Farhad Forouhar, Oliver B Clarke, Sergey Vorobiev, Shikha Singh, Gaetano T Montelione, Thomas Szyperski, Yan Xu, John F Hunt
Publikováno v:
The EMBO Journal. 41
The evolutionary benefit accounting for widespread conservation of oligomeric structures in proteins lacking evidence of intersubunit cooperativity remains unclear. Here, crystal and cryo-EM structures, and enzymological data, demonstrate that a cons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f5a269fa81a57b8afd93d3b8c14835e
https://doi.org/10.15252/embj.2021108368
https://doi.org/10.15252/embj.2021108368
Autor:
David F Thieker, Eric Klavins, Surya V.S.R.K. Pulavarti, Frank DiMaio, Jermel R. Griffin, David Baker, Matthew Cummins, Thomas Szyperski, Hugh K. Haddox, Devin Strickland, Brian Coventry, Brian Kuhlman, Samer Halabiya, Jack Maguire
Publikováno v:
Proteins
The FastDesign protocol in the molecular modeling program Rosetta iterates between sequence optimization and structure refinement to stabilize de novo designed protein structures and complexes. FastDesign has been used previously to design novel prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bedef066eb9c0f2c18fe7ae7ad81da0f
https://doi.org/10.1002/prot.26030
https://doi.org/10.1002/prot.26030
Autor:
Surya V. S. R. K. Pulavarti, Jack B. Maguire, Shirley Yuen, Joseph S. Harrison, Jermel Griffin, Lakshmanane Premkumar, Edward A. Esposito, George I. Makhatadze, Angel E. Garcia, Thomas M. Weiss, Edward H. Snell, Brian Kuhlman, Thomas Szyperski
Publikováno v:
The journal of physical chemistry. B. 126(6)
Understanding protein folding is crucial for protein sciences. The conformational spaces and energy landscapes of cold (unfolded) protein states, as well as the associated transitions, are hardly explored. Furthermore, it is not known how structure r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45cc676019c22a97458f9aba199032ba
https://pubmed.ncbi.nlm.nih.gov/35128921
https://pubmed.ncbi.nlm.nih.gov/35128921
Autor:
Ruikai Cao, Robert Rossdeutcher, Yi Shen, Daniel Miller, Yulong Zhong, Laura Sánchez B., Karishma Ramcharan, Xiangxiang Wu, Eva Zurek, Thomas Szyperski, Zhifeng Shao, Bing Gong
The precise spatial positioning of functional groups in biomacromolecules leads to astonishing binding, catalytic, and transport capabilities. In contrast, synthetic frameworks capable of convergently locking functional groups with minimized conforma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3a5ab60248820eabf78019283cf0cdfc
https://doi.org/10.21203/rs.3.rs-1264431/v1
https://doi.org/10.21203/rs.3.rs-1264431/v1
