Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Taras Dauzhenka"'
Autor:
Tom Dixon, Derek MacPherson, Barmak Mostofian, Taras Dauzhenka, Samuel Lotz, Dwight McGee, Sharon Shechter, Utsab R. Shrestha, Rafal Wiewiora, Zachary A. McDargh, Fen Pei, Rajat Pal, João V. Ribeiro, Tanner Wilkerson, Vipin Sachdeva, Ning Gao, Shourya Jain, Samuel Sparks, Yunxing Li, Alexander Vinitsky, Xin Zhang, Asghar M. Razavi, István Kolossváry, Jason Imbriglio, Artem Evdokimov, Louise Bergeron, Wenchang Zhou, Jagat Adhikari, Benjamin Ruprecht, Alex Dickson, Huafeng Xu, Woody Sherman, Jesus A. Izaguirre
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-24 (2022)
The formation of ternary degrader-protein complexes is a key step in the targeted degradation of proteins of interest. Here, the authors explore the structure and dynamics of such complexes applying high-performance computer simulations augmented wit
Externí odkaz:
https://doaj.org/article/c2e5bdee6705479cb8aa835a2985b507
Autor:
Tom Dixon, Derek MacPherson, Barmak Mostofian, Taras Dauzhenka, Samuel Lotz, Dwight McGee, Sharon Shechter, Utsab Shrestha, Rafal Wiewiora, Zachary McDargh, Fen Pei, Rajat Pal, Joao Vieira Ribeiro, Tanner Wilkerson, Vipin Sachdeva, Ning Gao, Shourya Jain, Samuel Sparks, Yunxing Li, Alexander Vinitsky, Xin Zhang, Asghar Razavi, István Kolossváry, Jason Imbriglio, Artem Evdokimov, Louise Bergeron, Alex Dickson, Huafeng Xu, Woody Sherman, Jesus Izaguirre
Targeted protein degradation (TPD) has emerged as a powerful approach for removing (rather than inhibiting) proteins implicated in diseases. A key step in TPD is the formation of an induced proximity complex where a degrader molecule recruits an E3 l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a5e7b51e04cb88578da974b61782146b
https://doi.org/10.21203/rs.3.rs-1318882/v1
https://doi.org/10.21203/rs.3.rs-1318882/v1
Autor:
Tom Dixon, Derek MacPherson, Barmak Mostofian, Taras Dauzhenka, Samuel Lotz, Dwight McGee, Sharon Shechter, Utsab R. Shrestha, Rafal Wiewiora, Zachary A. McDargh, Fen Pei, Rajat Pal, João V. Ribeiro, Tanner Wilkerson, Vipin Sachdeva, Ning Gao, Shourya Jain, Samuel Sparks, Yunxing Li, Alexander Vinitsky, Xin Zhang, Asghar M. Razavi, István Kolossváry, Jason Imbriglio, Artem Evdokimov, Louise Bergeron, Wenchang Zhou, Jagat Adhikari, Benjamin Ruprecht, Alex Dickson, Huafeng Xu, Woody Sherman, Jesus A. Izaguirre
Targeted protein degradation (TPD) has emerged as a powerful approach in drug discovery for removing (rather than inhibiting) proteins implicated in diseases. A key step in this approach is the formation of an induced proximity complex, where a degra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aab72e51a2dd74a1d61536d796a4ff20
https://doi.org/10.1101/2021.09.26.461830
https://doi.org/10.1101/2021.09.26.461830
Publikováno v:
Proteins
Protein docking is essential for structural characterization of protein interactions. Besides providing the structure of protein complexes, modeling of proteins and their complexes is important for understanding the fundamental principles and specifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11cac114abe99364d3592abe5ce842a1
http://hdl.handle.net/10044/1/78266
http://hdl.handle.net/10044/1/78266
Publikováno v:
Journal of Computational Chemistry. 39:2012-2021
Protein-protein docking procedures typically perform the global scan of the proteins relative positions, followed by the local refinement of the putative matches. Because of the size of the search space, the global scan is usually implemented as rigi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e632b2afe024834741629d47c211a93
https://doi.org/10.1002/jcc.25381
https://doi.org/10.1002/jcc.25381
Autor:
Ivan Anishchenko, Taras Dauzhenka, Daniil Mnevets, Petras J. Kundrotas, Ilya A. Vakser, Ian Kotthoff, Matthew M. Copeland
Publikováno v:
Protein Science. 27:172-181
Characterization of life processes at the molecular level requires structural details of protein interactions. The number of experimentally determined structures of protein–protein complexes accounts only for a fraction of known protein interaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::715f15763db172a9fa415acb6fb18de6
https://doi.org/10.1002/pro.3295
https://doi.org/10.1002/pro.3295
Publikováno v:
Biophysical Journal. 118:360a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0f60a36bd53512717c4f3af0ef1c4b7a
https://doi.org/10.1016/j.bpj.2019.11.2072
https://doi.org/10.1016/j.bpj.2019.11.2072
Publikováno v:
Biophysical Journal. 118:516a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e5f1d8f81c1e6fffeb4183cbb3dc7fe0
https://doi.org/10.1016/j.bpj.2019.11.2841
https://doi.org/10.1016/j.bpj.2019.11.2841
Autor:
Ivan Anishchenko, Ilya A. Vakser, Madhurima Das, Taras Dauzhenka, Petras J. Kundrotas, Varsha D. Badal
Publikováno v:
Proteins. 86
The paper presents analysis of our template-based and free docking predictions in the joint CASP12/CAPRI37 round. A new scoring function for template-based docking was developed, benchmarked on the Dockground resource, and applied to the targets. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b411a965ccb2ae01d1666c3715d2e64c
https://pubmed.ncbi.nlm.nih.gov/28905425
https://pubmed.ncbi.nlm.nih.gov/28905425
Autor:
Varsha D. Badal, Ivan Anishchenko, Ilya A. Vakser, Madhurima Das, Taras Dauzhenka, Petras J. Kundrotas, A. V. Tuzikov
Publikováno v:
Bioinformatics Research and Applications ISBN: 9783319387819
ISBRA
ISBRA
Structural characterization of protein-protein interactions is essential for fundamental understanding of biomolecular processes and applications in biology and medicine. The number of protein interactions in a genome is significantly larger than the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea75cb13a06a8a2af75ff0adc5bc02ba
https://doi.org/10.1007/978-3-319-38782-6_8
https://doi.org/10.1007/978-3-319-38782-6_8