Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Wade Borcherds"'
Publikováno v:
bioRxiv
Prion-like low-complexity domains (PLCDs) are involved in the formation and regulation of distinct biomolecular condensates that form via coupled associative and segregative phase transitions. We previously deciphered how evolutionarily conserved seq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daa07be7c6f919915a6df6a44244f2fa
https://doi.org/10.21203/rs.3.rs-2870258/v1
https://doi.org/10.21203/rs.3.rs-2870258/v1
Autor:
Mina Farag, Rohit V. Pappu, Ivan Peran, Tanja Mittag, Wade Borcherds, Anne Bremer, Erik W. Martin
Publikováno v:
Nature Chemistry. 14:196-207
Prion-like low-complexity domains (PLCDs) have distinctive sequence grammars that determine their driving forces for phase separation. Here we uncover the physicochemical underpinnings of how evolutionarily conserved compositional biases influence th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8a35292e111892370ca76d976c868d1
https://doi.org/10.1038/s41557-021-00840-w
https://doi.org/10.1038/s41557-021-00840-w
Autor:
Oluwakemi T. Sowemimo, Patrick Knox-Brown, Wade Borcherds, Tobias Rindfleisch, Anja Thalhammer, Gary W. Daughdrill
Publikováno v:
Biomolecules, Vol 9, Iss 3, p 84 (2019)
Cold-regulated (COR) 15A is an intrinsically disordered protein (IDP) from Arabidopsis thaliana important for freezing tolerance. During freezing-induced cellular dehydration, COR15A transitions from a disordered to mostly α-helical structure. We te
Externí odkaz:
https://doaj.org/article/56eccdf83e0d4e2e818786dcd1feadce
Publikováno v:
Biomolecules, Vol 9, Iss 3, p 83 (2019)
The disordered p53 transactivation domain (p53TAD) contains specific levels of transient helical secondary structure that are necessary for its binding to the negative regulators, mouse double minute 2 (Mdm2) and MdmX. The interactions of p53 with Md
Externí odkaz:
https://doaj.org/article/5147ba3f4eed4838bbae5c577139c52e
Autor:
Wade Borcherds, Qi Li, Sami Abdulkadir, Leixiang Yang, Jianfeng Cai, Gary W. Daughdrill, Yan Shi, Jiandong Chen, Lihong Chen, Junhao Lu, Peng Sang
Publikováno v:
Journal of Medicinal Chemistry
The use of peptidomimetic scaffolds is a promising strategy for the inhibition of protein–protein interactions (PPIs). Herein, we demonstrate that sulfono-γ-AApeptides can be rationally designed to mimic the p53 α-helix and inhibit p53–MDM2 PPI
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7d38a37838d7870022df38fcc3adcfd
https://doi.org/10.1021/acs.jmedchem.9b00993
https://doi.org/10.1021/acs.jmedchem.9b00993
Autor:
Malissa Fenton, Wade Borcherds, Lihong Chen, Asokan Anbanandam, Jiandong Chen, Gary Daughdrill
Publikováno v:
SSRN Electronic Journal.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b15c9854a39f25a9d616c630cffe2d4b
https://doi.org/10.2139/ssrn.4107498
https://doi.org/10.2139/ssrn.4107498
Autor:
Malissa Fenton, Wade Borcherds, Lihong Chen, Asokan Anbanandam, Robin Levy, Jiandong Chen, Gary Daughdrill
Publikováno v:
Journal of Molecular Biology. 434:167844
Autoinhibition of p53 binding to MDMX requires two short-linear motifs (SLiMs) containing adjacent tryptophan (WW) and tryptophan-phenylalanine (WF) residues. NMR spectroscopy was used to show the WW and WF motifs directly compete for the p53 binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d90904a4edd1602feff2b4c1725fcc9c
https://doi.org/10.1016/j.jmb.2022.167844
https://doi.org/10.1016/j.jmb.2022.167844
Autor:
Tanjing Song, Fan He, Wade Borcherds, Lihong Chen, Xi Wei, Jiandong Chen, Gary W. Daughdrill, Mousumi Das
Publikováno v:
Proceedings of the National Academy of Sciences. 116:8859-8868
The p53 tumor suppressor is a sequence-specific DNA binding protein that activates gene transcription to regulate cell survival and proliferation. Dynamic control of p53 degradation and DNA binding in response to stress signals are critical for tumor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fda4e96a587490237a5cc7dad07232b
https://doi.org/10.1073/pnas.1903077116
https://doi.org/10.1073/pnas.1903077116
Autor:
Gary W. Daughdrill, Wade Borcherds, Alex S. Holehouse, Ignacio E. Sánchez, Clara Blanes-Mira, Alejandro Estaña, Susana Barrera-Vilarmau, Amin Sagar, Gregorio Fernández-Ballester, Juan Cortés, Pau Bernadó, Rohit V. Pappu, Amélie Barozet, Juliana Glavina, Gonzalo de Prat-Gay, Lucía B. Chemes, Nicolas S. Gonzalez-Foutel
Many disordered proteins conserve essential functions in the face of extensive sequence variation. This makes it challenging to identify the forces responsible for functional selection. Viruses are robust model systems to investigate functional selec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74353c0c8cc7af904aedc731bc0f6b34
https://doi.org/10.1101/2021.05.14.444182
https://doi.org/10.1101/2021.05.14.444182
Publikováno v:
Curr Opin Struct Biol
Liquid-liquid phase separation is the mechanism underlying the formation of biomolecular condensates. Disordered protein regions often drive phase separation, but molecular interactions of disordered protein regions are not well understood, sometimes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3f9666f590f53e20e28530c2cb88641
http://arxiv.org/abs/2008.02917
http://arxiv.org/abs/2008.02917