SALL4 mediates teratogenicity as a thalidomide-dependent cereblon substrate

Autor: Mariko Riley, Katie Stamp, Xinde Zheng, Yan Ren, Kate Blease, Chin-Chun Lu, Julia Hui, Lawrence G Hamann, Philip P Chamberlain, Gang Lu, Polat Abdubek, Mary E Matyskiela, Gondi Kumar, Maria Wang, Wei Fang, Aaron Carpenter, Thomas Clayton, Clifton Drew, Suzana Couto, Chung-Wein Lee, Mark Rolfe, Rupert Vessey, James Hartke

Publikováno v: Nature Chemical Biology. 14:981-987

Targeted protein degradation via small-molecule modulation of cereblon offers vast potential for the development of new therapeutics. Cereblon-binding therapeutics carry the safety risks of thalidomide, which caused an epidemic of severe birth defect

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29f5299ace6c6c8aa0af7dbee0692fbc
https://doi.org/10.1038/s41589-018-0129-x

Crystal structure of a putative PII-like signaling protein (TM0021) from Thermotoga maritima at 2.5 A resolution

Autor: Jeff Velasquez, Mike DiDonato, Kevin Quijano, Xianhong Wang, Scott A. Lesley, Henry van den Bedem, Qingping Xu, Marc-André Elsliger, Polat Abdubek, Eric Hampton, Jie Ouyang, Timothy M. McPhillips, Xiaoping Dai, Jaume M. Canaves, Said Eshagi, Bill West, Guenter Wolf, Frank von Delft, Carina Grittini, Alyssa Robb, Lukasz Jaroszewski, Keith O. Hodgson, John Wooley, Andrew T. Morse, Mitchell D. Miller, Daniel McMullan, Inna Levin, Juli Vincent, H.-J. Chiu, Cathy Karlak, Robert Schwarzenbacher, Kin Moy, Slawomir K. Grzechnik, John S. Kovarik, Jamison Cambell, Eric Koesema, Peter Kuhn, Adam Godzik, Raymond C. Stevens, Tanja Biorac, Ross Floyd, Heath E. Klock, Linda S. Brinen, Andreas Kreusch, Rebecca Page, Glen Spraggon, Ashley M. Deacon, Ian A. Wilson, Eileen Ambing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80e22936274d8bbbd318faa4a48d40a6
https://doi.org/10.1002/prot.10647

Crystal structure of an Udp-n-acetylmuramate-alanine ligase MurC (TM0231) from Thermotoga maritima at 2.3 A resolution

Autor: Guenter Wolf, Peter Kuhn, Daniel McMullan, Inna Levin, Ross Floyd, Hsiu-Ju Chiu, Carina Grittini, John S. Kovarik, Ian A. Wilson, Eric Hampton, Kin Moy, Eileen Ambing, Glen Spraggon, Alyssa Robb, Jaume M. Canaves, Heath E. Klock, Kevin Quijano, John Wooley, Marc-André Elsliger, Andrew T. Morse, Timothy M. McPhillips, Bill West, Juli Vincent, Christian C. Lee, Polat Abdubek, Jie Ouyang, Frank von Delft, Xiaoping Dai, Jeff Velasquez, Linda S. Brinen, Slawomir K. Grzechnik, Tanya Biorac, Adam Godzik, Raymond C. Stevens, Jamison Cambell, Eric Koesema, Ashley M. Deacon, Andreas Kreusch, Rebecca Page, Xianhong Wang, Scott A. Lesley, Robert Schwarzenbacher, Mike DiDonato, Cathy Karlak, Henry van den Bedem, Qingping Xu, Keith O. Hodgson, Lukasz Jaroszewski, Said Eshagi, Mitchell D. Miller

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9f24e0c0055b4b6d898166918c69182
https://ora.ox.ac.uk/objects/uuid:1c251061-5885-44de-9629-1fd6bad0e6ff

Structure of BT_3984, a member of the SusD/RagB family of nutrient-binding molecules

Autor: Mark W. Knuth, Linda Okach, Keith O. Hodgson, Winnie W Lam, Tamara Astakhova, Debanu Das, Lukasz Jaroszewski, Kevin K. Jin, Abhinav Kumar, Scott A. Lesley, Joanna C Grant, Daniel McMullan, Gye Won Han, Herbert L. Axelrod, Amanda Nopakun, Kyle Ellrott, John Wooley, Piotr Kozbial, Henry J Tien, Polat Abdubek, Christine B Trame, Ashley M. Deacon, Sanjay Krishna, Christopher L. Rife, Henry van den Bedem, Ron Reyes, Lian Duan, Dana Weekes, Adam Godzik, Heath E. Klock, Marc André Elsliger, Carol L. Farr, David Marciano, Ian A. Wilson, Julie Feuerhelm, Christina Puckett, Edward Nigoghossian, Marc C. Deller, Qingping Xu, Constantina Bakolitsa, Connie Chen, Dennis Carlton, Hsiu-Ju Chiu, Mitchell D. Miller, Anna Grzechnik, Thomas Clayton, Andrew T. Morse

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta Crystallographica Section F: Structural Biology and Crystallization Communications

The crystal structure of BT_3984, a SusD-family protein, reveals a TPR N-terminal region providing support for a loop-rich C-terminal subdomain and suggests possible interfaces involved in sus complex formation.
The crystal structure of the Bact

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::651fbda37dbad2454e03450209b718f0
https://doi.org/10.1107/s1744309110032999

Structures of three members of Pfam PF02663 (FmdE) implicated in microbial methanogenesis reveal a conserved α+β core domain and an auxiliary C-terminal treble-clef zinc finger

Autor: Lukasz Jaroszewski, Polat Abdubek, Sanjay Krishna, Adam Godzik, Henry van den Bedem, Dennis Carlton, Marc-André Elsliger, Natasha Sefcovic, Edward Nigoghossian, Piotr Kozbial, Henry J Tien, Thomas Clayton, Debanu Das, Qingping Xu, Joanna C Grant, Gye Won Han, Heath E. Klock, Carol L. Farr, Ron Reyes, Daniel McMullan, John Wooley, Hsiu-Ju Chiu, Marc C. Deller, Herbert L. Axelrod, Connie Chen, Amanda Nopakun, Tamara Astakhova, Ian A. Wilson, Kevin K. Jin, Christine B Trame, Christina Puckett, Constantina Bakolitsa, David Marciano, Keith O. Hodgson, Winnie W Lam, Ashley M. Deacon, Andrew T. Morse, Mitchell D. Miller, Anna Grzechnik, Julie Feuerhelm, Abhinav Kumar, Tiffany Wooten, Dana Weekes, Lian Duan, Linda Okach, Mark W. Knuth, Scott A. Lesley, Kyle Ellrott

Publikováno v: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10

The first structures from the FmdE Pfam family (PF02663) reveal that some members of this family form tightly intertwined dimers consisting of two domains (N-terminal α+β core and C-terminal zinc-finger domains), whereas others contain only the cor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07744ab9a1701e66d2df720abda9b926
http://europepmc.org/articles/PMC2954224