The interplay between Bag-1, Hsp70, and Hsp90 reveals that inhibiting Hsp70 rebinding is essential for Glucocorticoid Receptor activity

Autor: Elaine Kirschke, Zygy Roe-Zurz, David A. Agard, Chari Noddings

The glucocorticoid receptor (GR), like many signaling proteins requires Hsp90 for sustained activity. Previous biochemical studies revealed that the requirement for Hsp90 is explained by its ability to reverse Hsp70-mediated inactivation of GR throug

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::456a3d87286382fe8e83de26808e6723
https://doi.org/10.1101/2020.05.03.075523

Structure of the 4-1BB/4-1BBL complex and distinct binding and functional properties of utomilumab and urelumab

Autor: Zygy Roe-Zurz, Feng Wang, Yik Andy Yeung, Shahram Salek-Ardakani, S. Michael Chin, Kevin Lindquist, Yuting Yang, Christopher R. Kimberlin, Javier Chaparro-Riggers, Colleen Brown, Sindy Liao-Chan, Nicole Schirle Oakdale, Debasish Sen, Pamela Zhang, Andrew R. Nager, Allison Xu

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Nature Communications

4-1BB (CD137, TNFRSF9) is an inducible costimulatory receptor expressed on activated T cells. Clinical trials of two agonist antibodies, utomilumab (PF-05082566) and urelumab (BMS-663513), are ongoing in multiple cancer indications, and both antibodi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6be09a904bc39c6eb1f5da1f4d79011a
https://doi.org/10.1038/s41467-018-07136-7

Crystal structure of a eukaryotic phosphate transporter

Autor: Bryant H. Chau, Massimiliano Bonomi, Hemant Kumar, Andrew B. Waight, Bjørn Panyella Pedersen, William Harries, Avner Schlessinger, Andrej Sali, Atul Kumar Johri, Zygy Roe-Zurz, Aaron J. Risenmay, Robert M. Stroud

Publikováno v: Pedersen, B P, Kumar, H, Waight, A B, Risenmay, A J, Roe-Zurz, Z, Chau, B H, Schlessinger, A, Bonomi, M, Harries, W, Sali, A, Johri, A K & Stroud, R M 2013, ' Crystal structure of a eukaryotic phosphate transporter ', Nature, vol. 496, no. 7446, pp. 533-536 . https://doi.org/10.1038/nature12042
Nature

The X-ray crystal structure of a high-affinity phosphate importer in an inward-facing, occluded state in the presence of phosphate is reported; this is the first structure of a membrane protein involved in inorganic phosphate uptake and the first cry

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d57c5f86d7a391273a619465b58f0dd0
https://pure.au.dk/portal/da/publications/crystal-structure-of-a-eukaryotic-phosphate-transporter(8591b635-61c4-4104-b08f-bb033a8af256).html

A survey of integral α-helical membrane proteins

Autor: Franklin A. Hays, Andrej Sali, Kathleen M. Giacomini, Ursula Pieper, Zygy Roe-Zurz, Min Li, Robert M. Stroud, Libusha Kelly, Narayanan Eswar, Deanna L. Kroetz

Publikováno v: Kelly, Libusha; Pieper, Ursula; Eswar, Narayanan; Hays, Franklin A.; Li, Min; Roe-Zurz, Zygy; et al.(2009). A survey of integral α-helical membrane proteins. Journal of Structural and Functional Genomics, 10(4), pp 269-280. doi: 10.1007/s10969-009-9069-8. Retrieved from: http://www.escholarship.org/uc/item/5md455gb
Journal of Structural and Functional Genomics

Membrane proteins serve as cellular gatekeepers, regulators, and sensors. Prior studies have explored the functional breadth and evolution of proteins and families of particular interest, such as the diversity of transport-associated membrane protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b95bb400673941489c23095a6e4c5eeb
http://www.escholarship.org/uc/item/5md455gb