Zobrazeno 1 - 10
of 240
pro vyhledávání: '"Josep Rizo"'
Autor:
Ioannis Tsagakis, Josep Rizo
Publikováno v:
FEBS Open Bio, Vol 14, Iss 1, Pp 8-12 (2024)
Josep Rizo is a Professor of Biophysics, Biochemistry and Pharmacology at the University of Texas Southwestern Medical Center, where he is Virginia Lazenby O'Hara Chair in Biochemistry. He is particularly interested in the study of the mechanisms of
Externí odkaz:
https://doaj.org/article/7150d7ae7fca4cd59f59911cca284d31
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-13 (2023)
Abstract Stimulation of autophagy could provide powerful therapies for multiple diseases, including cancer and neurodegeneration. An attractive drug target for this purpose is Bcl-2, which inhibits autophagy by binding to the Beclin 1 BH3-domain. How
Externí odkaz:
https://doaj.org/article/f2cdfe0f6d104515bde8bfd9b9a71b55
Autor:
Klaudia Jaczynska, Luis Esquivies, Richard A. Pfuetzner, Baris Alten, Kyle D. Brewer, Qiangjun Zhou, Ege T. Kavalali, Axel T. Brunger, Josep Rizo
Publikováno v:
FEBS Open Bio, Vol 13, Iss 1, Pp 26-50 (2023)
Characterizing interactions of Synaptotagmin‐1 with the SNARE complex is crucial to understand the mechanism of neurotransmitter release. X‐ray crystallography revealed how the Synaptotagmin‐1 C2B domain binds to the SNARE complex through a so
Externí odkaz:
https://doaj.org/article/4c5a346bf0504f2d810b8e365e02f59e
Publikováno v:
FEBS Open Bio, Vol 12, Iss 11, Pp 1912-1938 (2022)
The mechanism of neurotransmitter release has been extensively characterized, showing that vesicle fusion is mediated by the SNARE complex formed by syntaxin‐1, SNAP‐25 and synaptobrevin. This complex is disassembled by N‐ethylmaleimide sensiti
Externí odkaz:
https://doaj.org/article/803145b7720d4c278fadc50488a8c867
Publikováno v:
eLife, Vol 11 (2022)
Synaptic vesicles are primed into a state that is ready for fast neurotransmitter release upon Ca2+-binding to Synaptotagmin-1. This state likely includes trans-SNARE complexes between the vesicle and plasma membranes that are bound to Synaptotagmin-
Externí odkaz:
https://doaj.org/article/9c9e26cdaf4a4ffe9a419a7e10a7e504
Autor:
Chi-Wei Tien, Bin Yu, Mengjia Huang, Karolina P. Stepien, Kyoko Sugita, Xiaoyu Xie, Liping Han, Philippe P. Monnier, Mei Zhen, Josep Rizo, Shangbang Gao, Shuzo Sugita
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-18 (2020)
Opening of the UNC-64/syntaxin closed conformation by UNC-13/Munc13 to form the neuronal SNARE complex is critical for neurotransmitter release. Here the authors show that facilitating the opening of syntaxin enhances exocytosis not only in unc-13 nu
Externí odkaz:
https://doaj.org/article/96e3ef5c27104c518147da2404c45bad
Autor:
Carlos M. Roggero, Victoria Esser, Lingling Duan, Allyson M. Rice, Shihong Ma, Ganesh V. Raj, Michael K. Rosen, Zhi-Ping Liu, Josep Rizo
Publikováno v:
PLoS ONE, Vol 17, Iss 1 (2022)
The androgen receptor (AR) plays a central role in prostate cancer. Development of castration resistant prostate cancer (CRPC) requires androgen-independent activation of AR, which involves its large N-terminal domain (NTD) and entails extensive epig
Externí odkaz:
https://doaj.org/article/e7e67b262a224e239c6fb362756b46b7
Autor:
Marcial Camacho, Bradley Quade, Thorsten Trimbuch, Junjie Xu, Levent Sari, Josep Rizo, Christian Rosenmund
Publikováno v:
eLife, Vol 10 (2021)
Munc13-1 plays a central role in neurotransmitter release through its conserved C-terminal region, which includes a diacyglycerol (DAG)-binding C1 domain, a Ca2+/PIP2-binding C2B domain, a MUN domain and a C2C domain. Munc13-1 was proposed to bridge
Externí odkaz:
https://doaj.org/article/f74364d8bc6c4f60aedc50002b36330a
Publikováno v:
eLife, Vol 10 (2021)
Two proteins called Sec17 and Sec18 may have a larger role in membrane fusion than is commonly assumed in textbook models.
Externí odkaz:
https://doaj.org/article/e9ab954eb3364df68ba0d71b9f8adcd4
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-18 (2019)
Munc18-1 and Munc13-1 are key for the exquisite regulation of neurotransmitter release. Here biophysical experiments show how αSNAP inhibits liposome fusion mediated by the neuronal SNAREs and how Munc18-1 overcomes this inhibition, ensuring that re
Externí odkaz:
https://doaj.org/article/ee3eb8e8c9514aa6aec1f6119b3e36cb