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Items: 1 to 20 of 76

1.
Early-onset epilepsy and microcephaly-capillary malformation syndrome caused by a novel STAMBP mutation in a Chinese boy
Fangrui Wu, Ying Dai, Juan Wang, Min Cheng, Yanqin Wang, Xiujuan Li, Ping Yuan, Shuang Liao, Li Jiang, Jin Chen, Lisi Yan, Min Zhong
Mol Med Rep. 2019 Dec; 20(6): 5145–5151. Published online 2019 Oct 17. doi: 10.3892/mmr.2019.10757
PMCID:
PMC6854595
AbstractArticlePDF–612K
2.
The deubiquitinating enzyme STAMBP is a newly discovered driver of triple-negative breast cancer progression that maintains RAI14 protein stability
Qianqian Yang, Ding Yan, Chaoying Zou, Qian Xue, Shuhui Lin, Qingtian Huang, Xiaofen Li, Daolin Tang, Xin Chen, Jinbao Liu
Exp Mol Med. 2022 Nov; 54(11): 2047–2059. Published online 2022 Nov 25. doi: 10.1038/s12276-022-00890-1
PMCID:
PMC9723177
AbstractArticlePDF–6.9M
3.
Structural and functional characterization of ubiquitin variant inhibitors for the JAMM-family deubiquitinases STAMBP and STAMBPL1
Yusong Guo, Qi Liu, Evan Mallette, Cody Caba, Feng Hou, Julia Fux, Gabriel LaPlante, Aiping Dong, Qi Zhang, Hui Zheng, Yufeng Tong, Wei Zhang
J Biol Chem. 2021 Oct; 297(4): 101107. Published online 2021 Aug 21. doi: 10.1016/j.jbc.2021.101107
PMCID:
PMC8449267
AbstractArticlePDF–2.4M
4.
Targeting the deubiquitinase STAMBP inhibits NALP7 inflammasome activity
Joseph S. Bednash, Nathaniel Weathington, James Londino, Mauricio Rojas, Dexter L. Gulick, Robert Fort, SeungHye Han, Alison C. McKelvey, Bill B. Chen, Rama K. Mallampalli
Nat Commun. 2017; 8: 15203. Published online 2017 May 11. doi: 10.1038/ncomms15203
PMCID:
PMC5437278
AbstractArticlePDF–3.7M
5.
Mutations in STAMBP, encoding a deubiquitinating enzyme, cause Microcephaly-Capillary Malformation syndrome
Laura M. McDonell, Ghayda M. Mirzaa, Diana Alcantara, Jeremy Schwartzentruber, Melissa T. Carter, Leo J. Lee, Carol L. Clericuzio, John M. Graham, Jr, Deborah J. Morris-Rosendahl, Tilman Polster, Gyula Acsadi, Sharron Townshend, Simon Williams, Anne Halbert, Bertrand Isidor, Christopher D. Smyser, Alex R. Paciorkowski, Marcia Willing, John Woulfe, Soma Das, Chandree L. Beaulieu, Janet Marcadier, FORGE Canada Consortium, Michael T. Geraghty, Brendan J. Frey, Jacek Majewski, Dennis E. Bulman, William B. Dobyns, Mark O’Driscoll, Kym M. Boycott
Nat Genet. Author manuscript; available in PMC 2014 Apr 25.
Published in final edited form as: Nat Genet. 2013 May; 45(5): 556–562. Published online 2013 Mar 31. doi: 10.1038/ng.2602
PMCID:
PMC4000253
AbstractArticlePDF–1.1M
6.
AMSH is an endosome-associated ubiquitin isopeptidase
John McCullough, Michael J. Clague, Sylvie Urbé
J Cell Biol. 2004 Aug 16; 166(4): 487–492. doi: 10.1083/jcb.200401141
PMCID:
PMC2172215
AbstractArticlePDF–2.1M
7.
The deubiquitinase STAMBP modulates cytokine secretion through the NLRP3 inflammasome
Joseph S. Bednash, Finny Johns, Niharika Patel, Taylor R. Smail, James D. Londino, Rama K. Mallampalli
Cell Signal. Author manuscript; available in PMC 2023 May 22.
Published in final edited form as: Cell Signal. 2021 Mar; 79: 109859. Published online 2020 Nov 27. doi: 10.1016/j.cellsig.2020.109859
PMCID:
PMC10201604
AbstractArticlePDF–1.2M
8.
STAMBP promotes lung adenocarcinoma metastasis by regulating the EGFR/MAPK signaling pathway
Hui Xu, Xiaomei Yang, Xiaofeng Xuan, Di Wu, Jieru Zhang, Xinchun Xu, Yuanjie Zhao, Chunping Ma, Dawei Li
Neoplasia. 2021 Jun; 23(6): 607–623. Published online 2021 Jun 5. doi: 10.1016/j.neo.2021.05.011
PMCID:
PMC8190130
AbstractArticlePDF–8.0M
9.
Dynamics of an active-site flap contributes to catalysis in a JAMM family metallo deubiquitinase
Amy N. Bueno, Rashmi K. Shrestha, Judith A Ronau, Aditya Babar, Michael J. Sheedlo, Julian E. Fuchs, Lake N. Paul, Chittaranjan Das
Biochemistry. Author manuscript; available in PMC 2016 Oct 6.
Published in final edited form as: Biochemistry. 2015 Oct 6; 54(39): 6038–6051. doi: 10.1021/acs.biochem.5b00631
PMCID:
PMC4962790
AbstractArticlePDF–1.0M
10.
Chemoenzymatic Synthesis of Bifunctional Polyubiquitin Substrates for Monitoring Ubiquitin Chain Remodeling
Vivian H. Trang, Margaret L. Rodgers, Kevin J. Boyle, Aaron A. Hoskins, Eric R. Strieter
Chembiochem. Author manuscript; available in PMC 2015 Jul 21.
Published in final edited form as: Chembiochem. 2014 Jul 21; 15(11): 1563–1568. Published online 2014 Jun 24. doi: 10.1002/cbic.201402059
PMCID:
PMC4130216
AbstractArticlePDF–1.4M
11.
Mechanism of Recruitment and Activation of the Endosome-associated Deubiquitinase AMSH
Christopher W. Davies, Lake N. Paul, Chittaranjan Das
Biochemistry. Author manuscript; available in PMC 2014 Nov 5.
Published in final edited form as: Biochemistry. 2013 Nov 5; 52(44): 7818–7829. Published online 2013 Oct 23. doi: 10.1021/bi401106b
PMCID:
PMC3972757
AbstractArticlePDF–2.9M
12.
Structural basis for ESCRT-III CHMP3 recruitment of AMSH
Julianna Solomons, Charles Sabin, Emilie Poudevigne, Yoshiko Usami, David Lutje Hulsik, Pauline Macheboeuf, Bettina Hartlieb, Heinrich Göttlinger, Winfried Weissenhorn
Structure. Author manuscript; available in PMC 2012 Aug 10.
Published in final edited form as: Structure. 2011 Aug 10; 19(8): 1149–1159. doi: 10.1016/j.str.2011.05.011
PMCID:
PMC3154637
AbstractArticlePDF–1.8M
13.
Endosomal Deubiquitinating Enzymes Control Ubiquitination and Down-regulation of Protease-activated Receptor 2
Burcu Hasdemir, Jane E. Murphy, Graeme S. Cottrell, Nigel W. Bunnett
J Biol Chem. 2009 Oct 9; 284(41): 28453–28466. Published online 2009 Aug 14. doi: 10.1074/jbc.M109.025692
PMCID:
PMC2788894
AbstractArticlePDF–5.0M
14.
Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding
Alessia Zamborlini, Yoshiko Usami, Sheli R. Radoshitzky, Elena Popova, Giorgio Palu, Heinrich Göttlinger
Proc Natl Acad Sci U S A. 2006 Dec 12; 103(50): 19140–19145. Published online 2006 Dec 4. doi: 10.1073/pnas.0603788103
PMCID:
PMC1748189
AbstractArticlePDF–508K
15.
Loss of Neurons in the Hippocampus and Cerebral Cortex of AMSH-Deficient Mice
Naoto Ishii, Yuji Owada, Mitsuhiro Yamada, Shigeto Miura, Kazuko Murata, Hironobu Asao, Hisatake Kondo, Kazuo Sugamura
Mol Cell Biol. 2001 Dec; 21(24): 8626–8637. doi: 10.1128/MCB.21.24.8626-8637.2001
PMCID:
PMC100023
AbstractArticlePDF–1.0M
16.
Agonist-activated glucagon receptors are deubiquitinated at early endosomes by two distinct deubiquitinases to facilitate Rab4a-dependent recycling
Suneet Kaur, Yuqing Chen, Sudha K. Shenoy
J Biol Chem. 2020 Dec 4; 295(49): 16630–16642. Published online 2021 Jan 13. doi: 10.1074/jbc.RA120.014532
PMCID:
PMC7864061
AbstractArticlePDF–3.2M
17.
K63 ubiquitin chains target NLRP3 inflammasome for autophagic degradation in ox-LDL-stimulated THP-1 macrophages
Zhenfeng Zhou, Xiaoyan Zhu, Ruihua Yin, Tianwei Liu, Shaonan Yang, Lingyan Zhou, Xudong Pan, Aijun Ma
Aging (Albany NY) 2020 Jan 31; 12(2): 1747–1759. Published online 2020 Jan 29. doi: 10.18632/aging.102710
PMCID:
PMC7053591
AbstractArticlePDF–3.1M
18.
The Vps27/Hrs/STAM (VHS) Domain of the Signal-transducing Adaptor Molecule (STAM) Directs Associated Molecule with the SH3 Domain of STAM (AMSH) Specificity to Longer Ubiquitin Chains and Dictates the Position of Cleavage
Nardeen Baiady, Prasanth Padala, Bayan Mashahreh, Einav Cohen-Kfir, Emily A. Todd, Kelly E. Du Pont, Christopher E. Berndsen, Reuven Wiener
J Biol Chem. 2016 Jan 22; 291(4): 2033–2042. Published online 2015 Nov 24. doi: 10.1074/jbc.M115.689869
PMCID:
PMC4722476
AbstractArticlePDF–1.3M
19.
Structural basis for auto-inhibition of ESCRT-III CHMP3
Suman Lata, Manfred Roessle, Julianna Solomons, Marc Jamin, Heinrich G. Gőttlinger, Dimitri I. Svergun, Winfried Weissenhorn
J Mol Biol. Author manuscript; available in PMC 2009 Oct 2.
Published in final edited form as: J Mol Biol. 2008 May 9; 378(4): 818–827. Published online 2008 Mar 20. doi: 10.1016/j.jmb.2008.03.030
PMCID:
PMC2756293
AbstractArticlePDF–1.4M
20.
Cloning of a novel signaling molecule, AMSH-2, that potentiates transforming growth factor β signaling
Nieves Ibarrola, Irina Kratchmarova, Daisuke Nakajima, William P Schiemann, Aristidis Moustakas, Akhilesh Pandey, Matthias Mann
BMC Cell Biol. 2004; 5: 2. Published online 2004 Jan 19. doi: 10.1186/1471-2121-5-2
PMCID:
PMC385422
AbstractArticlePDF–528K

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