The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Architecture of the Tuberous Sclerosis Protein Complex
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“High-resolution structures have also been generated of the complexes that regulate mTORC1 activity, including the TSC complex 158, the Rag GTPases in complex with mTORC1 and Ragulator 159–161, and the binding of leucine by Sestrin2 162.”
From Targeting the biology of aging with mTOR inhibitors (2023) · cites this paper as [158]
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Cites
The TSC1–TSC2 complex: a molecular switchboard controlling cell growth
Huang, J., & Manning, B. D. (2008) · Biochemical Journal · doi:10.1042/bj20080281 · Cited by 1,237 · cited 1×
“The TSCC stimulates Rheb GTPase activity, accumulating the GTPase in the inactive, GDP-bound, state to suppress mTORC1.(10) Spatial regulation of TSCC between the cytoplasm and lysosome is known to be pivotal for its function as a Rheb-GAP, with the current understanding being that the TSCC translocates to the lysosom…”
BackgroundMechanisms of mTORC1 activation by RHEB and inhibition by PRAS40
Yang, H., Jiang, X., Li, B., Yang, H. J., Miller, M., Yang, A., Dhar, A., & Pavletich, N. P. (2017) · Nature · doi:10.1038/nature25023 · Cited by 548
TSC1 Stabilizes TSC2 by Inhibiting the Interaction between TSC2 and the HERC1 Ubiquitin Ligase
Chong-Kopera, H., Inoki, K., Li, Y., Zhu, T., Garcia-Gonzalo, F. R., Rosa, J. L., & Guan, K.-L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c500451200 · Cited by 234
The Ras-related Protein Rheb Is Farnesylated and Antagonizes Ras Signaling and Transformation
Clark, G. J., Kinch, M. S., Rogers-Graham, K., Sebti, S. M., Hamilton, A. D., & Der, C. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10608 · Cited by 177
Lysosomal recruitment of TSC2 is a universal response to cellular stress
Demetriades, C., Plescher, M., & Teleman, A. A. (2016) · Nature Communications · doi:10.1038/ncomms10662 · Cited by 160
The Rap–RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues
Scrima, A., Thomas, C., Deaconescu, D., & Wittinghofer, A. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.30 · Cited by 127
Shumway, S. D., Li, Y., & Xiong, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200499200 · Cited by 74 · cited 1×
“…by AKT (Menon et al, 2014), and other kinases, which are thought to regulate localisation through an unknown mechanism involving 14-3-3 binding (Shumway et al, 2003; Cai et al, 2006), as well as TSCC breakdown by ubiquitination-targeted TSC2 degradation (Benvenuto et al, 2000; Chong-Kopera et…”
BackgroundQin, J., Wang, Z., Hoogeveen-Westerveld, M., Shen, G., Gong, W., Nellist, M., & Xu, W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.701870 · Cited by 37
Zech, R., Kiontke, S., Mueller, U., Oeckinghaus, A., & Kümmel, D. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.732446 · Cited by 29
Sun, W., Zhu, Y. J., Wang, Z., Zhong, Q., Gao, F., Lou, J., Gong, W., & Xu, W. (2013) · Nature Communications · doi:10.1038/ncomms3135 · Cited by 27
Flagged first, then by citations
Research works printed but not linked: 20
- Henske, 2016, Tuberous sclerosis complex, Nature Rev. Dis. Prim., 2, 16035, 10.1038/nrdp.2016.35 · DOI
- Nellist, 1999, Characterization of the cytosolic tuberin-hamartin complex. Tuberin is a cytosolic chaperone for hamartin, J. Biol. Chem., 274, 35647, 10.1074/jbc.274.50.35647 · DOI
- Santiago Lima, 2014, Identification of regions critical for the integrity of the TSC1-TSC2-TBC1D7 complex, PLoS One, 9, 10.1371/journal.pone.0093940 · DOI
- van Slegtenhorst, 1998, Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products, Hum. Mol. Genet., 7, 1053, 10.1093/hmg/7.6.1053 · DOI · Paper page
- Dibble, 2012, TBC1D7 is a third subunit of the TSC1}-{TSC2 complex upstream of {mTORC1}, Mol. Cell., 47, 535, 10.1016/j.molcel.2012.06.009 · DOI · Paper page
- González, 2017, Nutrient sensing and TOR signaling in yeast and mammals, EMBO J., 36, 397, 10.15252/embj.201696010 · DOI
- Menon, 2014, Spatial control of the TSC complex integrates insulin and nutrient regulation of mTORC1 at the lysosome, Cell, 156, 771, 10.1016/j.cell.2013.11.049 · DOI · Paper page
- Cai, 2006, Activity of TSC2 is inhibited by {AKT}-mediated phosphorylation and membrane partitioning, J. Cell. Biol., 173, 279, 10.1083/jcb.200507119 · DOI · Paper page
- Benvenuto, 2000, The tuberous sclerosis-1 (TSC1) gene product hamartin suppresses cell growth and augments the expression of the TSC2 product tuberin by inhibiting its ubiquitination, Oncogene, 19, 6306, 10.1038/sj.onc.1204009 · DOI
- Hansmann, 2020, Structural analysis of the TSC2 GAP domain: mechanistic insight into catalysis and pathogenic mutations, Structure, 10.1016/j.str.2020.05.008 · DOI
- Gai, 2016, Structure of the TBC1D7}-{TSC1 complex reveals that TBC1D7 stabilizes dimerization of the TSC1 C-terminal coiled coil region, J. Mol. Cell. Biol., 10.1093/jmcb/mjw001 · DOI
- Hoogeveen-Westerveld, 2010, Analysis of TSC1 truncations defines regions involved in TSC1 stability, aggregation and interaction, Biochim. Biophys. Acta - Mol. Basis Dis., 1802, 774, 10.1016/j.bbadis.2010.06.004 · DOI · Paper page
- Woodford, 2017, Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients, EMBO J., 36, 10.15252/embj.201796700 · DOI
- Zheng, 2017, MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy, Nature Methods, 14, 331, 10.1038/nmeth.4193 · DOI
- Rohou, 2015, CTFFIND4: fast and accurate defocus estimation from electron micrographs, J. Struct. Biol., 192, 216, 10.1016/j.jsb.2015.08.008 · DOI
- Tang, 2007, EMAN2: an extensible image processing suite for electron microscopy, J. Struct. Biol., 157, 38, 10.1016/j.jsb.2006.05.009 · DOI
- Scheres, 2012, RELION: Implementation of a Bayesian approach to cryo-EM structure determination, J. Struct. Biol., 180, 519, 10.1016/j.jsb.2012.09.006 · DOI · Paper page
- Zivanov, 2018, RELION-3: new tools for automated high-resolution cryo-EM structure determination, BioRxiv, 7
- Bepler, 2018, Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs, Nature Methods, 10812, 245
- Emsley, 2010, Features and development of Coot, Acta Crystallogr. Sect. D Biol. Crystallogr., 66, 486, 10.1107/S0907444910007493 · DOI · Paper page
Cited by
Sorted by citations
Targeting the biology of aging with mTOR inhibitors
Mannick, J. B., & Lamming, D. W. (2023) · Nature Aging · doi:10.1038/s43587-023-00416-y · Cited by 372
Tuberous sclerosis complex is associated with a novel human tauopathy
Hwang, J.-H. L., Perloff, O. S., Gaus, S. E., Benitez, C., Alquezar, C., Cosme, C. Q., Nana, A. L., Vatsavayai, S. C., Ramos, E. M., Geschwind, D. H., et al. (2023) · Acta Neuropathologica · doi:10.1007/s00401-022-02521-5 · Cited by 15
“DNA samples were screened at the University of California, Los Angeles (UCLA) using targeted sequencing of a panel of genes previously implicated in neurodegenerative disorders, including TSC1 and TSC2, as previously described [12, 16, 18].”
Method
Metadata
- Authors
- Ramlaul, K., Fu, W., Li, H., de Martin Garrido, N., He, L., Trivedi, M., Cui, W., Aylett, C. H. S., & Wu, G.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2021-01
- Volume
- 433
- Issue
- 2
- Pages
- 166743
- ISSN
- 0022-2836
- PMC
- PMC7840889
- Cited by
- 34
- References
- 11
- Language
- en
- Licence
- Funders
- Wellcome Trust
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