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Items: 12

1.

Structural and functional insights into transmembrane AMPA receptor regulatory protein complexes.

Twomey EC, Yelshanskaya MV, Sobolevsky AI.

J Gen Physiol. 2019 Oct 15. pii: jgp.201812264. doi: 10.1085/jgp.201812264. [Epub ahead of print] Review.

PMID:
31615831
2.

Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding.

Twomey EC, Ji Z, Wales TE, Bodnar NO, Ficarro SB, Marto JA, Engen JR, Rapoport TA.

Science. 2019 Aug 2;365(6452). pii: eaax1033. doi: 10.1126/science.aax1033. Epub 2019 Jun 27.

PMID:
31249135
3.

Mechanisms of Channel Block in Calcium-Permeable AMPA Receptors.

Twomey EC, Yelshanskaya MV, Vassilevski AA, Sobolevsky AI.

Neuron. 2018 Sep 5;99(5):956-968.e4. doi: 10.1016/j.neuron.2018.07.027. Epub 2018 Aug 16.

4.

Mechanism of calmodulin inactivation of the calcium-selective TRP channel TRPV6.

Singh AK, McGoldrick LL, Twomey EC, Sobolevsky AI.

Sci Adv. 2018 Aug 15;4(8):eaau6088. doi: 10.1126/sciadv.aau6088. eCollection 2018 Aug.

5.

Opening of the human epithelial calcium channel TRPV6.

McGoldrick LL, Singh AK, Saotome K, Yelshanskaya MV, Twomey EC, Grassucci RA, Sobolevsky AI.

Nature. 2018 Jan 11;553(7687):233-237. doi: 10.1038/nature25182. Epub 2017 Dec 20.

6.

Structural Mechanisms of Gating in Ionotropic Glutamate Receptors.

Twomey EC, Sobolevsky AI.

Biochemistry. 2018 Jan 23;57(3):267-276. doi: 10.1021/acs.biochem.7b00891. Epub 2017 Oct 27.

7.

Channel opening and gating mechanism in AMPA-subtype glutamate receptors.

Twomey EC, Yelshanskaya MV, Grassucci RA, Frank J, Sobolevsky AI.

Nature. 2017 Sep 7;549(7670):60-65. doi: 10.1038/nature23479. Epub 2017 Jul 24.

8.

Structural Bases of Desensitization in AMPA Receptor-Auxiliary Subunit Complexes.

Twomey EC, Yelshanskaya MV, Grassucci RA, Frank J, Sobolevsky AI.

Neuron. 2017 May 3;94(3):569-580.e5. doi: 10.1016/j.neuron.2017.04.025.

9.

Elucidation of AMPA receptor-stargazin complexes by cryo-electron microscopy.

Twomey EC, Yelshanskaya MV, Grassucci RA, Frank J, Sobolevsky AI.

Science. 2016 Jul 1;353(6294):83-6. doi: 10.1126/science.aaf8411.

10.

Substantial conformational change mediated by charge-triad residues of the death effector domain in protein-protein interactions.

Twomey EC, Cordasco DF, Kozuch SD, Wei Y.

PLoS One. 2013 Dec 31;8(12):e83421. doi: 10.1371/journal.pone.0083421. eCollection 2013.

11.

Profound conformational changes of PED/PEA-15 in ERK2 complex revealed by NMR backbone dynamics.

Twomey EC, Cordasco DF, Wei Y.

Biochim Biophys Acta. 2012 Dec;1824(12):1382-93. doi: 10.1016/j.bbapap.2012.07.001. Epub 2012 Jul 20.

PMID:
22820249
12.

High-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions.

Twomey EC, Wei Y.

Biochem Biophys Res Commun. 2012 Jul 20;424(1):141-6. doi: 10.1016/j.bbrc.2012.06.091. Epub 2012 Jun 23.

PMID:
22732408

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