Lin, Meng-Chin A; Cannon, Stephen C; Papazian, Diane M (2018) Kv4.2 autism and epilepsy mutation enhances inactivation of closed channels but impairs access to inactivated state after opening. Proc Natl Acad Sci U S A 115:E3559-E3568
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Duarri, Anna; Lin, Meng-Chin A; Fokkens, Michiel R et al. (2015) Spinocerebellar ataxia type 19/22 mutations alter heterocomplex Kv4.3 channel function and gating in a dominant manner. Cell Mol Life Sci 72:3387-99
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Lee, Hane; Lin, Meng-chin A; Kornblum, Harley I et al. (2014) Exome sequencing identifies de novo gain of function missense mutation in KCND2 in identical twins with autism and seizures that slows potassium channel inactivation. Hum Mol Genet 23:3481-9
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Lin, Meng-chin A; Hsieh, Jui-Yi; Mock, Allan F et al. (2011) R1 in the Shaker S4 occupies the gating charge transfer center in the resting state. J Gen Physiol 138:155-63
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Lin, Meng-chin A; Abramson, Jeff; Papazian, Diane M (2010) Transfer of ion binding site from ether-a-go-go to Shaker: Mg2+ binds to resting state to modulate channel opening. J Gen Physiol 135:415-31
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Koag, Myong-Chul; Papazian, Diane M (2009) Voltage-dependent conformational changes of KVAP S4 segment in bacterial membrane environment. Channels (Austin) 3:356-65
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Lin, Meng Chin A; Papazian, Diane M (2007) Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating. Channels (Austin) 1:429-37
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Waters, Michael F; Minassian, Natali A; Stevanin, Giovanni et al. (2006) Mutations in voltage-gated potassium channel KCNC3 cause degenerative and developmental central nervous system phenotypes. Nat Genet 38:447-51
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Bannister, John P A; Chanda, Baron; Bezanilla, Francisco et al. (2005) Optical detection of rate-determining ion-modulated conformational changes of the ether-a-go-go K+ channel voltage sensor. Proc Natl Acad Sci U S A 102:18718-23
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Silverman, W R; Tang, C Y; Mock, A F et al. (2000) Mg(2+) modulates voltage-dependent activation in ether-a-go-go potassium channels by binding between transmembrane segments S2 and S3. J Gen Physiol 116:663-78
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