Zobrazeno 1 - 10
of 124
pro vyhledávání: '"Minor, DL"'
Publikováno v:
Chang, A; Abderemane-Ali, F; Hura, GL; Rossen, ND; Gate, RE; & Minor, DL. (2018). A Calmodulin C-Lobe Ca2+-Dependent Switch Governs Kv7 Channel Function. Neuron, 97(4), 836-852.e6. doi: 10.1016/j.neuron.2018.01.035. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/0dr1g0tf
© 2018 Elsevier Inc. Kv7 (KCNQ) voltage-gated potassium channels control excitability in the brain, heart, and ear. Calmodulin (CaM) is crucial for Kv7 function, but how this calcium sensor affects activity has remained unclear. Here, we present X-r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::48aa34c77de141216bf6cdf49f56b1d0
http://www.escholarship.org/uc/item/0dr1g0tf
http://www.escholarship.org/uc/item/0dr1g0tf
Autor:
Payandeh, J, Minor, DL
Publikováno v:
Payandeh, J; & Minor, DL. (2015). Bacterial voltage-gated sodium channels (BacNaVs) from the soil, sea, and salt lakes enlighten molecular mechanisms of electrical signaling and pharmacology in the brain and heart. Journal of Molecular Biology, 427(1), 3-30. doi: 10.1016/j.jmb.2014.08.010. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/33h3h9zq
© 2014 The Authors. Published by Elsevier Ltd. Voltage-gated sodium channels (NaVs) provide the initial electrical signal that drives action potential generation in many excitable cells of the brain, heart, and nervous system. For more than 60 years
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::56667c149238ec88106f3d3aea7c44fe
http://www.escholarship.org/uc/item/33h3h9zq
http://www.escholarship.org/uc/item/33h3h9zq
Tethered protein display identifies a novel kir3.2 (GIRK2) regulator from protein scaffold libraries
Publikováno v:
Minor, Daniel; Bagriantsev, SN; Chatelain, FC; Clark, KA; Alagem, N; Reuveny, E; et al.(2014). Tethered protein display identifies a novel kir3.2 (GIRK2) regulator from protein scaffold libraries. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/4028p35w
© 2014 American Chemical Society.Use of randomized peptide libraries to evolve molecules with new functions provides a means for developing novel regulators of protein activity. Despite the demonstrated power of such approaches for soluble targets,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::d4f36ab0a522f8f9bac4a9ff0c73f2b8
http://www.escholarship.org/uc/item/4028p35w
http://www.escholarship.org/uc/item/4028p35w
Publikováno v:
Lolicato, M; Riegelhaupt, PM; Arrigoni, C; Clark, KA; & Minor, DL. (2014). Transmembrane helix straightening and buckling underlies activation of mechanosensitive and thermosensitive K2P channels. Neuron, 84(6), 1198-1212. doi: 10.1016/j.neuron.2014.11.017. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/1x63q9v9
© 2014 Elsevier Inc. Mechanical and thermal activation of ion channels iscentral to touch, thermosensation, and pain. TheTRAAK/TREK K2P potassium channel subfamily produces background currents that alter neuronal excitability in response to pressure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::29d3acbdba5dea57270ec28a06187e7c
http://www.escholarship.org/uc/item/1x63q9v9
http://www.escholarship.org/uc/item/1x63q9v9
Publikováno v:
Neuron, vol 80, iss 3
Isacoff, EY; Jan, LY; & Minor, DL. (2013). Conduits of life's spark: A perspective on ion channel research since the birth of neuron. Neuron, 80(3), 658-674. doi: 10.1016/j.neuron.2013.10.040. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/08x9757c
Isacoff, EY; Jan, LY; & Minor, DL. (2013). Conduits of life's spark: A perspective on ion channel research since the birth of neuron. Neuron, 80(3), 658-674. doi: 10.1016/j.neuron.2013.10.040. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/08x9757c
Heartbeats, muscle twitches, and lightning-fast thoughts are all manifestations of bioelectricity and rely on the activity of a class of membrane proteins known as ion channels. The basic function of an ion channel can be distilled into, "The hole op
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::41a6e7bb0675004f25a32e37feda2a0c
https://escholarship.org/uc/item/08x9757c
https://escholarship.org/uc/item/08x9757c
Autor:
Minor, Daniel, Renslo, Adam, Arkin, Michelle, Bagriantsev, SN, Ang, KH, Gallardo-Godoy, A, Clark, KA, Arkin, MR, Renslo, AR, Minor, DL
Publikováno v:
Minor, Daniel; Renslo, Adam; Arkin, Michelle; Bagriantsev, SN; Ang, KH; Gallardo-Godoy, A; et al.(2013). A high-throughput functional screen identifies small molecule regulators of temperature-and mechano-sensitive K2P channels. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/5jc0k9qr
K2P (KCNK) potassium channels generate "leak" potassium currents that strongly influence cellular excitability and contribute to pain, somatosensation, anesthesia, and mood. Despite their physiological importance, K2Ps lack specific pharmacology. Add
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::a00fa9123faa6890241244e04e6df793
http://www.escholarship.org/uc/item/5jc0k9qr
http://www.escholarship.org/uc/item/5jc0k9qr
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 110, iss 16
Tien, J; Lee, HY; Minor, DL; Jan, YN; & Jan, LY. (2013). Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC). Proceedings of the National Academy of Sciences of the United States of America, 110(16), 6352-6357. doi: 10.1073/pnas.1303672110. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/9cf2p049
Tien, J; Lee, HY; Minor, DL; Jan, YN; & Jan, LY. (2013). Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC). Proceedings of the National Academy of Sciences of the United States of America, 110(16), 6352-6357. doi: 10.1073/pnas.1303672110. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/9cf2p049
Transmembrane proteins with unknown function 16 (TMEM16A) is a calcium-activated chloride channel (CaCC) important for neuronal, exocrine, and smooth muscle functions. TMEM16A belongs to a family of integral membrane proteins that includes another Ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::97ace9e1be5a23b054018590422c1251
https://escholarship.org/uc/item/9cf2p049
https://escholarship.org/uc/item/9cf2p049
Publikováno v:
Xu, Q; Chang, A; Tolia, A; & Minor, DL. (2013). Structure of a Ca2 +/CaM:Kv7.4 (KCNQ4) B-helix complex provides insight into M current modulation. Journal of Molecular Biology, 425(2), 378-394. doi: 10.1016/j.jmb.2012.11.023. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/0xp1493m
Calmodulin (CaM) is an important regulator of Kv7.x (KCNQx) voltage-gated potassium channels. Channels from this family produce neuronal M currents and cardiac and auditory IKScurrents and harbor mutations that cause arrhythmias, epilepsy, and deafne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::f32d9d54f5175886742b84b3824c21f1
http://www.escholarship.org/uc/item/0xp1493m
http://www.escholarship.org/uc/item/0xp1493m
Publikováno v:
Minor, Daniel; Bagriantsev, SN; Clark, KA; & Minor, DL. (2012). Metabolic and thermal stimuli control K 2P 2.1 (TREK-1) through modular sensory and gating domains. UC San Francisco: Retrieved from: http://www.escholarship.org/uc/item/9mj328x8
K 2P 2.1 (TREK-1) is a polymodal two-pore domain leak potassium channel that responds to external pH, GPCR-mediated phosphorylation signals, and temperature through the action of distinct sensors within the channel. How the various intracellular and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::8f8eada0b7afaba7b26cd5cc670ef6f5
http://www.escholarship.org/uc/item/9mj328x8
http://www.escholarship.org/uc/item/9mj328x8
Autor:
Chatelain FC, Gazzarrini S, Fujiwara Y, Arrigoni C, Domigan C, Ferrara G, Pantoja C, Thiel G, Moroni A, Minor DL Jr.
Publikováno v:
PloS one 4 (2009): e7496.
info:cnr-pdr/source/autori:Chatelain FC, Gazzarrini S, Fujiwara Y, Arrigoni C, Domigan C, Ferrara G, Pantoja C, Thiel G, Moroni A, Minor DL Jr./titolo:Selection of inhibitor-resistant viral potassium channels identifies a common change that affects barium and amantadine block/doi:/rivista:PloS one/anno:2009/pagina_da:e7496/pagina_a:/intervallo_pagine:e7496/volume:4
info:cnr-pdr/source/autori:Chatelain FC, Gazzarrini S, Fujiwara Y, Arrigoni C, Domigan C, Ferrara G, Pantoja C, Thiel G, Moroni A, Minor DL Jr./titolo:Selection of inhibitor-resistant viral potassium channels identifies a common change that affects barium and amantadine block/doi:/rivista:PloS one/anno:2009/pagina_da:e7496/pagina_a:/intervallo_pagine:e7496/volume:4
Methodology/Principal Findings: We used genetic selection methods to probe the interaction of two ion channel blockers, barium and amantadine, with the miniature viral potassium channel Kcv. Selection for Kcv mutants that were resistant to either blo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=cnr_________::aa975636107f74a4d381e39719b5cda4
https://publications.cnr.it/doc/9819
https://publications.cnr.it/doc/9819