Cargando…

Poring over furrows

Cryo-electron microscopy reveals the structure of a chloride channel that is closely related to a protein that transports lipids.

Detalles Bibliográficos
Autores principales:	Fisher, Skylar ID, Hartzell, H Criss
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	eLife Sciences Publications, Ltd 2017
Materias:	Biophysics and Structural Biology
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5451261/ https://www.ncbi.nlm.nih.gov/pubmed/28561734 http://dx.doi.org/10.7554/eLife.27933

Ejemplares similares

Identification of a lipid scrambling domain in ANO6/TMEM16F
por: Yu, Kuai, et al.
Publicado: (2015)

Lipids and ions traverse the membrane by the same physical pathway in the nhTMEM16 scramblase
por: Jiang, Tao, et al.
Publicado: (2017)

Dilation of fusion pores by crowding of SNARE proteins
por: Wu, Zhenyong, et al.
Publicado: (2017)

Importin-β modulates the permeability of the nuclear pore complex in a Ran-dependent manner
por: Lowe, Alan R, et al.
Publicado: (2015)

Malaria parasite CelTOS targets the inner leaflet of cell membranes for pore-dependent disruption
por: Jimah, John R, et al.
Publicado: (2016)

A selectivity filter at the intracellular end of the acid-sensing ion channel pore
por: Lynagh, Timothy, et al.
Publicado: (2017)

CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin
por: van Pee, Katharina, et al.
Publicado: (2017)

Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex
por: Vovk, Andrei, et al.
Publicado: (2016)

Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin
por: Leung, Carl, et al.
Publicado: (2014)

Single molecule compression reveals intra-protein forces drive cytotoxin pore formation
por: Czajkowsky, Daniel M, et al.
Publicado: (2015)

Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel
por: Banerjee, Anirban, et al.
Publicado: (2013)

Correction: Stepwise visualization of membrane pore formation by suilysin, a bacterial cholesterol-dependent cytolysin
por: Leung, Carl, et al.
Publicado: (2015)

Single molecule FRET reveals pore size and opening mechanism of a mechano-sensitive ion channel
por: Wang, Yong, et al.
Publicado: (2014)

Photo-switchable tweezers illuminate pore-opening motions of an ATP-gated P2X ion channel
por: Habermacher, Chloé, et al.
Publicado: (2016)

Atomistic simulations indicate the c-subunit ring of the F(1)F(o) ATP synthase is not the mitochondrial permeability transition pore
por: Zhou, Wenchang, et al.
Publicado: (2017)

Effect of helical kink in antimicrobial peptides on membrane pore formation
por: Tuerkova, Alzbeta, et al.
Publicado: (2020)

Sublytic gasdermin-D pores captured in atomistic molecular simulations
por: Schaefer, Stefan L, et al.
Publicado: (2022)

Investigating molecular crowding within nuclear pores using polarization-PALM
por: Fu, Guo, et al.
Publicado: (2017)

Mechanosensitive pore opening of a prokaryotic voltage-gated sodium channel
por: Strege, Peter R, et al.
Publicado: (2023)

Interplay between VSD, pore, and membrane lipids in electromechanical coupling in HCN channels
por: Elbahnsi, Ahmad, et al.
Publicado: (2023)

Spatial structure of disordered proteins dictates conductance and selectivity in nuclear pore complex mimics
por: Ananth, Adithya N, et al.
Publicado: (2018)

A sulfur-aromatic gate latch is essential for opening of the Orai1 channel pore
por: Yeung, Priscilla S-W, et al.
Publicado: (2020)

Ion permeation pathway within the internal pore of P2X receptor channels
por: Tam, Stephanie W, et al.
Publicado: (2023)

Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions
por: Sorum, Ben, et al.
Publicado: (2017)

A hydrophobic gate in the inner pore helix is the major determinant of inactivation in mechanosensitive Piezo channels
por: Zheng, Wang, et al.
Publicado: (2019)

The Candida albicans virulence factor candidalysin polymerizes in solution to form membrane pores and damage epithelial cells
por: Russell, Charles M, et al.
Publicado: (2022)

Calcium-dependent electrostatic control of anion access to the pore of the calcium-activated chloride channel TMEM16A
por: Lam, Andy KM, et al.
Publicado: (2018)

ML277 specifically enhances the fully activated open state of KCNQ1 by modulating VSD-pore coupling
por: Hou, Panpan, et al.
Publicado: (2019)

The P2X7 receptor forms a dye-permeable pore independent of its intracellular domain but dependent on membrane lipid composition
por: Karasawa, Akira, et al.
Publicado: (2017)

A critical residue in the α(1)M2–M3 linker regulating mammalian GABA(A) receptor pore gating by diazepam
por: Nors, Joseph W, et al.
Publicado: (2021)

Pore mutation N617D in the skeletal muscle DHPR blocks Ca(2+) influx due to atypical high-affinity Ca(2+) binding
por: Dayal, Anamika, et al.
Publicado: (2021)

Dilated cardiomyopathy mutation E525K in human beta-cardiac myosin stabilizes the interacting-heads motif and super-relaxed state of myosin
por: Rasicci, David V, et al.
Publicado: (2022)

Finding FISH in a small pond
por: Jan, Calvin H
Publicado: (2016)

Ambiguities in helical reconstruction
por: Egelman, Edward H
Publicado: (2014)

Effect of microstructure on the mechanical and damping behaviour of dragonfly wing veins
por: Rajabi, H., et al.
Publicado: (2016)

Mechanical sensitivity of Piezo1 ion channels can be tuned by cellular membrane tension
por: Lewis, Amanda H, et al.
Publicado: (2015)

Structural basis of pathogen recognition by an integrated HMA domain in a plant NLR immune receptor
por: Maqbool, A, et al.
Publicado: (2015)

Row with the flow
por: Friedrich, Benjamin M, et al.
Publicado: (2014)

Spermatozoa scattering by a microchannel feature: an elastohydrodynamic model
por: Montenegro-Johnson, T. D., et al.
Publicado: (2015)

How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4
por: Ren, Xuefeng, et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_o929a1q1eio92cuhg1sarnddha