Mutations at arginine 352 alter the pore architecture of CFTR.
about
The Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): THREE-DIMENSIONAL STRUCTURE AND LOCALIZATION OF A CHANNEL GATEImpact of distant charge reversals within a robust beta-barrel protein poreEvolutionary and functional divergence between the cystic fibrosis transmembrane conductance regulator and related ATP-binding cassette transporters.Single residue within the antigen translocation complex TAP controls the epitope repertoire by stabilizing a receptive conformation.Three charged amino acids in extracellular loop 1 are involved in maintaining the outer pore architecture of CFTR.Dual roles of the sixth transmembrane segment of the CFTR chloride channel in gating and permeation.Modeling the conformational changes underlying channel opening in CFTRFull-open and closed CFTR channels, with lateral tunnels from the cytoplasm and an alternative position of the F508 region, as revealed by molecular dynamics.A Point Mutation in the Ubiquitin Ligase RNF170 That Causes Autosomal Dominant Sensory Ataxia Destabilizes the Protein and Impairs Inositol 1,4,5-Trisphosphate Receptor-mediated Ca2+ SignalingCystic fibrosis transmembrane conductance regulator: a molecular model defines the architecture of the anion conduction path and locates a "bottleneck" in the pore.Murine and human CFTR exhibit different sensitivities to CFTR potentiators.Nonintegral stoichiometry in CFTR gating revealed by a pore-lining mutation.Transmembrane helical interactions in the CFTR channel pore.Locating a plausible binding site for an open-channel blocker, GlyH-101, in the pore of the cystic fibrosis transmembrane conductance regulator.The CFTR ion channel: gating, regulation, and anion permeationTwo salt bridges differentially contribute to the maintenance of cystic fibrosis transmembrane conductance regulator (CFTR) channel function.Acute inhibition of the cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel by thyroid hormones involves multiple mechanisms.Functional architecture of the CFTR chloride channel.Electrostatic tuning of the pre- and post-hydrolytic open states in CFTRArchitecture and functional properties of the CFTR channel pore.Tuning of CFTR chloride channel function by location of positive charges within the pore.Regulation of conductance by the number of fixed positive charges in the intracellular vestibule of the CFTR chloride channel pore.Changes in accessibility of cytoplasmic substances to the pore associated with activation of the cystic fibrosis transmembrane conductance regulator chloride channel.Cystic Fibrosis Transmembrane Conductance Regulator (CFTR): CLOSED AND OPEN STATE CHANNEL MODELS.Cystic fibrosis transmembrane conductance regulator: using differential reactivity toward channel-permeant and channel-impermeant thiol-reactive probes to test a molecular model for the pore.Structural mechanisms of CFTR function and dysfunction.ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore.
P2860
Q27674253-7CE7B005-C149-460C-B7CF-BE8643E8B73EQ30156821-E1B7AABB-63EB-4E31-8CDC-F44D9C35EFFAQ30484656-959C7194-DD37-4534-80D9-D7243AB49382Q33927361-C3E0FC0C-4EA3-4F2B-B119-FB9E230ACA89Q33964059-089998D9-5B6F-494F-8B86-ED9DF958C0CAQ34096449-CBC3BC8C-351A-467E-A526-90A7397A4DF8Q35005061-4178B8DE-37E6-4AC4-BED9-9D65BC0501B2Q35306053-37ED3BA4-6E9F-4FBC-BAD0-252F3D6942BBQ35662322-21FA18DB-7EF3-4967-92BE-6E6427CB0E3DQ35862414-AD3F0770-8FBB-41A4-B222-9A47E98E0DE5Q36122891-F2186374-9B15-4DFA-85D9-3B39343CA2B1Q36277880-BBA4335A-B609-4BD2-B37F-0D9386C0172EQ36412336-FCBB8899-C02D-4409-B9A0-EA6051D947F0Q36412828-64DE41E0-26D8-4CBE-93E8-0347AC6ABD9BQ36488258-ADCA962B-E176-47B1-9E38-A55F73FA5898Q37012562-108D1B20-53DC-477B-B707-89AD3DAE7377Q37234590-0C81135D-618E-4BF3-A703-AE5F5D462E90Q38171539-24F3FAFD-A406-4917-9029-CF5240548AAEQ38938736-7ABC0FB0-569F-42F3-B0DE-2EAA7970905CQ38971502-FA116FDC-EF7A-4824-B3B9-EAF3969C1BF0Q39256255-14A575AC-2CB3-466D-942A-713A418C1345Q39289067-96D146C5-61A9-4D8A-8E92-A02A8234E15EQ39673058-44AD05CF-802E-4CE6-ADC4-577B7E44B56FQ40675000-F18D4B8F-269B-4C31-B4A9-DEA1F8CE5240Q42588798-D9BF2CE1-9F07-4144-8D48-9079C000BB18Q52629670-AAE49F82-66B7-44DE-B6EE-D46004EE8959Q54211454-0F7FA5C3-EDB9-46D1-9DE9-E644A9A382CA
P2860
Mutations at arginine 352 alter the pore architecture of CFTR.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Mutations at arginine 352 alter the pore architecture of CFTR.
@ast
Mutations at arginine 352 alter the pore architecture of CFTR.
@en
type
label
Mutations at arginine 352 alter the pore architecture of CFTR.
@ast
Mutations at arginine 352 alter the pore architecture of CFTR.
@en
prefLabel
Mutations at arginine 352 alter the pore architecture of CFTR.
@ast
Mutations at arginine 352 alter the pore architecture of CFTR.
@en
P2093
P2860
P1476
Mutations at arginine 352 alter the pore architecture of CFTR.
@en
P2093
Andrew R W O'Brien
Binlin Song
Guiying Cui
Nael A McCarty
Zhi-Ren Zhang
P2860
P2888
P304
P356
10.1007/S00232-008-9105-9
P577
2008-03-01T00:00:00Z