Review. SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator. - Wikidata - awgldk - TriplyDB

Review. SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator.

Review. SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator.

http://www.wikidata.org/entity/Q37319861

about

Mutations in ABCD4 cause a new inborn error of vitamin B12 metabolism Store-independent activation of Orai1 by SPCA2 in mammary tumors Sulfonylurea receptor 1 in central nervous system injury: a focused review Molecular action of sulphonylureas on KATP channels: a real partnership between drugs and nucleotides Insights into How Nucleotide-Binding Domains Power ABC Transport Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states Structural basis for allosteric cross-talk between the asymmetric nucleotide binding sites of a heterodimeric ABC exporter.Identification of putative potassium channel homologues in pathogenic protozoa Transcriptome-based identification of ABC transporters in the western tarnished plant bug Lygus hesperus Inhibition of the Sur1-Trpm4 channel reduces neuroinflammation and cognitive impairment in subarachnoid hemorrhage Brief suppression of Abcc8 prevents autodestruction of spinal cord after trauma Asymmetric switching in a homodimeric ABC transporter: a simulation study Quaternary structure of KATP channel SUR2A nucleotide binding domains resolved by synchrotron radiation X-ray scattering.The molecular mechanisms and pharmacotherapy of ATP-sensitive potassium channel gene mutations underlying neonatal diabetes Mutations of the same conserved glutamate residue in NBD2 of the sulfonylurea receptor 1 subunit of the KATP channel can result in either hyperinsulinism or neonatal diabetes Glibenclamide for the treatment of ischemic and hemorrhagic stroke.ATP-Binding Cassette Transporter Structure Changes Detected by Intramolecular Fluorescence Energy Transfer for High-Throughput Screening.Ionotropic GABA and Glutamate Receptor Mutations and Human Neurologic Diseases.Sulfonylurea Receptor 1 in Humans with Post-Traumatic Brain Contusions.Silencing of Abcc8 or inhibition of newly upregulated Sur1-Trpm4 reduce inflammation and disease progression in experimental autoimmune encephalomyelitis.KATP Channels in the Cardiovascular System.The sulfonylurea receptor 1 (Sur1)-transient receptor potential melastatin 4 (Trpm4) channel TRPM5-mediated calcium uptake regulates mucin secretion from human colon goblet cells.Comparative proteomic analysis of the ATP-sensitive K+ channel complex in different tissue types Sulfonylurea receptor 1 expression in human cerebral infarcts.Sulfonylurea receptor 1 subunits of ATP-sensitive potassium channels and myocardial ischemia/reperfusion injury.Exploring conformational equilibria of a heterodimeric ABC transporter.Glibenclamide in cerebral ischemia and stroke Permanent neonatal diabetes due to activating mutations in ABCC8 and KCNJ11.Neonatal diabetes caused by activating mutations in the sulphonylurea receptor Mitochondrial channels: ion fluxes and more.Comparative review of dipeptidyl peptidase-4 inhibitors and sulphonylureas.Clinical or ATPase domain mutations in ABCD4 disrupt the interaction between the vitamin B12-trafficking proteins ABCD4 and LMBD1.Mechanistic diversity in ATP-binding cassette (ABC) transporters.Molecular mechanisms of congenital hyperinsulinism due to autosomal dominant mutations in ABCC8.The Pancreatic β-Cell: A Bioenergetic Perspective.Phosphatidylinositol 4,5-biphosphate (PIP2) modulates interaction of syntaxin-1A with sulfonylurea receptor 1 to regulate pancreatic β-cell ATP-sensitive potassium channels.The ATP-sensitive K(+) channel ABCC8 S1369A type 2 diabetes risk variant increases MgATPase activity.LKB1 couples glucose metabolism to insulin secretion in mice.

P2860

Q24297470-676FB595-B3BF-4F70-9ECB-4EE254189A3D Q24301440-E36760C2-A6F5-45D1-9FD6-AB7EAA2A48C5 Q24606564-EF4CCF03-7A26-4937-B134-44AAF1E795A6 Q26777728-17F0CD30-14D8-46D6-9D11-D8F4260E2ABC Q27657410-099E78EF-804A-4035-9849-F220639C8E6D Q27678196-DE48FF83-88A3-44BC-AEA6-10262CC1E09A Q27678363-F02831FD-117F-4426-A5BC-9E0CC0F8C331 Q27684709-95E7513C-8FDC-4140-9FE2-92D9B3099362 Q28481066-6F2A87CC-B132-4364-9F7E-E45534A4CCD1 Q28544994-7DE5FFA0-63BF-4856-BE4D-FD6155D57708 Q28575299-EFEE1708-0102-4E13-AEA4-56068F044E1A Q30273785-63C1DBC2-1C29-4ADC-A2BF-1D57A76EA2EC Q33573560-4652D3C1-AAAF-4299-BDD0-F42A79F12106 Q33638129-1A3147D4-781B-4A4E-B8CA-60C34366847F Q34316689-EF5E2631-0DBC-45B2-A8C4-B4B638FE6BFB Q35043410-507638EC-C532-4B35-BC50-F335699425E7 Q35380697-400F398B-DF9A-4FFD-8763-B10C061F16C0 Q35617947-37B2151B-DB31-4A1E-B314-1AE58D668F90 Q35745930-3543BD9F-1C9D-4FF6-B9DF-6AC86F0B1542 Q36108663-C861C2DF-FFE6-4704-A47A-86BE7BD91F8E Q36298402-BE833B6B-79AE-4590-BFBA-1E5C1ED12E7B Q36422478-3C4D8E91-490F-421B-8A6E-32BD1598732A Q36579645-AB5EB36B-C40B-4561-947E-931AF7DE47E8 Q36887004-BC5A0DC5-6FC6-4EA0-ACB7-8D87697A6BE3 Q37030254-C1793E50-7C25-4423-826B-4B78CF8E0C49 Q37167025-05F2D7BE-B70C-4305-A1AC-FB237B48C1BB Q37252932-88DFFFE2-566E-4648-8976-EAA083E8D128 Q37564876-34AFCFC5-174D-49AB-BEBE-25FEC6324F6B Q37638478-8CA956EB-17A5-4948-AC95-11AE2DF4DAB4 Q37797962-663EBAC6-52C0-4E4B-B87D-BCA44669FE17 Q38117598-C71DBE5F-705C-48D8-84B2-A588185B715D Q38201407-3B3D67DE-8EBE-493A-BE39-EA60C61AFDFF Q38644587-CFB9EEE8-67D7-40A4-9AEC-87EFC0FF7C5C Q38701568-81FBBA8B-4821-4BBA-ACA0-3E792AB9B7D8 Q38856661-BFF9588B-BA50-4077-AA04-7A3A8780AB66 Q38861985-2CD7897D-FCC2-4DB9-A583-525C803C0A9D Q38943061-9597CAC7-F648-48FE-80C0-BD1F3D32C964 Q39034153-9CBED2BF-2150-4B6A-9375-FE9A3BB84F21 Q39783056-D3EA2341-EB55-4E55-886C-8C5BDD9F67D3 Q41072650-4B4784A7-2553-41E9-B75B-35B332B50B11

P2860

Review. SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator.

http://www.wikidata.org/entity/Q37319861

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on January 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Review. SUR1: a unique ATP-bin ...... s as an ion channel regulator.

@en

Review. SUR1: a unique ATP-bin ...... s as an ion channel regulator.

@nl

type

label

Review. SUR1: a unique ATP-bin ...... s as an ion channel regulator.

@en

Review. SUR1: a unique ATP-bin ...... s as an ion channel regulator.

@nl

prefLabel

Review. SUR1: a unique ATP-bin ...... s as an ion channel regulator.

@en

Review. SUR1: a unique ATP-bin ...... s as an ion channel regulator.

@nl

P1433

Q37319861-EE871B7A-5998-431E-93CE-E4E1A00A5A9D

P1476

Q37319861-2D88A06C-61FB-4987-B653-61595215A654

P2093

Q37319861-09F29827-D063-44FD-9157-26F35094C130

Q37319861-83A4AE9A-4BE0-454C-AA5F-4F4B47428C15

Q37319861-9F3AF117-CE23-4C4D-90DD-1216A097D27D

Q37319861-F5F83EEA-3B2F-4789-B7E7-E58D1559107C

P2860

Q37319861-00F0C223-AF3D-46E6-B4B0-0B3FCF0B35B0

Q37319861-06320FA7-643B-49BE-88B9-65E30F00EA96

Q37319861-071F3BB8-15C8-4D3E-BFAD-D5A9705C9796

Q37319861-0753481E-B517-4B6B-82AD-1810A6FF5E65

Q37319861-0AD64827-7248-49BF-833E-25C20A5C2D1B

Q37319861-15BB6003-4CBF-4ACF-981C-33ED5C00DE0F

Q37319861-16629D40-641A-4EF1-A98D-3B82EB6ED028

Q37319861-19BEEF67-0A75-4A5B-8613-6A4D86DBFCC1

Q37319861-1E940083-7421-4D34-9DA0-87AC227783C5

Q37319861-1FD6B7AE-2A2E-44FE-98E0-6FF2850E471F

P304

Q37319861-1658BBFD-7EFB-427A-9831-291636DB0984

P31

Q37319861-925BEDAF-6AA0-4844-9C2A-173CB941C77A

P356

Q37319861-E04695AA-E274-4A2C-A4F2-373F60EBA76F

P407

Q37319861-BD07F329-9AD9-4025-A0DC-49EFE010B612

P433

Q37319861-D6F99957-40FD-405C-B4CB-B12181E620BB

P478

Q37319861-452BFA81-8D89-4D02-A570-1E6DE30DA1A4

P50

Q37319861-67E48DC3-C337-4BEE-BB80-39EA042F9B66

Q37319861-D590F6A0-B350-4C85-89C2-8D8FCBD49323

P577

Q37319861-5980ABEC-70AF-4EE0-A333-14D0FA94AC95

P5875

Q37319861-9CFE90DE-96A4-4D36-9033-69558F132453

P698

Q37319861-F8E201E2-6627-4119-B0C9-2C0A5CF19302

P932

Q37319861-3EE3D850-2938-47C9-AACE-68D05BFD0313

P356

P1433

Philosophical Transactions of the Royal Society B

P1476

Review. SUR1: a unique ATP-bin ...... ns as an ion channel regulator

@en

P2093

Constantina Fotinou

http://www.w3.org/2001/XMLSchema#string

Frances M Ashcroft

http://www.w3.org/2001/XMLSchema#string

Jussi Aittoniemi

http://www.w3.org/2001/XMLSchema#string

Peter Proks

http://www.w3.org/2001/XMLSchema#string

P2860

The synaptic vesicle cycle

The essential role of the Walker A motifs of SUR1 in K-ATP channel activation by Mg-ADP and diazoxide

M-LDH serves as a sarcolemmal K(ATP) channel subunit essential for cell protection against ischemia

A mutation (R826W) in nucleotide-binding domain 1 of ABCC8 reduces ATPase activity and causes transient neonatal diabetes

The ABC protein turned chloride channel whose failure causes cystic fibrosis

Flexibility in the ABC transporter MsbA: Alternating access with a twist.

Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP

Two regions of sulfonylurea receptor specify the spontaneous bursting and ATP inhibition of KATP channel isoforms.

A heterozygous activating mutation in the sulphonylurea receptor SUR1 (ABCC8) causes neonatal diabetes.

Activating mutations in the ABCC8 gene in neonatal diabetes mellitus.

P304

257-267

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1098/RSTB.2008.0142

http://www.w3.org/2001/XMLSchema#string

P407

P433

1514

http://www.w3.org/2001/XMLSchema#string

P478

364

http://www.w3.org/2001/XMLSchema#string

P50

P577

2009-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

23457874

http://www.w3.org/2001/XMLSchema#string

P698

18990670

http://www.w3.org/2001/XMLSchema#string

P932

2674095

http://www.w3.org/2001/XMLSchema#string