ABC transporters: the power to change - Test2 - elhamkhani - TriplyDB

ABC transporters: the power to change

ABC transporters: the power to change

http://www.wikidata.org/entity/Q24634548

about

Two ABCB4 point mutations of strategic NBD-motifs do not prevent protein targeting to the plasma membrane but promote MDR3 dysfunction Hyperinsulinemic Hypoglycemia - The Molecular Mechanisms How Does the VSG Coat of Bloodstream Form African Trypanosomes Interact with External Proteins?Structural Features of the ATP-Binding Cassette (ABC) Transporter ABCA3 Visualizing functional motions of membrane transporters with molecular dynamics simulations Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery Inter-domain communication mechanisms in an ABC importer: a molecular dynamics study of the MalFGK2E complex Structural basis of GDP release and gating in G protein coupled Fe2+ transport Insights into How Nucleotide-Binding Domains Power ABC Transport Structural insights into tail-anchored protein binding and membrane insertion by Get3 The role of vicinal tyrosine residues in the function of Haemophilus influenzae ferric-binding protein A ABC ATPase signature helices in Rad50 link nucleotide state to Mre11 interface for DNA repair.Crystal structure of a phosphorylation-coupled saccharide transporter Evidence for an allosteric mechanism of substrate release from membrane-transporter accessory binding proteins Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition A suite of Switch I and Switch II mutant structures from the G-protein domain of FeoB Assembly and mechanism of a group II ECF transporter myo-Inositol and D-Ribose Ligand Discrimination in an ABC Periplasmic Binding Protein Structure and mechanism of the UvrA-UvrB DNA damage sensor Structural and Thermodynamic Characterization of the Interaction between Two Periplasmic Treponema pallidum Lipoproteins that are Components of a TPR-Protein-Associated TRAP Transporter (TPAT)Asymmetric states of vitamin B₁₂ transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF Crystallization and preliminary crystallographic analysis of GanB, a GH42 intracellular β-galactosidase fromGeobacillus stearothermophilus Structural and Functional Characterization of an Orphan ATP-Binding Cassette ATPase Involved in Manganese Utilization and Tolerance in Leptospira spp Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC Structure of a bacterial energy-coupling factor transporter Crystal structure of a folate energy-coupling factor transporter from Lactobacillus brevis Crystal structures of nucleotide-free and glutathione-bound mitochondrial ABC transporter Atm1 Structure-specificity relationships in Abp, a GH27 β-L-arabinopyranosidase from Geobacillus stearothermophilus T6 Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F Structure-function relationships in Gan42B, an intracellular GH42 β-galactosidase from Geobacillus stearothermophilus Metrabase: a cheminformatics and bioinformatics database for small molecule transporter data analysis and (Q)SAR modeling An update on iron acquisition by Legionella pneumophila: new pathways for siderophore uptake and ferric iron reduction A gene optimization strategy that enhances production of fully functional P-glycoprotein in Pichia pastoris Molecular evolutionary analysis of ABCB5: the ancestral gene is a full transporter with potentially deleterious single nucleotide polymorphisms Optimized purification of a heterodimeric ABC transporter in a highly stable form amenable to 2-D crystallization A novel flow cytometric HTS assay reveals functional modulators of ATP binding cassette transporter ABCB6 Tuning the drug efflux activity of an ABC transporter in vivo by in vitro selected DARPin binders BIRB796, the inhibitor of p38 mitogen-activated protein kinase, enhances the efficacy of chemotherapeutic agents in ABCB1 overexpression cells The ATP-binding cassette transporter Cbc (choline/betaine/carnitine) recruits multiple substrate-binding proteins with strong specificity for distinct quaternary ammonium compounds

P2860

Q24336685-E17A51B7-076E-489F-B51A-3CE90DD0342E Q26749617-A522F2D2-BF74-49EE-B030-A16087F15D59 Q26771466-C7ABFD4F-8ABC-4786-9583-6E209AA0FBDC Q26795758-20E67C61-0F7C-43F7-9EE6-25DA1508A26D Q26826746-29476B43-272B-4A35-998A-380F544B2236 Q26850111-A6DB1EDF-3B20-4693-AB4E-3881AC1E116E Q27333190-0646F0AE-D44B-459E-A71C-C41DD0BF539D Q27656687-6EA3F2F0-FD08-4041-B3DF-F0AFFC78DD52 Q27657410-A4283875-9BDE-4BC0-A7F8-B69585DAC3E0 Q27658386-4FCDD391-B165-4067-8F6E-A145E43A943B Q27664200-AE8402CB-4276-470A-9934-34FC59128747 Q27667335-D9F2187F-E19A-4397-8E64-44E7D0C36CFC Q27667450-86563C00-33E0-4935-8FA4-F505CF4296B1 Q27675569-1CC1DF68-C54F-47C9-A850-BA16CB90CC96 Q27675630-298E225B-1BF7-41D1-801D-29CE52A6BBAE Q27675670-0E0CB2A0-DAD8-4A16-8F10-423A796EEF55 Q27676043-15877E56-68BC-4CF9-8FBE-C5BD7A77CBF6 Q27676855-45C7B434-F57B-4010-9033-7E79568179DC Q27677070-B76ABE80-3DCA-4BB6-A5EE-4EE6AB8C64F9 Q27678513-8D6E295B-409A-485E-809F-F94F05247FFF Q27678966-DF47111C-E837-44BD-B937-A773CBA4893D Q27680178-3DD5F641-516D-416D-B520-C0F4A21AC6DE Q27680331-8A3995E5-C094-4976-806B-9D20D919C206 Q27682423-B68C4446-AB12-4874-9528-6CE574BD11AB Q27683855-47FC8C04-6DE9-4387-AA11-9F9F436E4179 Q27684411-85E69A43-10C4-40EF-91D2-4CE200D509E9 Q27684413-776E7375-FD73-4BC1-9986-C751A08F969A Q27689450-11B93731-0D0D-41DC-B695-EF02D55086EB Q27696147-2B118380-BC93-4DA1-BE32-35EC20039CB2 Q27696181-AD1A0C88-5BF5-4DFC-96B2-BCA920E12395 Q27702912-9963146E-B545-4CB5-8727-57B8B08D9241 Q27902340-48BF940A-9B92-4951-A2F2-5E1485B49A91 Q28082373-33147761-ABE9-4C13-9AA3-90BFD47A94F1 Q28476421-6386E86D-CF12-4A40-BDB9-AA7E01B37FD7 Q28476833-A3BD7A02-143A-485F-B990-0BF023F8D2AE Q28478129-C80348E6-5CA4-4AC9-805B-8D66F6ED92BF Q28481236-9B0FBF5B-618A-4442-A843-F4C4CC5DC654 Q28484084-6E22CD60-4FEC-4737-B70B-6667EFD5B70C Q28485188-6AEAA991-16AE-42F2-B72B-E5BF941F313B Q28492830-7BBB37AA-2348-4BCA-9A15-08ADAEAA8E5C

P2860

ABC transporters: the power to change

http://www.wikidata.org/entity/Q24634548

description

2009 nî lūn-bûn

@nan

2009 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մարտին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

ABC transporters: the power to change

@ast

ABC transporters: the power to change

@en

ABC transporters: the power to change

@nl

type

label

ABC transporters: the power to change

@ast

ABC transporters: the power to change

@en

ABC transporters: the power to change

@nl

prefLabel

ABC transporters: the power to change

@ast

ABC transporters: the power to change

@en

ABC transporters: the power to change

@nl

P1433

Q24634548-FFF9EF1B-13E2-4768-9BE6-7537B82D5657

P1476

Q24634548-F52610D9-6695-4BE1-A7D8-BB07F7DE5623

P2093

Q24634548-281084A4-BD34-4B75-8A4F-CD6C8E2EFB5F

Q24634548-6904A8C4-0852-4E2B-BD27-8DD2A6D35D0E

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P2860

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Q24634548-2425FA56-EC32-42EA-9EE4-D8254C7062CB

P2888

Q24634548-FD94945D-83AB-469B-A654-1F359E761F86

P304

Q24634548-A154BE7F-3876-4EBA-B3AD-4F6AB0CE9562

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P3181

Q24634548-27A76A07-4DF9-4FCB-BF27-7A45576BFC74

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Q24634548-950E78A4-B38A-42C9-A420-1D3BC1965E27

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Q24634548-555791CE-F930-40E6-A4E6-008C28FF4836

P478

Q24634548-7A5A8E3A-E53B-465C-890D-AF88CCBFF7C8

P577

Q24634548-7603239F-CA28-43B0-92A8-4A9062E0CBC2

P5875

Q24634548-773E33B9-086B-401D-9D53-5DA3382A11FC

P6179

Q24634548-A7D58BEE-0848-41EE-8515-A623AC243DF3

P698

Q24634548-BD23C38D-C33E-4E84-BE1C-B112B2AE20A3

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P932

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P3181

P356

P1433

Nature Reviews Molecular Cell Biology

P1476

ABC transporters: the power to change

@en

P2093

Douglas C Rees

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

Eric Johnson

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

Oded Lewinson

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

P2860

The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

The Protein Data Bank

H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer

Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters

Ras-catalyzed hydrolysis of GTP: a new perspective from model studies

Structure, function, and evolution of bacterial ATP-binding cassette systems

Structural insights into ABC transporter mechanism

The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation

P2888

P304

218-27

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

P31

scholarly article

P3181

183471

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

P356

10.1038/NRM2646

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

P407

P433

3

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

P478

10

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

P577

2009-03-01T00:00:00Z

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

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24032263

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

P6179

1007127980

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

P698

19234479

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

P921

P932

2830722

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