Cardiolipin: a proton trap for oxidative phosphorylation. - Wikidata - wikimedia - TriplyDB

Cardiolipin: a proton trap for oxidative phosphorylation.

Cardiolipin: a proton trap for oxidative phosphorylation.

http://www.wikidata.org/entity/Q34151397

about

Alkaliphilic Bacteria with Impact on Industrial Applications, Concepts of Early Life Forms, and Bioenergetics of ATP Synthesis Bioenergetics and the role of soluble cytochromes C for alkaline adaptation in gram-negative alkaliphilic Pseudomonas Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into Barth syndrome Cardiolipin membrane domains in prokaryotes and eukaryotes Cardiolipin and electron transport chain abnormalities in mouse brain tumor mitochondria: lipidomic evidence supporting the Warburg theory of cancer Barth Syndrome: From Mitochondrial Dysfunctions Associated with Aberrant Production of Reactive Oxygen Species to Pluripotent Stem Cell Studies Response mechanisms of bacterial degraders to environmental contaminants on the level of cell walls and cytoplasmic membrane Cardiolipin and its different properties in mitophagy and apoptosis Molecular dynamics simulations of the bacterial UraA H+-uracil symporter in lipid bilayers reveal a closed state and a selective interaction with cardiolipin Antimicrobial Peptides Targeting Gram-Positive Bacteria Lipids in the assembly of membrane proteins and organization of protein supercomplexes: implications for lipid-linked disorders X-ray structure, thermodynamics, elastic properties and MD simulations of cardiolipin/dimyristoylphosphatidylcholine mixed membranes Cardiolipin fingerprinting of leukocytes by MALDI-TOF/MS as a screening tool for Barth syndrome Disorders of phospholipid metabolism: an emerging class of mitochondrial disease due to defects in nuclear genes Evaluation of the cardiolipin biosynthetic pathway and its interactions in the diabetic heart The self-organizing fractal theory as a universal discovery method: the phenomenon of life Induction of P-glycoprotein expression and activity by Aconitum alkaloids: Implication for clinical drug-drug interactions Magic angle spinning 31P NMR spectroscopy reveals two essentially identical ionization states for the cardiolipin phosphates in phospholipid liposomes Cardiolipin, a critical determinant of mitochondrial carrier protein assembly and function.Membrane deformation under local pH gradient: mimicking mitochondrial cristae dynamics Relationship between cardiolipin metabolism and oxygen availability in Bacillus subtilis.Direct MALDI-MS analysis of cardiolipin from rat organs sections.Cytochrome c signalosome in mitochondria.The role of calcium-independent phospholipase A2 in cardiolipin remodeling in the spontaneously hypertensive heart failure rat heart Identification of unique cardiolipin and monolysocardiolipin species in Acinetobacter baumannii.F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches.Protonmotive pathways and mechanisms in the cytochrome bc1 complex.Microbial diversity and biogeochemical cycling in soda lakes.Chromosome Replication in Escherichia coli: Life on the Scales.Crosstalk between DnaA protein, the initiator of Escherichia coli chromosomal replication, and acidic phospholipids present in bacterial membranes.New findings in ATP supply in rod outer segments: insights for retinopathies.Complete genome sequence of "Thioalkalivibrio sulfidophilus" HL-EbGr7.Alkaline pH homeostasis in bacteria: new insights.Molecular strategies for targeting antioxidants to mitochondria: therapeutic implications.Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes Heterogeneity of genetic pathways toward daptomycin nonsusceptibility in Staphylococcus aureus determined by adjunctive antibiotics Localized proton microcircuits at the biological membrane-water interface Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that support the ability to grow in an external pH range from 7.5 to 11.4.

P2860

Q21131320-B1632E5F-AA1E-4A11-8745-C32793AB451E Q21284487-E2819989-CC93-42E6-AF43-913F0139F0ED Q24598420-A056B342-E1A0-47E2-91D2-EEAE1A961B82 Q24651872-170AFB2C-F7A2-416A-A320-0B62EF3C8177 Q24657248-791F6505-5715-4A7A-B818-46DD04F4BB4F Q24658168-23FC658B-3C2F-48EE-BF39-F07BC5D07A3D Q26772690-B4A0BBE0-4D81-4171-81E1-A9AF53CFDCEF Q27012745-F6D235E3-CFCD-4BB3-8302-B6F8C4AC5E31 Q27024440-DEAED427-AD2B-4032-AD07-4503E7E6E638 Q27319873-B922ADDF-69DC-482F-8706-0D21056F7A12 Q28077888-6ADBC4C7-3E3B-46C2-88BF-CCDA8997A505 Q28386214-0A40425D-6806-421A-8A1B-29CE8E94B95E Q28386282-4580216F-E14B-4043-89A9-FD8F5FA01F54 Q28386643-39345ADA-EDF5-4B1B-8A03-7D9CC0674C4F Q28387241-E485EBDD-944C-4F9F-B370-6E8E4E0A2A27 Q28390032-7ACEA9CB-3690-4106-A1DC-2F7B9A2DB3A2 Q28740893-C0CD4A8F-AF33-42D1-A0DB-59907186DA46 Q28833675-B368CC7B-B2B6-4117-9DE3-F373850A4E8D Q29247994-B1E58686-B841-4A2B-BA76-E05EE19E565C Q30376858-050C5C61-9EAE-46DA-8A18-B899A5BF27A4 Q30484410-D9731AED-E5BE-4BB6-B25F-B28521637B5D Q30540198-11334DE5-04D9-41C9-B649-4587097E942E Q33266037-3EB1341B-23D4-4438-9040-511D8A7CC9AC Q33352540-D3C103FA-0A51-4A15-A080-332BD6D3C012 Q33634137-B9AF7465-282E-454F-BA05-9BF1C1AC511C Q33774463-2356BA7F-B215-4CBE-A5B3-16F64F0285F8 Q33931346-FFE87C44-0AA6-42B1-B73E-AB9564C42DD0 Q33944665-31AE9433-376F-4C2C-9023-B68073F80C8C Q33966394-D8073D5A-AEDE-4C3E-9184-DE9FE95770B9 Q34151974-01A43AD4-C69C-47AD-B651-646BB474A269 Q34295716-9CD5A024-1AA5-480B-82C9-72099B3D5C42 Q34339951-611FBD08-02E2-442F-98D5-168C0D525C67 Q34713848-098A304D-0C22-49B3-B69C-BF1E9119E745 Q34769079-A0854A92-827F-4192-9272-4225B713298B Q34772638-4E77EEAF-7BC1-4B57-B35F-64867B5058CB Q35148462-1BA1F155-2F34-42BB-AC87-769658EF9D53 Q35220127-4C54ECBE-B4D5-45EE-9042-28CAC64DD944 Q35385568-EB387834-274F-47FE-9464-292E5E3F997E Q35544455-AF568E1F-C85F-4C9B-8618-49293EEB39CF Q35587253-18888940-B2FE-430F-994A-8A154AF13AD6

P2860

Cardiolipin: a proton trap for oxidative phosphorylation.

http://www.wikidata.org/entity/Q34151397

description

2002 nî lūn-bûn

@nan

2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Cardiolipin: a proton trap for oxidative phosphorylation.

@ast

Cardiolipin: a proton trap for oxidative phosphorylation.

@en

Cardiolipin: a proton trap for oxidative phosphorylation.

@nl

type

label

Cardiolipin: a proton trap for oxidative phosphorylation.

@ast

Cardiolipin: a proton trap for oxidative phosphorylation.

@en

Cardiolipin: a proton trap for oxidative phosphorylation.

@nl

prefLabel

Cardiolipin: a proton trap for oxidative phosphorylation.

@ast

Cardiolipin: a proton trap for oxidative phosphorylation.

@en

Cardiolipin: a proton trap for oxidative phosphorylation.

@nl

P1433

Q34151397-DBE5CB59-836B-40A3-8CEF-345E71E67418

P1476

Q34151397-AE2827BF-3525-4508-87B0-56AE79EE6BB0

P2093

Q34151397-06B01869-608A-4233-9D20-8D664A0DCC13

Q34151397-D88F7C94-F645-47C8-9119-36A41430881B

P2860

Q34151397-01B486B7-B7A2-4691-BF14-7F9FD2EBFFCD

Q34151397-069507EE-D49A-4216-8D12-B33BD0D6A2A5

Q34151397-0841C368-DF49-41D9-8BB5-DB798BCC06AE

Q34151397-10B28962-5EAB-4F56-820D-8ADBB0482F88

Q34151397-168D684B-E330-4063-A60C-92DF3D77A053

Q34151397-2A5766B6-178E-41C1-9C8C-4AFF9BBE8977

Q34151397-30397DDB-787C-4B95-AD2C-7B04FA428C41

Q34151397-3E7C9465-2358-441E-80A1-D145601F5B5F

Q34151397-421B908C-2CBA-4868-8D79-6BB65CE83E38

Q34151397-54B9687B-11D9-4C42-BC9D-2C52B77BE2BC

P304

Q34151397-9C03933D-50F0-4902-8C37-AB81F9502260

P31

Q34151397-00E66326-E0E1-4EED-B879-14B7DE57FE37

P356

Q34151397-1BC7B4BB-FA31-413F-A78D-456E7EBBBE34

P407

Q34151397-68217AC9-6571-46B6-9CD2-67EFC0194A19

P433

Q34151397-981566E0-EF24-4D84-8C2E-FAE93AD12EF5

P478

Q34151397-4E823554-E299-41C7-8F91-1442AB647855

P577

Q34151397-2C80344C-5627-46BE-827A-546C4E4CFA0D

P698

Q34151397-9A8E8BA9-AADF-4E00-AC93-AF5BE7D46834

P921

Q34151397-F47B4252-D067-4937-96BD-19BABD82F7FD

P356

S0014-5793(02)03292-1

P1433

P1476

Cardiolipin: a proton trap for oxidative phosphorylation.

@en

P2093

Norbert A Dencher

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

Thomas H Haines

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

P2860

Supercomplexes in the respiratory chains of yeast and mammalian mitochondria

Structural details of an interaction between cardiolipin and an integral membrane protein

Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c

Absence of cardiolipin in the crd1 null mutant results in decreased mitochondrial membrane potential and reduced mitochondrial function.

Lateral communication by fast proton conduction: a model membrane study

Is there a conserved interaction between cardiolipin and the type II bacterial reaction center?

The biosynthesis and functional role of cardiolipin

Cardiolipin is not essential for the growth of Saccharomyces cerevisiae on fermentable or non-fermentable carbon sources.

Cardiolipins and mitochondrial proton-selective leakage.

Reverse engineering a protein: the mechanochemistry of ATP synthase.

P304

35-39

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

P31

scholarly article

P356

10.1016/S0014-5793(02)03292-1

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

P407

P433

1-3

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

P478

528

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

P577

2002-09-01T00:00:00Z

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

P698

12297275

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

P921

phosphorylation