Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1. - Wikidata - awgldk - TriplyDB

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1.

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1.

http://www.wikidata.org/entity/Q42170057

about

Structure, function, and evolution of bacterial ATP-binding cassette systems Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery X-ray structure of the complete ABC enzyme ABCE1 from Pyrococcus abyssi Structural basis of highly conserved ribosome recycling in eukaryotes and archaea The function of ORAOV1/LTO1, a gene that is overexpressed frequently in cancer: essential roles in the function and biogenesis of the ribosome.The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species.Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry Complementation of Sulfolobus solfataricus PBL2025 with an α-mannosidase: effects on surface attachment and biofilm formation.Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation siRNA‑induced ABCE1 silencing inhibits proliferation and invasion of breast cancer cells The biological regulation of ABCE1.Iron chelators of the di-2-pyridylketone thiosemicarbazone and 2-benzoylpyridine thiosemicarbazone series inhibit HIV-1 transcription: identification of novel cellular targets--iron, cyclin-dependent kinase (CDK) 2, and CDK9 Genome-wide identification of whole ATP-binding cassette (ABC) transporters in the intertidal copepod Tigriopus japonicus.Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1.The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1 partner in the green lineage.Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast.A bridging [4Fe-4S] cluster and nucleotide binding are essential for function of the Cfd1-Nbp35 complex as a scaffold in iron-sulfur protein maturation.The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC protein Rli1 for iron-sulfur cluster insertion.MicroRNA-299-3p promotes the sensibility of lung cancer to doxorubicin through directly targeting ABCE1.A novel role for methyl cysteinate, a cysteine derivative, in cesium accumulation in Arabidopsis thaliana.Role of cellular iron and oxygen in the regulation of HIV-1 infection.ABCE1 is essential for S phase progression in human cells The CCG-domain-containing subunit SdhE of succinate:quinone oxidoreductase from Sulfolobus solfataricus P2 binds a [4Fe-4S] cluster Dynamic Regulation of a Ribosome Rescue Pathway in Erythroid Cells and Platelets.Oligomerization of human ATP-binding cassette transporters and its potential significance in human disease.Natural history of ABC systems: not only transporters.Inducible and constitutive promoters for genetic systems in Sulfolobus acidocaldarius The Candidate Antimalarial Drug MMV665909 Causes Oxygen-Dependent mRNA Mistranslation and Synergizes with Quinoline-Derived Antimalarials.Invited review: Architectures and mechanisms of ATP binding cassette proteins.EPR studies of wild type and mutant Dre2 identify essential [2Fe--2S] and [4Fe--4S] clusters and their cysteine ligands.The role of ABCE1 in eukaryotic posttermination ribosomal recycling.Mitochondrial Ferredoxin Determines Vulnerability of Cells to Copper Excess.SIMPLE LEAF3 encodes a ribosome-associated protein required for leaflet development in Cardamine hirsuta.Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways.Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation.Fe-S Clusters Emerging as Targets of Therapeutic Drugs.In a quest for engineering acidophiles for biomining applications: challenges and opportunities.Clinical and genetic aspects of defects in the mitochondrial iron-sulfur cluster synthesis pathway.ABCE Proteins: From Molecules to Development

P2860

Q24643436-C54C29D0-57C9-4694-B897-C998B159FF51 Q26850111-F6D0B18A-E054-4BC1-976B-90EDF914476F Q27649434-EC5E0997-483A-47A5-AB97-FC3D538BB21C Q27677430-2BF397E6-7983-42AC-B265-7D83E89DDCB3 Q27935986-9CD13358-B533-4A38-8B9E-B78A4BE7B19D Q27939493-0095E04D-2126-49F5-B9D6-D598228A2572 Q28821599-AA1A58E9-88DC-4FD3-8E82-445D8575E792 Q34077321-426E74E4-7D7B-44F0-A783-A5AE1FB2827A Q34094284-EF1D23A7-5482-413F-B8D2-F780D28356F1 Q34105175-66559CAE-41E6-4982-8607-483D424E26D5 Q34301701-B5A28A5F-4398-4387-9613-6F8AD51E8688 Q34458484-D9CC26CF-701C-4C83-B0CD-A4FF156B876A Q34584687-9C04D091-3F62-4257-8DC2-78207EBF729F Q34602675-2F6B84A2-10C2-4D8E-A859-78E8BF2FD4C4 Q34867547-C7270F96-C759-4712-99A2-3012514F946C Q35651041-7F568510-0ED7-456E-937B-89C8ED51E5A1 Q35874509-AE55C749-AA5D-49DC-8E4B-41EF99D9D73D Q35913501-3A257B8B-1ADA-4220-B974-F910BC2ECE73 Q36261264-16E2E0B4-83D0-4FF2-9033-ED4AF8FEC7FE Q36288111-8910E992-890D-44A7-B597-3736BB803619 Q36839068-39AC8B4B-24DF-4EE9-BE1E-5A08F30265F9 Q36956965-C9EB038D-CF28-4A85-AA5D-7F05A4215C1E Q37369269-76CE3CFA-5924-40FD-865F-B46E0CF888D3 Q37417290-EEBD2A03-7B0D-4DB7-85E0-CB2733E297F0 Q37564553-4F17BE06-100C-4D1C-BCE4-2C971E87E1EA Q37941750-A7921622-BD43-4D02-9D86-581AB3C74888 Q38345844-34D6060F-A6F0-4A03-A90D-0B8BA8C21AD3 Q38708103-4C12CE61-630F-493F-97F8-2C96123E79E1 Q38796195-D7510AF7-2A54-4CD4-B03D-16725EDB6375 Q39348082-5A320364-0FE8-4DD6-88D9-83C6D047756D Q41929275-1154793F-D5A2-41C0-85A0-4DD6199B97E0 Q42640010-04B13420-A43F-4D99-8AAC-E2EF06F58712 Q46788406-E9520229-9C68-43DA-BB82-B3FA861BF45A Q47862572-6046C6F4-6587-4588-8245-62650051C312 Q48337146-C6084AA2-946A-4114-83AC-4D58901EA094 Q49312659-FA18AF40-8281-41C5-8367-445E379CEE05 Q50868052-4DDACCDB-DD09-468C-A3F1-E29F3358E296 Q52721206-A91D5D93-FC09-45D6-B070-952A60BC7E1B Q57609560-6CF466E1-275E-4F3F-9178-9CEA32523C5B

P2860

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1.

http://www.wikidata.org/entity/Q42170057

description

2007 nî lūn-bûn

@nan

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

Structural organization of ess ...... inding cassette protein ABCE1.

@en

Structural organization of ess ...... inding cassette protein ABCE1.

@nl

type

label

Structural organization of ess ...... inding cassette protein ABCE1.

@en

Structural organization of ess ...... inding cassette protein ABCE1.

@nl

prefLabel

Structural organization of ess ...... inding cassette protein ABCE1.

@en

Structural organization of ess ...... inding cassette protein ABCE1.

@nl

P1433

Q42170057-841FB55B-5EEE-4723-B989-86EE52BE6B31

P1476

Q42170057-247932E4-FB4F-48F4-AE22-47BFD24AB526

P2093

Q42170057-154917AD-81AF-467E-A9A3-6F42A7255E30

Q42170057-20B79B48-B4C8-4579-A8E9-DA01AA164DBC

Q42170057-3095DCC1-FD80-4245-9EBB-417AB3657209

Q42170057-3744F4AB-CB8C-4EE7-9562-487304C4138E

Q42170057-53931459-5558-4ED9-B4E6-8D736BD5D952

Q42170057-90785236-EFEA-48E6-8921-49170217D26B

Q42170057-AD88C3AA-8A12-4585-807D-FBE8C69E43B9

Q42170057-F4545533-7392-462F-8C98-FB9C208D9928

P2860

Q42170057-0047A98C-4D92-44B3-8D3C-8BFAFB3ABA2C

Q42170057-03F341D2-1770-497B-ACFE-CF44D4E51BA3

Q42170057-0406D1DB-9797-4948-944B-848944980C68

Q42170057-0D54C73C-012D-4812-BCD1-C48CA4DD1596

Q42170057-166FA144-63A0-4DB1-B9F1-CFA929D6195C

Q42170057-16A1697C-3664-4E58-BAA7-4358E70E7C6D

Q42170057-30F64586-D6DF-46AD-A83C-16DDC7495D2E

Q42170057-397D6557-B7C8-4A4F-898E-7B280CDCD77B

Q42170057-3980FC4D-E4B5-4E46-8505-145CFDC0C42D

Q42170057-44686675-AB4D-4F65-82B1-8A834CCB0C2B

P304

Q42170057-38B56A53-4C06-42DD-8923-C741CF6B6BD7

P31

Q42170057-532D1E49-6B41-409D-8DCA-56568CDE4EAF

P356

Q42170057-175C8FB0-919D-4D82-B4B0-3B7EC41ED2AB

P407

Q42170057-E88322A2-36F7-4F0E-8611-63AC53CC404A

P433

Q42170057-0FC24066-B735-431A-95F7-7D2F876532FF

P478

Q42170057-84099C7E-87D8-4B12-AB0A-6E720FD42F17

P50

Q42170057-126AB65A-1651-4A0E-8131-19BEDE665C2E

Q42170057-5896857C-1A8F-47AA-8A6F-7F1C118FD431

Q42170057-AE1D772E-7D24-43DE-A609-9B9CA67B8406

Q42170057-E7E72BF2-DEA3-47E8-BB0E-08CAB9864292

P577

Q42170057-87F953CA-5929-4454-B432-C7BC4569833D

P698

Q42170057-12E004B3-5622-4E51-947C-F2BE61CCDE31

P356

P1433

Journal of Biological Chemistry

P1476

Structural organization of ess ...... binding cassette protein ABCE1

@en

P2093

Adam Janoschka

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

Dominik Barthelme

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

Eckhard Bill

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

Marco Salamone Stagni

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

Stephanie Dinkelaker

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

Urte Scheele

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

Volker Schünemann

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

Wolfram Meyer-Klaucke

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

P2860

Cloning and characterization of a RNAse L inhibitor. A new component of the interferon-regulated 2-5A pathway

Functional link between ribosome formation and biogenesis of iron-sulfur proteins

How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation

The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly.

The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins.

The ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p.

Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria.

Computational identification of cis-regulatory elements associated with groups of functionally related genes in Saccharomyces cerevisiae

The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif

Iron-sulfur clusters: nature's modular, multipurpose structures.

P304

14598-14607

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

P31

scholarly article

P356

10.1074/JBC.M700825200

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

P407

P433

19

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

P478

282

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

P50

Sonja-Verena Albers

Arnold J.M Driessen

Fraser MacMillan

P577

2007-03-12T00:00:00Z

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

P698

17355973

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