The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels. - Wikidata - awgldk - TriplyDB

The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels.

The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels.

http://www.wikidata.org/entity/Q39961786

about

The Rise and Fall of an Evolutionary Innovation: Contrasting Strategies of Venom Evolution in Ancient and Young Animals The insecticidal neurotoxin Aps III is an atypical knottin peptide that potently blocks insect voltage-gated sodium channels Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif Diversification of a single ancestral gene into a successful toxin superfamily in highly venomous Australian funnel-web spiders.Insect-Active Toxins with Promiscuous Pharmacology from the African Theraphosid Spider Monocentropus balfouri Arthropod venoms: a vast arsenal of insecticidal neuropeptides.Spider-venom peptides as bioinsecticides Construction of a hypervirulent and specific mycoinsecticide for locust control.Isolation and preliminary characterization of proteinaceous toxins with insecticidal and antibacterial activities from black widow spider (L. tredecimguttatus) eggs Synthesis, solution structure, and phylum selectivity of a spider delta-toxin that slows inactivation of specific voltage-gated sodium channel subtypes.The insecticidal potential of venom peptides.Voltage-sensitive chloride ion channels in Anopheles gambiae Sua-1B cells.Do vicinal disulfide bridges mediate functionally important redox transformations in proteins?An insecticidal toxin from Nephila clavata spider venom.

P2860

Q27310156-E0ECEE9D-CBEB-46DB-89D3-6E27119CC9C9 Q27676741-F2D59F77-E217-410C-AD72-D09FB5A0D938 Q28533266-4CB36FF3-B3D5-44B1-BFF2-59CA975896D8 Q28743024-EC52B85D-7496-4B88-B5AB-89E76A66DBCF Q33642446-6964D396-267C-4460-8E08-A70644568FDB Q33744738-01FBA145-C555-4675-A535-7C6AFF5AEF8D Q34314435-6E5E0851-A97A-40A6-87CD-D20CBC7C23E1 Q34319661-921ACE51-794F-4498-BA48-95984793180B Q34635308-38A55903-FBC9-4238-AA4F-A7FA5770791E Q35232727-5BEE033E-C54F-4366-BFB4-035249002027 Q37433422-F4D59C58-0C3E-4B58-9FBD-07D32CA4009E Q38092679-697DAC47-0039-4187-8120-A4DACD522937 Q39243120-2BAC0D54-71F2-42B2-BAB6-9A8A48E472CB Q42844088-4C2E78FE-94CC-4603-AA36-AE66D5AB077B Q51006867-6EF3F9C8-27B4-499E-90AD-854A2E5658A8

P2860

The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels.

http://www.wikidata.org/entity/Q39961786

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年学术文章

@wuu

2008年学术文章

@zh-cn

2008年学术文章

@zh-hans

2008年学术文章

@zh-my

2008年学术文章

@zh-sg

2008年學術文章

@yue

2008年學術文章

@zh

2008年學術文章

@zh-hant

name

The Janus-faced atracotoxins are specific blockers of invertebrate K

@nl

The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels.

@en

type

label

The Janus-faced atracotoxins are specific blockers of invertebrate K

@nl

The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels.

@en

prefLabel

The Janus-faced atracotoxins are specific blockers of invertebrate K

@nl

The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels.

@en

P1433

Q39961786-6168E589-4CFC-4144-8B73-65CD9B2A97FE

P1476

Q39961786-151C1EA7-E13C-4823-A2C9-92E03E43035B

P2093

Q39961786-00E73529-F1B7-4969-8920-070692869C46

Q39961786-3F2E1CAB-3A2E-4F72-BC23-0BF90A0A2B32

Q39961786-482802EE-C087-4A08-857E-60EEB5197689

P2860

Q39961786-0EE19D40-A1D6-4474-A2A4-674C9DC5F848

Q39961786-11824DE1-F8BA-4DAA-9267-4ABBF307E5B6

Q39961786-11BBB2F0-7885-49CE-A6FB-59E193F7015A

Q39961786-16D89233-2FB8-4AED-BF72-8E73670DF307

Q39961786-1739E283-018B-446E-92EF-D82CCE7FB67B

Q39961786-25FD20F8-0488-4E0D-BEBA-972F19741712

Q39961786-2DBB18BA-5497-4855-9DF9-7A3D9810E4D6

Q39961786-3301B45C-55DD-4CA5-AB0D-9AAD519AA8E1

Q39961786-3390D67D-E105-47EB-AE6B-A0C1D6788CCC

Q39961786-3A088D55-9D86-40F8-A2CD-BC528D4D18F3

P304

Q39961786-D7005204-9484-40C7-81EF-CC23B64316E1

P31

Q39961786-D4F9C806-EB3A-4687-ADEA-ABE35CF8DF00

P356

Q39961786-9B6605FA-F0F7-46AD-8305-EAD5A24B4AF8

P407

Q39961786-51E12487-922F-4641-B665-2578BD6C6539

P433

Q39961786-753D4A76-FC79-478D-BFF4-5E384B53E10F

P478

Q39961786-E26E1BCE-A00C-44EA-8309-9E977CC65869

P50

Q39961786-76E21CAB-F18E-41B5-8A24-156B0FA3BBDA

Q39961786-8364C23B-7E4E-4999-AB97-A72861B94B53

Q39961786-95ADB9EA-4765-40BD-B790-BB5327596212

P577

Q39961786-C207F274-C177-475E-8E5D-B63BE27B12B1

P5875

Q39961786-5F82BD49-0569-45CF-945A-44C32867A292

P698

Q39961786-367B13A9-F5B9-4694-B508-B132CCD9AFE1

P356

J.1742-4658.2008.06545.X

P1433

P1476

The Janus-faced atracotoxins are specific blockers of invertebrate K(Ca) channels

@en

P2093

Francesco Maggio

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

Monique J Windley

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

Simon J Gunning

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

P2860

Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog

Inactivation of BK channels by the NH2 terminus of the beta2 auxiliary subunit: an essential role of a terminal peptide segment of three hydrophobic residues

Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N terminus

Inactivation of BK channels mediated by the NH(2) terminus of the beta3b auxiliary subunit involves a two-step mechanism: possible separation of binding and blockade

Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge

On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures

The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider

The structure of versutoxin (delta-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel

Interaction of agitoxin2, charybdotoxin, and iberiotoxin with potassium channels: selectivity between voltage-gated and Maxi-K channels

Calcium-activated potassium channels

P304

4045-4059

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

P31

scholarly article

P356

10.1111/J.1742-4658.2008.06545.X

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

P407

P433

16

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

P478

275

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

P50

Stella M. Valenzuela

Graham M Nicholson

P577

2008-07-09T00:00:00Z

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

P5875

5227404

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

P698

18625007

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