Interactions of halichondrin B and eribulin with tubulin. - Wikidata - awgldk - TriplyDB

Interactions of halichondrin B and eribulin with tubulin.

Interactions of halichondrin B and eribulin with tubulin.

http://www.wikidata.org/entity/Q35088820

about

Phylogeny drives large scale patterns in Australian marine bioactivity and provides a new chemical ecology rationale for future biodiscovery A novel natural phenyl alkene with cytotoxic activity Natural products as sources of new drugs over the 30 years from 1981 to 2010 Tumour biology, metastatic sites and taxanes sensitivity as determinants of eribulin mesylate efficacy in breast cancer: results from the ERIBEX retrospective, international, multicenter study.The design, synthesis and biological evaluation of conformationally restricted 4-substituted-2,6-dimethylfuro[2,3-d]pyrimidines as multi-targeted receptor tyrosine kinase and microtubule inhibitors as potential antitumor agents.Evading Pgp activity in drug-resistant cancer cells: a structural and functional study of antitubulin furan metotica compounds.Complementary isonitrile-based multicomponent reactions for the synthesis of diversified cytotoxic hemiasterlin analogues Eribulin targets a ch-TOG-dependent directed migration of cancer cells Eribulin mesylate: mechanism of action of a unique microtubule-targeting agent.Eribulin: a novel cytotoxic chemotherapy agent.Molecular simulations of drug-receptor complexes in anticancer research.Cytotoxicity and glycan-binding properties of an 18 kDa lectin isolated from the marine sponge Halichondria okadai.Clinical efficacy of eribulin mesylate for the treatment of metastatic soft tissue sarcoma.HMBA is a putative HSP70 activator stimulating HEXIM1 expression that is down-regulated by estrogen.Eribulin alone or in combination with the PLK1 inhibitor BI 6727 triggers intrinsic apoptosis in Ewing sarcoma cell lines.Managing sarcoma: where have we come from and where are we going?Effects of eribulin, vincristine, paclitaxel and ixabepilone on fast axonal transport and kinesin-1 driven microtubule gliding: implications for chemotherapy-induced peripheral neuropathy.Antineoplastic agents. 592. Highly effective cancer cell growth inhibitory structural modifications of dolastatin 10.[Search for natural substances with therapeutic activity: George R. Pettit].

P2860

Q28536739-8715259E-F588-423D-9CA5-C3C62F0DDB1B Q28820748-11466C54-44F8-4CC9-A74F-9F5D76506A87 Q29616640-79C8A030-7685-422B-867B-3973E2E08074 Q33426567-5DE17018-C28A-44E8-9499-03395FE92E89 Q35539229-0E48245E-C0B0-4B6F-9946-26CB2F5E8087 Q35951551-4A78C2E3-F82E-402E-A4CB-9105E1146A8E Q36389900-C1C5F4B3-6CBB-4E6D-B288-0A4B4D1B9FF7 Q36561555-3E6B3117-6946-43F0-A9B3-66834C08E8EB Q36742259-C22A1315-7192-473A-B217-F88175DE9FC0 Q38012442-BCE7BF78-5FC5-4593-844E-0DD9B0FFE4E9 Q38054133-F5F9193F-3846-4718-9046-BF1E5D14998F Q38323687-E3C0C45E-4D13-451B-8F21-B0050D52AC17 Q38688042-7B465FF4-F54C-4953-961A-7B67AB23907C Q38715966-8B5E44C0-415B-4DF8-AF81-A5779918049E Q41592750-4B491981-E156-4B66-A0B7-558D1B555F67 Q41988197-655A34C8-B39C-479F-9D92-6DBAA6216BC3 Q42112858-3E887272-8698-4F7F-A118-5165194A5F54 Q42761153-376DFEFE-86E6-49E4-93E4-C1538EBF8522 Q52335669-59415AAE-F567-4558-A81A-28A2F4268B26

P2860

Interactions of halichondrin B and eribulin with tubulin.

http://www.wikidata.org/entity/Q35088820

description

2011 nî lūn-bûn

@nan

2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Interactions of halichondrin B and eribulin with tubulin.

@ast

Interactions of halichondrin B and eribulin with tubulin.

@en

type

label

Interactions of halichondrin B and eribulin with tubulin.

@ast

Interactions of halichondrin B and eribulin with tubulin.

@en

prefLabel

Interactions of halichondrin B and eribulin with tubulin.

@ast

Interactions of halichondrin B and eribulin with tubulin.

@en

P1433

Q35088820-AB63FD77-9C95-432A-89FB-192E46BE0D83

P1476

Q35088820-109EBB4A-FBB0-4FE2-A3BA-8B988D90D8FE

P2093

Q35088820-286BE132-D628-4A71-A2E6-BC313B33FED8

Q35088820-3A4B9D4F-7B8B-460C-8C46-BFA0B92E2010

Q35088820-46A456D6-C74E-4CF6-A1CA-41D8E59FD67A

Q35088820-9E7AA12E-AD91-4CBE-A26C-AE4364F3EE0B

Q35088820-A6611913-3A83-4224-A83D-E5E6AE8359C3

Q35088820-AE1C4B6E-750E-41C3-A76C-4C696F7B023A

Q35088820-CBC6D25E-23F3-494E-88BC-AF61A495C463

Q35088820-D3D3B265-F53E-4761-8A50-ED15A26F02A2

Q35088820-ED21B13B-54A6-4B63-AA10-60A2A231F765

P2860

Q35088820-0CCD0ECE-F6DC-4966-9B78-0049A24F9354

Q35088820-16553F68-ADC6-4757-9212-0B25FEA300ED

Q35088820-259BA0D8-4D1D-4672-B129-50074A5B0DC2

Q35088820-437AA5C1-DDC0-4573-9C02-65B39E5C790A

Q35088820-4EDEB1E4-EBA1-4DD6-A7FA-1E2300219DB6

Q35088820-4F8AB777-2B02-4D07-A25F-65393F1911A6

Q35088820-53BE4DA0-8C76-4623-B3B9-FDA58C2B2B6C

Q35088820-5D41A3F7-9EA9-4DEE-B379-78B6DC94632A

Q35088820-63CB2108-BA13-4FCA-BC83-C9CD4E2D8308

Q35088820-663236D3-3170-48CF-AC67-C77A830AD66F

P304

Q35088820-37018A2C-5C64-4921-A8EC-981B5F6CA04A

P31

Q35088820-2B742A02-37F4-4D06-9575-224469F1927C

P356

Q35088820-C680FD8F-6387-4819-A814-AFFC2239928F

P433

Q35088820-37585DDC-804C-43EC-B536-46EA5DD5AE6C

P478

Q35088820-74622399-C58A-4DB4-9CFC-0DFF55F444C6

P577

Q35088820-BFC137AF-8F9D-441A-AA1A-B2A7D4967D28

P5875

Q35088820-736D50A9-BF04-4547-9BE5-E7BF9F91AB58

P698

Q35088820-D1E0ABD7-2FF2-46B1-AB0D-FF7143F1777D

P932

Q35088820-67B14DF6-7C80-47E6-8209-C142FDDB0E8A

P356

P1433

Journal of Chemical Information and Modeling

P1476

Interactions of halichondrin B and eribulin with tubulin.

@en

P2093

Amos B Smith

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

Ernest Hamel

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

George R Pettit

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

James C Burnett

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

Murray H G Munro

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

Onur Atasoylu

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

Rick Gussio

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

Ruoli Bai

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

Tam Luong Nguyen

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

P2860

Eribulin binds at microtubule ends to a single site on tubulin to suppress dynamic instability

Inhibition of centromere dynamics by eribulin (E7389) during mitotic metaphase

Refined structure of alpha beta-tubulin at 3.5 A resolution

Structural insight into the inhibition of tubulin by vinca domain peptide ligands

Variations in the colchicine-binding domain provide insight into the structural switch of tubulin

AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

In vitro and in vivo anticancer activities of synthetic macrocyclic ketone analogues of halichondrin B

The primary antimitotic mechanism of action of the synthetic halichondrin E7389 is suppression of microtubule growth

Halichondrin B and homohalichondrin B, marine natural products binding in the vinca domain of tubulin. Discovery of tubulin-based mechanism of action by analysis of differential cytotoxicity data

Phase II evaluation of eribulin mesylate (E7389, NSC 707389) in patients with metastatic or recurrent squamous cell carcinoma of the head and neck: Southwest Oncology Group trial S0618.

P304

1393-1404

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

P31

scholarly article

P356

10.1021/CI200077T

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

P433

6

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

P478

51

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

P577

2011-05-13T00:00:00Z

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

P5875

51095299

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

P698

21539396

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

P932

3130535

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