Antimycobacterial Rufomycin Analogues from Streptomyces atratus Strain MJM3502 (Q89592353)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:32031795%20AND%20SRC:MED&resulttype=core&format=json

6 April 2020

title

Antimycobacterial Rufomycin Analogues from Streptomyces atratus Strain MJM3502 (English)

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6 April 2020

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JSZUQPCUWLSQDN-XNBMOWNFSA-N

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DFIBTJXEVPMOBW-CFTAYRILSA-N

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(3S,6S,9S,12S,15S,18S,21S)-15-[(E)-but-2-enyl]-6-[(4-hydroxy-3-nitrophenyl)methyl]-1,3,10-trimethyl-12-[[1-(2-methylbut-3-en-2-yl)indol-3-yl]methyl]-9,18,21-tris(2-methylpropyl)-1,4,7,10,13,16,19-heptazacyclohenicosane-2,5,8,11,14,17,20-heptone

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WXBUPQKGSIPZCL-GXETYBQQSA-N

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1

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6 April 2020

Hyun Lee

12

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6 April 2020

Jonathan Bisson

13

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6 April 2020

James B McAlpine

14

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6 April 2020

Shao-Nong Chen

15

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6 April 2020

Sang-Hyun Cho

16

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6 April 2020

Scott G. Franzblau

17

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6 April 2020

Guido F Pauli

18

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6 April 2020

author name string

Gauri Shetye

2

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6 April 2020

Yang Yu

3

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6 April 2020

Bernard D Santarsiero

4

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6 April 2020

Larry L Klein

5

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6 April 2020

Cele Abad-Zapatero

6

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6 April 2020

Nina M Wolf

7

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6 April 2020

Jinhua Cheng

8

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6 April 2020

Yingyu Jin

9

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6 April 2020

Hanki Lee

10

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6 April 2020

Joo-Won Suh

11

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6 April 2020

publication date

7 February 2020

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full work available at URL

6 April 2020

https://pubs.acs.org/doi/pdf/10.1021/acs.jnatprod.9b01095

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19 March 2024

https://api.unpaywall.org/v2/10.1021/acs.jnatprod.9b01095?email=unpaywall_01@example.com

published in

Journal of Natural Products

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6 April 2020

volume

83

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6 April 2020

page(s)

657-667

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6 April 2020

issue

3

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6 April 2020

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19 March 2024

https://api.unpaywall.org/v2/10.1021/acs.jnatprod.9b01095?email=unpaywall_01@example.com

access restriction status

open access

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inferred from online access status

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Residual Complexity Does Impact Organic Chemistry and Drug Discovery: The Case of Rufomyazine and Rufomycin.

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Rufomycin Targets ClpC1 Proteolysis in Mycobacterium tuberculosis and M. abscessus

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12 December 2020

High-Resolution Structure of ClpC1-Rufomycin and Ligand Binding Studies Provide a Framework to Design and Optimize Anti-Tuberculosis Leads

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