Evidence map›Paper›PMID 25815151›Full record

ArticleACS medicinal chemistry letters2015

Synthesis and Evaluation of Quinazolines as Inhibitors of the Bacterial Cell Division Protein FtsZ.

Gabriella M Nepomuceno, Katie M Chan, Valerie Huynh, Kevin S Martin, Jared T Moore, Terrence E O'Brien, Luiz A E Pollo, Francisco J Sarabia, Clarissa Tadeus, Zi Yao and 3 more

Abstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Compound Uptake intoACS infectious diseases · 2021
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Targeting the Bacterial Division Protein FtsZ.Journal of medicinal chemistry · 2016
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Gabriella M NepomucenoUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Katie M ChanUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Valerie HuynhUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Kevin S MartinUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Jared T MooreUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Terrence E O'BrienUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Luiz A E PolloUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Francisco J SarabiaUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Clarissa TadeusUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Zi YaoUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
David E AndersonUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
James B AmesUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.
Jared T ShawUniversity of California, Davis , One Shields Avenue, Davis, California 95616, United States.

Funding

New Research Initiatives and Collaborative Interdisciplinary Research ($10,000-$2R01AI080931 · NIAID · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SHAW, JARED THOMAS · 2010 to 2014
$1.9M
6 · The paper itself

Abstract

The bacterial cell division protein FtsZ is one of many potential targets for the development of novel antibiotics. Recently, zantrin Z3 was shown to be a cross-species inhibitor of FtsZ; however, its specific interactions with the protein are still unknown. Herein we report the synthesis of analogues that contain a more tractable core structure and an analogue with single-digit micromolar inhibition of FtsZ's GTPase activity, which represents the most potent inhibitor of Escherichia coli FtsZ reported to date. In addition, the zantrin Z3 core has been converted to two potential photo-cross-linking reagents for proteomic studies that could shed light on the molecular interactions between FtsZ and molecules related to zantrin Z3.

Indexed as

bacterial cell divisionFtsZSARzantrin Z3

Identifiers

PMID25815151
PMCPMC4360151

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.