Evidence map›Paper›PMID 27189123›Full record

ArticleThe Journal of antibiotics2016

Quinovosamycins: new tunicamycin-type antibiotics in which the α, β-1″,11'-linked N-acetylglucosamine residue is replaced by N-acetylquinovosamine.

Neil Pj Price, David P Labeda, Todd A Naumann, Karl E Vermillion, Michael J Bowman, Mark A Berhow, William W Metcalf, Kenneth M Bischoff

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in The Journal of antibiotics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.6field-weighted citation impact, top 15% of its field
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

12 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Staying in the loop to make ends meet: roles and regulation of GlmR inbioRxiv : the preprint server for biology · 2025
    Article
  3. Approaches to stereoselective 1,1'-glycosylation.Beilstein journal of organic chemistry · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Tunicamycin: chemical synthesis and biosynthesis.The Journal of antibiotics · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
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

8 authors at 2 institutions in 1 country.

Neil Pj PriceRenewable Products Technology Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, IL, USA.
David P LabedaMycotoxin Prevention and Applied Microbiology Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, IL, USA.
Todd A NaumannMycotoxin Prevention and Applied Microbiology Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, IL, USA.
Karl E VermillionFunctional Foods Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, IL, USA.
Michael J BowmanBioenergy Research Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, IL, USA.
Mark A BerhowFunctional Foods Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, IL, USA.
William W MetcalfDepartment of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
Kenneth M BischoffRenewable Products Technology Unit, National Center for Agricultural Utilization Research, USDA-ARS, Peoria, IL, USA.
National Center for Agricultural Utilization Research · USUniversity of Illinois Urbana-Champaign · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tunicamycins (TUN) are potent inhibitors of polyprenyl phosphate N-acetylhexosamine 1-phosphate transferases (PPHP), including essential eukaryotic GPT enzymes and bacterial HexNAc 1-P translocases. Hence, TUN blocks the formation of eukaryotic N-glycoproteins and the assembly of bacterial call wall polysaccharides. The genetic requirement for TUN production is well-established. Using two genes unique to the TUN pathway (tunB and tunD) as probes we identified four new prospective TUN-producing strains. Chemical analysis showed that one strain, Streptomyces niger NRRL B-3857, produces TUN plus new compounds, named quinovosamycins (QVMs). QVMs are structurally akin to TUN, but uniquely in the 1″,11'-HexNAc sugar head group, which is invariably d-GlcNAc for the known TUN, but is d-QuiNAc for the QVM. Surprisingly, this modification has only a minor effect on either the inhibitory or antimicrobial properties of QVM and TUN. These findings have unexpected consequences for TUN/QVM biosynthesis, and for the specificity of the PPHP enzyme family.

Indexed as

AcetylglucosamineAnti-Bacterial AgentsEnzyme InhibitorsGlucosamineStreptomycesTunicamycin6-desoxy-D-glucosamineAcetylglucosamineAnti-Bacterial AgentsEnzyme InhibitorsGlucosamineTunicamycin

Identifiers

PMID27189123
OpenAlexW2400176803

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.