Evidence map›Paper›PMID 21812451›Full record

ArticleOrganic letters2011

Enzymatic timing and tailoring of macrolactamization in syringolin biosynthesis.

William M Wuest, Daniel Krahn, Markus Kaiser, Christopher T Walsh

Abstract read
In one paragraph

Article in Organic letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. 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

4 authors.

William M WuestDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Daniel Krahn
Markus Kaiser
Christopher T Walsh

Funding

The Vancomycin Biosynthetic Assembly lineR01GM049338 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALSH, CHRISTOPHER T · 1993 to 2012
$6.2M
Formation, Tailoring and Incorporation of Piperazates in Kutzneride BiosynthesisF32GM091779 · NIGMS · HARVARD MEDICAL SCHOOL · PI WUEST, WILLIAM M · 2010 to 2011
$77k
NIGMS NIH HHS F32 GM091779NIGMS NIH HHS GM091779NIGMS NIH HHS GM49338NIGMS NIH HHS R01 GM049338
6 · The paper itself

Abstract

The enzymatic activation of 3,4-dehydrolysine and subsequent formation of the 12-membered syringolin macrolactam were investigated. The timing of the desaturation was elucidated through the analysis of the initial adenylation domain of SylD. The SylD-TTE didomain was characterized and demonstrated to be the catalyst for formation of 12-membered macrocycles. When the SylD thioesterase domain was reacted with a family of acyclic CoA both natural and unnatural macrocycles were generated.

Indexed as

Molecular StructurePeptides, CyclicStereoisomerismThiolester HydrolasesUreaPeptides, Cyclicsyringolin Asyringolin BThiolester HydrolasesUrea

Identifiers

PMID21812451
PMCPMC3163001

What OpenQuestion holds

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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.