Evidence map›Paper›PMID 27936626›Full record

ReviewChemical reviews2017

Oxidative Cyclization in Natural Product Biosynthesis.

Man-Cheng Tang, Yi Zou, Kenji Watanabe, Christopher T Walsh, Yi Tang

Open access · greenAbstract readReview
In one paragraph

Review in Chemical reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
34.9field-weighted citation impact, top 1% 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

142 citing papers in PubMed, 412 citations in OpenAlex.

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82 more citing papers are in PubMed but not listed here.

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

5 authors at 3 institutions in 2 countries.

Man-Cheng TangDepartment of Chemical and Biomolecular Engineering, and Department of Chemistry and Biochemistry, University of California, Los Angeles , 420 Westwood Plaza, Los Angeles, California 90095, United States.
Yi ZouDepartment of Chemical and Biomolecular Engineering, and Department of Chemistry and Biochemistry, University of California, Los Angeles , 420 Westwood Plaza, Los Angeles, California 90095, United States.
Kenji WatanabeDepartment of Pharmaceutical Sciences, University of Shizuoka , Shizuoka 422-8526, Japan.
Christopher T WalshStanford University Chemistry, Engineering, and Medicine for Human Health (ChEM-H), Stanford University , 443 Via Ortega, Stanford, California 94305, United States.
Yi TangDepartment of Chemical and Biomolecular Engineering, and Department of Chemistry and Biochemistry, University of California, Los Angeles , 420 Westwood Plaza, Los Angeles, California 90095, United States.ORCID http://orcid.org/0000-0003-1597-0141
University of California, Los Angeles · USStanford University · USUniversity of Shizuoka · JP

Funding

Genomic and synthetic biology tools for expressing natural product gene clustersU01GM110706 · NIGMS · STANFORD UNIVERSITY · PI DAVIS, RONALD WAYNE, STEINMETZ, LARS M · 2014 to 2018
$10.9M
MIRA: Enzymology and Self-Resistance of Natural Product BiosynthesisR35GM118056 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Yi Tang · 2016 to 2026
$6.1M
Stanford ChEM-H Chemistry/Biology Interface Predoctoral Training ProgramT32GM139791 · NIGMS · STANFORD UNIVERSITY · PI Carolyn Bertozzi, Christine Jacobs-Wagner · 2021 to 2026
$2.4M
NIGMS NIH HHS R35 GM118056NIGMS NIH HHS T32 GM139791NIGMS NIH HHS U01 GM110706
6 · The paper itself

Abstract

Oxidative cyclizations are important transformations that occur widely during natural product biosynthesis. The transformations from acyclic precursors to cyclized products can afford morphed scaffolds, structural rigidity, and biological activities. Some of the most dramatic structural alterations in natural product biosynthesis occur through oxidative cyclization. In this Review, we examine the different strategies used by nature to create new intra(inter)molecular bonds via redox chemistry. This Review will cover both oxidation- and reduction-enabled cyclization mechanisms, with an emphasis on the former. Radical cyclizations catalyzed by P450, nonheme iron, α-KG-dependent oxygenases, and radical SAM enzymes are discussed to illustrate the use of molecular oxygen and S-adenosylmethionine to forge new bonds at unactivated sites via one-electron manifolds. Nonradical cyclizations catalyzed by flavin-dependent monooxygenases and NAD(P)H-dependent reductases are covered to show the use of two-electron manifolds in initiating cyclization reactions. The oxidative installations of epoxides and halogens into acyclic scaffolds to drive subsequent cyclizations are separately discussed as examples of "disappearing" reactive handles. Last, oxidative rearrangement of rings systems, including contractions and expansions, will be covered.

Indexed as

Biological ProductsCyclizationEnzymesOxidation-ReductionBiological ProductsEnzymes

Identifiers

PMID27936626
PMCPMC5406274
OpenAlexW2562468815

What OpenQuestion holds

Textmetadata
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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.