Evidence map›Paper›PMID 31495713›Full record

ArticleCell chemical biology2019

Light Regulation of Enzyme Allostery through Photo-responsive Unnatural Amino Acids.

Andrea C Kneuttinger, Kristina Straub, Philipp Bittner, Nadja A Simeth, Astrid Bruckmann, Florian Busch, Chitra Rajendran, Enrico Hupfeld, Vicki H Wysocki, Dominik Horinek and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 2 institutions in 3 countries.

Andrea C KneuttingerInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Kristina StraubInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Philipp BittnerInstitute of Organic Chemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Nadja A SimethInstitute of Organic Chemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany; Centre for Systems Chemistry, Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 4, 9747 AG Groningen, the Netherlands.
Astrid BruckmannInstitute of Biochemistry, Genetics and Microbiology, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Florian BuschDepartment of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA.
Chitra RajendranInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Enrico HupfeldInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Vicki H WysockiDepartment of Chemistry and Biochemistry and Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA.
Dominik HorinekInstitute of Physical and Theoretical Chemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Burkhard KönigInstitute of Organic Chemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Rainer MerklInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany.
Reinhard SternerInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany. Electronic address: reinhard.sterner@ur.de.
University of Regensburg · DEThe Ohio State University · US

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI SOMOGYI, ARPAD · 2018 to 2022
$7.6M
NIGMS NIH HHS P41 GM128577
6 · The paper itself

Abstract

Imidazole glycerol phosphate synthase (ImGPS) is an allosteric bienzyme complex in which substrate binding to the synthase subunit HisF stimulates the glutaminase subunit HisH. To control this stimulation with light, we have incorporated the photo-responsive unnatural amino acids phenylalanine-4'-azobenzene (AzoF), o-nitropiperonyl-O-tyrosine (NPY), and methyl-o-nitropiperonyllysine (mNPK) at strategic positions of HisF. The light-mediated isomerization of AzoF at position 55 (fS55AzoF

Indexed as

LightAllosteric RegulationAllosteric SiteAmino AcidsAminohydrolasesGlutamineIsomerismKineticsMolecular Dynamics SimulationProtein SubunitsAmino AcidsAminohydrolasesGlutamineimidazole glycerol phosphate synthaseProtein Subunitsallosteryenzyme catalysisphoto-controlprotein designsynthetic biologyunnatural amino acids

Identifiers

PMID31495713
PMCPMC7293202
OpenAlexW2972077284

What OpenQuestion holds

Textmetadata
LicenceTDM
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.