Evidence map›Paper›PMID 33894563›Full record

ArticleBiophysical chemistry2021

Mapping protein-protein interactions in homodimeric CYP102A1 by crosslinking and mass spectrometry.

Dana Felker, Haoming Zhang, Zhiyuan Bo, Miranda Lau, Yoshihiro Morishima, Santiago Schnell, Yoichi Osawa

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

7 authors.

Dana FelkerDepartment of Pharmacology, University of Michigan Medical School, 1301 MSRB III, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-5632, USA. Electronic address: dbfelker@umich.edu.
Haoming ZhangDepartment of Pharmacology, University of Michigan Medical School, 1301 MSRB III, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-5632, USA. Electronic address: haom@umich.edu.
Zhiyuan BoDepartment of Pharmacology, University of Michigan Medical School, 1301 MSRB III, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-5632, USA. Electronic address: zybo@umich.edu.
Miranda LauDepartment of Pharmacology, University of Michigan Medical School, 1301 MSRB III, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-5632, USA. Electronic address: laumiran@umich.edu.
Yoshihiro MorishimaDepartment of Pharmacology, University of Michigan Medical School, 1301 MSRB III, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-5632, USA. Electronic address: ymo@umich.edu.
Santiago SchnellDepartment of Molecular & Integrative Physiology, 7744 MS II, 1137 E. Catherine St., Ann Arbor, MI 48109-5622, USA. Electronic address: schnells@umich.edu.
Yoichi OsawaDepartment of Pharmacology, University of Michigan Medical School, 1301 MSRB III, 1150 W. Medical Center Dr., Ann Arbor, MI 48109-5632, USA. Electronic address: osawa@umich.edu.

Funding

ENVIRONMENTAL TOXICOLOGY PRE/POST DOCTORAL RES.TRAININGT32ES007062 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Justin Adam Colacino · 1985 to 2026
$10.5M
TSPO and Neuroinflammation in Alzheimer's DiseaseR01ES007062 · NIEHS · JOHNS HOPKINS UNIVERSITY · PI GUILARTE, TOMAS R · 1995 to 2023
$7.3M
P450 and NO Synthase Regulation by Multiprotein ComplexesR01GM077430 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OSAWA, YOICHI, ZHANG, HAOMING · 2006 to 2022
$6.5M
Mechanisms of motor neuron toxicity in Kennedy DiseaseR01NS055746 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LIEBERMAN, ANDREW P, OSAWA, YOICHI · 2007 to 2021
$6.0M
Structural basis for detoxification of environmental pollutants by native complexes of CYP2B family with its redox partnersR21ES030791 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SU, MIN, ZHANG, HAOMING · 2020 to 2021
$429k
NIEHS NIH HHS R01 ES007062NIEHS NIH HHS R21 ES030791NIEHS NIH HHS T32 ES007062NIGMS NIH HHS R01 GM077430NINDS NIH HHS R01 NS055746
6 · The paper itself

Abstract

Covalent crosslinking and mass spectrometry techniques hold great potential in the study of multiprotein complexes, but a major challenge is the inability to differentiate intra- and inter- protein crosslinks in homomeric complexes. In the current study we use CYP102A1, a well-characterized homodimeric P450, to examine a subtractive method that utilizes limited crosslinking with disuccinimidyl dibutyric urea (DSBU) and isolation of the monomer, in addition to the crosslinked dimer, to identify inter-monomer crosslinks. The utility of this approach was examined with the use of MS-cleavable crosslinker DSBU and recently published cryo-EM based structures of the CYP102A1 homodimer. Of the 31 unique crosslinks found, 26 could be fit to the reported structures whereas 5 exceeded the spatial constraints. Not only did these crosslinks validate the cryo-EM structure, they point to new conformations of CYP102A1 that bring the flavins in closer proximity to the heme.

Indexed as

Bacterial ProteinsCross-Linking ReagentsCytochrome P-450 Enzyme SystemMass SpectrometryModels, MolecularNADPH-Ferrihemoprotein ReductaseProtein BindingBacterial ProteinsCross-Linking ReagentsCytochrome P-450 Enzyme Systemflavocytochrome P450 BM3 monoxygenasesNADPH-Ferrihemoprotein ReductaseBM3CrosslinkingCXL-MSCYP102A1Mass spectrometryProtein-protein interactions

Identifiers

PMID33894563
PMCPMC8137598

What OpenQuestion holds

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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.