Evidence map›Paper›PMID 33893105›Full record

ArticleScience advances2021

Multiple substrate recognition by yeast diadenosine and diphosphoinositol polyphosphate phosphohydrolase through phosphate clamping.

María Ángeles Márquez-Moñino, Raquel Ortega-García, Megan L Shipton, Elsa Franco-Echevarría, Andrew M Riley, Julia Sanz-Aparicio, Barry V L Potter, Beatriz González

Abstract read
In one paragraph

Article in Science advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Review
  2. Review
  3. The Diphosphoinositol Polyphosphate Phosphohydrolase 1 family binds IPInternational journal of biological macromolecules · 2026
    Article
  4. Review
  5. ApaH decaps NpNature chemical biology · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Fluorination Influences the Bioisostery of Myo-Inositol Pyrophosphate Analogs.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  16. Article
  17. Article
  18. 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.

María Ángeles Márquez-MoñinoDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.ORCID 0000-0003-4177-9359
Raquel Ortega-GarcíaDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Megan L ShiptonDrug Discovery and Medicinal Chemistry, Department of Pharmacology, University of Oxford Mansfield Road, Oxford OX1 3QT, UK.ORCID 0000-0002-9982-0927
Elsa Franco-EchevarríaDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.ORCID 0000-0001-7306-6594
Andrew M RileyDrug Discovery and Medicinal Chemistry, Department of Pharmacology, University of Oxford Mansfield Road, Oxford OX1 3QT, UK.ORCID 0000-0001-9003-3540
Julia Sanz-AparicioDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
Barry V L PotterDrug Discovery and Medicinal Chemistry, Department of Pharmacology, University of Oxford Mansfield Road, Oxford OX1 3QT, UK.ORCID 0000-0003-3255-9135
Beatriz GonzálezDepartment of Crystallography and Structural Biology, Institute of Physical-Chemistry Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain. xbeatriz@iqfr.csic.es.ORCID 0000-0002-0710-0202

Funding

Wellcome Trust
6 · The paper itself

Abstract

The yeast diadenosine and diphosphoinositol polyphosphate phosphohydrolase DDP1 is a Nudix enzyme with pyrophosphatase activity on diphosphoinositides, dinucleotides, and polyphosphates. These substrates bind to diverse protein targets and participate in signaling and metabolism, being essential for energy and phosphate homeostasis, ATPase pump regulation, or protein phosphorylation. An exhaustive structural study of DDP1 in complex with multiple ligands related to its three diverse substrate classes is reported. This allowed full characterization of the DDP1 active site depicting the molecular basis for endowing multisubstrate abilities to a Nudix enzyme, driven by phosphate anchoring following a defined path. This study, combined with multiple enzyme variants, reveals the different substrate binding modes, preferences, and selection. Our findings expand current knowledge on this important structural superfamily with implications extending beyond inositide research. This work represents a valuable tool for inhibitor/substrate design for

Identifiers

PMID33893105
PMCPMC8064635

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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.