Evidence map›Paper›PMID 17940044›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote, Dictyostelium discoideum, with a role in cytokinesis.

Haiyu Zhang, María R Gómez-García, Xiaobing Shi, Narayana N Rao, Arthur Kornberg

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

34 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. The Protein Scaffolding Functions of Polyphosphate.Journal of molecular biology · 2024
    Review
  7. Starvation Induces Extracellular Accumulation of Polyphosphate inInternational journal of molecular sciences · 2023
    Article
  8. Review
  9. Did Cyclic Metaphosphates Have a Role in the Origin of Life?Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2021
    Review
  10. Article
  11. [A fluorometric method for direct detection of inorganic polyphosphate in enterohemorrhagicNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2019
    Article
  12. Review
  13. Polyphosphate granule biogenesis is temporally and functionally tied to cell cycle exit during starvation inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. Article
  15. Acidocalcisomes of eukaryotes.Current opinion in cell biology · 2016
    Review
  16. Polyphosphate and acidocalcisomes.Biochemical Society transactions · 2016
    Review
  17. Review
  18. Developmental accumulation of inorganic polyphosphate affects germination and energetic metabolism in Dictyostelium discoideum.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Review
  20. 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

5 authors at 1 institution in 1 country.

Haiyu ZhangDepartment of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.
María R Gómez-García
Xiaobing Shi
Narayana N Rao
Arthur Kornberg
Stanford University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyphosphate kinase 1 (PPK1), the principal enzyme responsible for reversible synthesis of polyphosphate (poly P) from the terminal phosphate of ATP, is highly conserved in bacteria and archaea. Dictyostelium discoideum, a social slime mold, is one of a few eukaryotes known to possess a PPK1 homolog (DdPPK1). Compared with PPK1 of Escherichia coli, DdPPK1 contains the conserved residues for ATP binding and autophosphorylation, but has an N-terminal extension of 370 aa, lacking homology with any known protein. Polyphosphate or ATP promote oligomerization of the enzyme in vitro. The DdPPK1 products are heterogeneous in chain length and shorter than those of E. coli. The unique DdPPK1 N-terminal domain was shown to be necessary for its enzymatic activity, cellular localization, and physiological functions. Mutants of DdPPK1, as previously reported, are defective in development, sporulation, and predation, and as shown here, in late stages of cytokinesis and cell division.

Indexed as

CytokinesisAdenosine TriphosphateAmino Acid SequenceAnimalsDictyosteliumEscherichia coli ProteinsGreen Fluorescent ProteinsMolecular Sequence DataMutationPhosphotransferases (Alcohol Group Acceptor)Phosphotransferases (Phosphate Group Acceptor)Protein Structure, TertiaryProtozoan ProteinsAdenosine TriphosphateEscherichia coli ProteinsGreen Fluorescent ProteinsPhosphotransferases (Alcohol Group Acceptor)Phosphotransferases (Phosphate Group Acceptor)polyphosphate kinasepolyphosphate kinase, E coliProtozoan Proteins

Identifiers

PMID17940044
PMCPMC2034253
OpenAlexW2123394717

What OpenQuestion holds

Textmetadata
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.