Evidence map›Paper›PMID 11284715›Full record

ArticleThe Biochemical journal2001

Identification and characterization of a novel sucrose-non-fermenting protein kinase/AMP-activated protein kinase-related protein kinase, SNARK.

D L Lefebvre, Y Bai, N Shahmolky, M Sharma, R Poon, D J Drucker, C F Rosen

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. AMPK in skeletal muscle function and metabolism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. AMP kinase-related kinase NUAK2 affects tumor growth, migration, and clinical outcome of human melanoma.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Sucrose nonfermenting AMPK-related kinase (SNARK) mediates contraction-stimulated glucose transport in mouse skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  17. Article
  18. The Snf1-related kinase, Hunk, is essential for mammary tumor metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  19. Article
  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

7 authors at 2 institutions in 1 country.

D L LefebvreDepartment of Medicine, Division of Dermatology, Toronto General Hospital, Banting Institute, Room 317, 100 College Street, Toronto M5G 1L5, Ontario, Canada.
Y Bai
N Shahmolky
M Sharma
R Poon
D J Drucker
C F Rosen
Toronto General Hospital · CADiabetes Canada · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Subtraction hybridization after the exposure of keratinocytes to ultraviolet radiation identified a differentially expressed cDNA that encodes a protein of 630 amino acid residues possessing significant similarity to the catalytic domain of the sucrose-non-fermenting protein kinase (SNF1)/AMP-activated protein kinase (AMPK) family of serine/threonine protein kinases. Northern blotting and reverse-transcriptase-mediated PCR demonstrated that mRNA transcripts for the SNF1/AMPK-related kinase (SNARK) were widely expressed in rodent tissues. The SNARK gene was localized to human chromosome 1q32 by fluorescent in situ hybridization. SNARK was translated in vitro to yield a single protein band of approx. 76 kDa; Western analysis of transfected baby hamster kidney (BHK) cells detected two SNARK-immunoreactive bands of approx. 76-80 kDa. SNARK was capable of autophosphorylation in vitro; immunoprecipitated SNARK exhibited phosphotransferase activity with the synthetic peptide substrate HMRSAMSGLHLVKRR (SAMS) as a kinase substrate. SNARK activity was significantly increased by AMP and 5-amino-4-imidazolecarboxamide riboside (AICAriboside) in rat keratinocyte cells, implying that SNARK might be activated by an AMPK kinase-dependent pathway. Furthermore, glucose deprivation increased SNARK activity 3-fold in BHK fibroblasts. These findings identify SNARK as a glucose- and AICAriboside-regulated member of the AMPK-related gene family that represents a new candidate mediator of the cellular response to metabolic stress.

Indexed as

Hydrogen-Ion ConcentrationAdenosine MonophosphateAmino Acid SequenceAminoimidazole CarboxamideAnimalsBase SequenceCells, CulturedChromosome MappingCricetinaeDNA, ComplementaryEnzyme ActivationGlucoseHumansMolecular Sequence DataPhosphorylationPrecipitin TestsAdenosine MonophosphateAICA ribonucleotideAminoimidazole CarboxamideDNA, ComplementaryGlucoseNUAK2 protein, humanNuak2 protein, ratProtein Serine-Threonine KinasesRibonucleotidesRNA, Messenger

Identifiers

PMID11284715
PMCPMC1221739
OpenAlexW1967642818

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.