Evidence map›Paper›PMID 10318917›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Interaction of rat hormone-sensitive lipase with adipocyte lipid-binding protein.

W J Shen, K Sridhar, D A Bernlohr, F B Kraemer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 197 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. An Overview of Hormone-Sensitive Lipase (HSL).TheScientificWorldJournal · 2022
    Review
  12. Article
  13. A-FABP in Metabolic Diseases and the Therapeutic Implications: An Update.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review
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

4 authors at 3 institutions in 1 country.

W J ShenDivision of Endocrinology, Department of Medicine, Stanford University, Stanford, CA 94305-5103, USA.
K Sridhar
D A Bernlohr
F B Kraemer
Stanford University · USUniversity of Minnesota · USVA Palo Alto Health Care System · US

Funding

Diabetes, Endocrinology and Metabolism Training GrantT32DK007217 · NIDDK · STANFORD UNIVERSITY · PI Justin Pierce Annes, David Matthew Maahs · 1987 to 2026
$7.2M
REGULATION OF HORMONE SENSITIVE LIPASER01DK046942 · NIDDK · STANFORD UNIVERSITY · PI KRAEMER, FREDRIC B. · 1995 to 2003
$742k
REGULATION OF CHOLESTEROL ESTERASE IN STEROIDOGENESISR01DK049705 · NIDDK · STANFORD UNIVERSITY · PI KRAEMER, FREDRIC B. · 1996 to 1999
–
NIDDK NIH HHS DK 07217NIDDK NIH HHS DK 46942NIDDK NIH HHS DK 49705NIDDK NIH HHS R01 DK046942NIDDK NIH HHS T32 DK007217
6 · The paper itself

Abstract

Hormone-sensitive lipase (HSL) is a cytosolic neutral lipase that functions as the rate-limiting enzyme for the mobilization of free fatty acids in adipose tissue. By using the yeast two-hybrid system to examine the potential interaction of HSL with other cellular proteins, evidence is provided to demonstrate a direct interaction of HSL with adipocyte lipid-binding protein (ALBP), a member of the family of intracellular lipid-binding proteins that binds fatty acids, retinoids, and other hydrophobic ligands. The interaction was demonstrated in vitro by the binding of ALBP to HSL translated in vitro, to HSL in extracts of HSL overexpressing Chinese hamster ovary (CHO) cells, and to HSL in extracts of rat adipose tissue. Finally, the presence of ALBP was documented in immune complexes from rat adipose tissue immunoprecipitated with anti-HSL antibodies. The HSL-ALBP interaction was mapped to an N-terminal 300-aa region of HSL that is distinct from the C-terminal catalytic domain. These results suggest that HSL-derived fatty acids are bound by ALBP to facilitate intracellular trafficking of hydrophobic lipids.

Indexed as

Neoplasm ProteinsNerve Tissue ProteinsAmino Acid SequenceAnimalsCarrier ProteinsCHO CellsCricetinaeFatty Acid-Binding Protein 7Fatty Acid-Binding ProteinsFatty AcidsMolecular Sequence DataMutationMyelin P2 ProteinPrecipitin TestsProtein BindingProtein Structure, SecondaryCarrier ProteinsFABP4 protein, ratFabp7 protein, ratFatty Acid-Binding Protein 7Fatty Acid-Binding ProteinsFatty AcidsMyelin P2 ProteinNeoplasm ProteinsNerve Tissue ProteinsRecombinant ProteinsSterol Esterase

Identifiers

PMID10318917
PMCPMC21893
OpenAlexW1973862154

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.