Evidence map›Paper›PMID 8761444›Full record

ReviewThe Biochemical journal1996

The lipocalin protein family: structure and function.

D R Flower

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 512 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
512citing papers in PubMed, 1 pooled it
16.2field-weighted citation impact, top 1% 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

512 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,681 citations in OpenAlex.

  1. Pooled it
  2. Lipocalin 13 Mitigates Metabolic Dysfunction-Associated Steatotic Liver Disease Through Inhibiting the ADRB2/ERK Signalling Pathway.Liver international : official journal of the International Association for the Study of the Liver · 2026
    Article
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  7. Non-transferrin-bound iron uptake by cardiomyocytes.Journal of molecular medicine (Berlin, Germany) · 2026
    Review
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  16. Plant signaling & behavior · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. Dark Matter Carried byInternational journal of molecular sciences · 2025
    Article

452 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

D R FlowerDepartment of Physical Chemistry and BioAnalysis, Astra Charnwood, Loughborough, Leics, U.K.
Loughborough University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lipocalin protein family is a large group of small extracellular proteins. The family demonstrates great diversity at the sequence level; however, most lipocalins share three characteristic conserved sequence motifs, the kernel lipocalins, while a group of more divergent family members, the outlier lipocalins, share only one. Belying this sequence dissimilarity, lipocalin crystal structures are highly conserved and comprise a single eight-stranded continuously hydrogen-bonded antiparallel beta-barrel, which encloses an internal ligand-binding site. Together with two other families of ligand-binding proteins, the fatty-acid-binding proteins (FABPs) and the avidins, the lipocalins form part of an overall structural superfamily: the calycins. Members of the lipocalin family are characterized by several common molecular-recognition properties: the ability to bind a range of small hydrophobic molecules, binding to specific cell-surface receptors and the formation of complexes with soluble macromolecules. The varied biological functions of the lipocalins are mediated by one or more of these properties. In the past, the lipocalins have been classified as transport proteins; however, it is now clear that the lipocalins exhibit great functional diversity, with roles in retinol transport, invertebrate cryptic coloration, olfaction and pheromone transport, and prostaglandin synthesis. The lipocalins have also been implicated in the regulation of cell homoeostasis and the modulation of the immune response, and, as carrier proteins, to act in the general clearance of endogenous and exogenous compounds.

Indexed as

Neoplasm ProteinsAdjuvants, ImmunologicAmino Acid SequenceAvidinCarrier ProteinsFatty Acid-Binding ProteinsLigandsModels, MolecularMolecular Sequence DataMyelin P2 ProteinPheromonesProtein BindingProteinsReceptors, Cell SurfaceSmellAdjuvants, ImmunologicAvidinCarrier ProteinsFatty Acid-Binding ProteinsLigandsMyelin P2 ProteinNeoplasm ProteinsPheromonesProteinsReceptors, Cell Surface

Identifiers

PMID8761444
PMCPMC1217580
OpenAlexW2040141270

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.