Evidence map›Paper›PMID 19875079›Full record

ArticleChemistry & biology2009

Hemoglobin digestion in blood-feeding ticks: mapping a multipeptidase pathway by functional proteomics.

Martin Horn, Martina Nussbaumerová, Miloslav Sanda, Zuzana Kovárová, Jindrich Srba, Zdenek Franta, Daniel Sojka, Matthew Bogyo, Conor R Caffrey, Petr Kopácek and 1 more

Open access · greenAbstract read
In one paragraph

Article in Chemistry & biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

85 citing papers in PubMed, 201 citations in OpenAlex.

  1. Article
  2. Article
  3. FirstCurrent research in parasitology & vector-borne diseases · 2026
    Article
  4. Exploring Spiders Without Venom as New Sources of Peptidase Inhibitors.International journal of molecular sciences · 2025
    Article
  5. Article
  6. Egg Protein Compositions over Embryonic Development inAnimals : an open access journal from MDPI · 2024
    Article
  7. Article
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  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

25 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

11 authors at 5 institutions in 3 countries.

Martin HornInstitute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 16610 Praha, Czech Republic.
Martina Nussbaumerová
Miloslav Sanda
Zuzana Kovárová
Jindrich Srba
Zdenek Franta
Daniel Sojka
Matthew Bogyo
Conor R Caffrey
Petr Kopácek
Michael Mares
Czech Academy of Sciences · CZUniversity of South Bohemia in České Budějovice · CZCharles University · CZQB3 · USStanford University · US

Funding

CORE 6 : PROJECT LEADERSHIP AND ADMINISTRATIONU54RR020843 · NCRR · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI SMITH, JEFFREY W · 2004 to 2009
$19.1M
Small Molecule Imaging of Protease ActivityR01EB005011 · NIBIB · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2005 to 2013
$3.0M
NCRR NIH HHS U54 RR020843NCRR NIH HHS U54-RR020843NIBIB NIH HHS R01 EB005011
6 · The paper itself

Abstract

Hemoglobin digestion is an essential process for blood-feeding parasites. Using chemical tools, we deconvoluted the intracellular hemoglobinolytic cascade in the tick Ixodes ricinus, a vector of Lyme disease and tick-borne encephalitis. In tick gut tissue, a network of peptidases was demonstrated through imaging with specific activity-based probes and activity profiling with peptidic substrates and inhibitors. This peptidase network is induced upon blood feeding and degrades hemoglobin at acidic pH. Selective inhibitors were applied to dissect the roles of the individual peptidases and to determine the peptidase-specific cleavage map of the hemoglobin molecule. The degradation pathway is initiated by endopeptidases of aspartic and cysteine class (cathepsin D supported by cathepsin L and legumain) and is continued by cysteine amino- and carboxy-dipeptidases (cathepsins C and B). The identified enzymes are potential targets to developing novel anti-tick vaccines.

Indexed as

Amino Acid SequenceAnimalsAsparaginyl EndopeptidaseCatalytic DomainCathepsin BCathepsin CCathepsin DCathepsin LCysteine EndopeptidasesEndopeptidasesEnzyme InhibitorsHemoglobinsHydrogen-Ion ConcentrationIxodesMolecular Sequence DataProteomicsAsparaginyl EndopeptidaseCathepsin BCathepsin CCathepsin DCathepsin LCysteine EndopeptidasesEndopeptidasesEnzyme InhibitorsHemoglobins

Identifiers

PMID19875079
PMCPMC2801564
OpenAlexW2063800518

What OpenQuestion holds

Textmetadata
LicenceTDM
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.