Evidence map›Paper›PMID 26688791›Full record

ArticleCurrent opinion in insect science2015

Clip-domain serine proteases as immune factors in insect hemolymph.

Michael R Kanost, Haobo Jiang

Abstract read
In one paragraph

Article in Current opinion in insect science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
–field-weighted citation impact
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

126 citing papers in PubMed.

  1. Virulence · 2026
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  7. Transcriptional predictors of rescue behaviour in ants.The Journal of experimental biology · 2026
    Article
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  9. Partial reconstitution of the prophenoloxidase activation system inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. mbioRxiv : the preprint server for biology · 2026
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  19. The expanded immunoregulatory protease network in mosquitoes is governed by gene coexpression.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  20. Article

66 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

2 authors.

Michael R KanostDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506 USA.
Haobo JiangDepartment of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, 74078 USA.

Funding

Initiation and Regulation of Prophenoloxidase ActivationR01GM058634 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI JIANG, HAOBO · 1999 to 2022
$4.0M
Supplement 2 to promote diversity in health related res.: protease systems in insR37GM041247 · NIGMS · KANSAS STATE UNIVERSITY · PI KANOST, MICHAEL R · 2011 to 2020
$3.8M
SERINE PROTEINASE INHIBITORS IN INSECTSR01GM041247 · NIGMS · KANSAS STATE UNIVERSITY · PI KANOST, MICHAEL R · 1994 to 2010
$3.1M
NIGMS NIH HHS R01 GM041247NIGMS NIH HHS R01 GM058634NIGMS NIH HHS R37 GM041247
6 · The paper itself

Abstract

CLIP proteases are non-digestive serine proteases present in hemolymph of insects and other arthropods. They are composed of one or more amino-terminal clip domains followed by a linker sequence and a carboxyl-terminal S1A family serine protease domain. The genes for CLIP proteases have evolved as four clades (CLIPA, CLIPB, CLIPC, CLIPD), each present as multigene families in insect genomes. CLIP proteases in hemolymph function in innate immune responses. These include proteolytic activation of the cytokine Spätzle, to form an active Toll ligand leading to synthesis of antimicrobial peptides, and specific activation of prophenoloxidase, required for the melanization response. CLIP proteases act in cascade pathways. In the immune pathways that have been characterized, microbial surface molecules stimulate activation of an initiating modular serine protease, which then activates a CLIPC, which in turn activates a CLIPB. The active CLIPB then cleaves and activates an effector molecule (proSpätzle or prophenoloxidase). CLIPA proteins are pseudoproteases, lacking proteolytic activity, but some can function as regulators of the activity of other CLIP proteases and form high molecular weight immune complexes. A few three dimensional structures for CLIP proteases are now available for structure-function analysis of these immune factors, revealing structural features that may act in specific activation or in formation of immune complexes. The functions of most CLIP proteases are unknown, even in well studied insect species. It is very likely that additional proteins activated by CLIP proteases and acting in immunity remain to be discovered.

Identifiers

PMID26688791
PMCPMC4680995

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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.