Evidence map›Paper›PMID 18477463›Full record

ArticleArchives of biochemistry and biophysics2008

Mutagenesis of the cysteine-rich clip domain in the Drosophila patterning protease, Snake.

Sufang Tian, Ellen K LeMosy

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
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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 at 2 institutions in 2 countries.

Sufang TianDepartment of Cellular Biology and Anatomy, Medical College of Georgia, 1120 15th Street, CB1101, Augusta, GA 30912, USA.
Ellen K LeMosy
Augusta University · USWuhan University · CN

Funding

Spatial Control of Proteolysis in Dorsoventral PolarityR01GM067738 · NIGMS · MEDICAL COLLEGE OF GEORGIA (MCG) · PI LEMOSY, ELLEN K · 2004 to 2009
$1.4M
NIGMS NIH HHS R01 GM067738
6 · The paper itself

Abstract

A common motif found in invertebrate serine proteases involved in immunity and development is the clip domain, proposed to regulate catalytic activity or protein-protein interactions within proteolytic cascades. Snake functions in a cascade that patterns the Drosophila embryo, and provides an accessible model for exploring the structural requirements for clip domain function. We tested Snake zymogens bearing charged-to-alanine mutations in the clip domain for their ability to rescue embryos lacking endogenous Snake and for their interactions by S2 cell co-transfection with upstream Gastrulation Defective and downstream Easter in the protease cascade. Of 13 single and multiple substitutions, one double mutant in a predicted protruding region exhibited a severe defect in embryonic rescue but showed only minimal defects in the co-transfection assay. We discuss implications of these and other results for potential biological roles of the Snake clip domain and for use of the in vitro assay in predicting protease behavior.

Indexed as

MutagenesisAlanineAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionAnimalsCatalysisCatalytic DomainCysteineDrosophilaDrosophila ProteinsEmbryo, NonmammalianMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryRNA, MessengerAlanineCysteineDrosophila ProteinsRNA, MessengerSerine Endopeptidasessnk protein, Drosophila

Identifiers

PMID18477463
PMCPMC2518291
OpenAlexW2020882421

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.