Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 334

The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.

HtrA1 serine protease inhibits signaling mediated by Tgfβ family proteins

Oka, Chio, Tsujimoto, Rumi, Kajikawa, Miwa, Koshiba-Takeuchi, Kazuko, Ina, Junko, Yano, Masato, Tsuchiya, Akiho, Ueta, Yoshihumi, Soma, Akinobu, Kanda, Hidenobu, Matsumoto, Michio, Kawaichi, Masashi·2004·Development
DOI 10.1242/dev.00999
Open this paper in CoChat — free account

Abstract

HtrA1, a member of the mammalian HtrA serine protease family, has a highly conserved protease domain followed by a PDZ domain. Because HtrA1 is a secretory protein and has another functional domain with homology to follistatin, we examined whether HtrA1 functions as an antagonist of Tgfβfamily proteins. During embryo development, mouse HtrA1 was expressed in specific areas where signaling by Tgfβ family proteins plays important regulatory roles. The GST-pulldown assay showed that HtrA1 binds to a broad range of Tgfβ family proteins, including Bmp4, Gdf5, Tgfβs and activin. HtrA1 inhibited signaling by Bmp4, Bmp2, and Tgfβ1 in C2C12 cells, presumably by preventing receptor activation. Experiments using a series of deletion mutants indicated that the binding activity of HtrA1 required the protease domain and a small linker region preceding it, and that inhibition of Tgfβ signaling is dependent on the proteolytic activity of HtrA1. Misexpression of HtrA1 near the developing chick eye led to suppression of eye development that was indistinguishable from the effects of noggin. Taken together, these data indicate that HtrA1 protease is a novel inhibitor of Tgfβ family members.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1242/dev.00999

Cites

52 of 52 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Cited by

See all 334

Metadata

Authors
Oka, C., Tsujimoto, R., Kajikawa, M., Koshiba-Takeuchi, K., Ina, J., Yano, M., Tsuchiya, A., Ueta, Y., Soma, A., Kanda, H., Matsumoto, M., & Kawaichi, M.
Venue
Development
Publisher
The Company of Biologists
Published
2004-03-01
Volume
131
Issue
5
Pages
1041-1053
ISSN
  • 0950-1991 (ISSN-L)
  • 1477-9129
DOI
10.1242/dev.00999
OpenAlex
W2078222204
Cited by
334
References
52
FWCI
3.50
Type
journal article
Language
en
Open access
closed

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.