Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 1,191

The DOI matches its Crossref record.

Identification of a Ten-Amino Acid Proline-Rich SH3 Binding Site

Ren, Ruibao, Mayer, Bruce J., Cicchetti, Piera, Baltimore, David·1993·Science

Abstract

The Src homology 3 (SH3) region is a small protein domain present in a very large group of proteins, including cytoskeletal elements and signaling proteins. It is believed that SH3 domains serve as modules that mediate protein-protein associations and, along with Src homology 2 (SH2) domains, regulate cytoplasmic signaling. The SH3 binding sites of two SH3 binding proteins were localized to a nine- or ten-amino acid stretch very rich in proline residues. Similar SH3 binding motifs exist in the formins, proteins that function in pattern formation in embryonic limbs of the mouse, and one subtype of the muscarinic acetylcholine receptor. Identification of the SH3 binding site provides a basis for understanding the interaction between the SH3 domains and their targets.

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 · 10.1126/science.8438166

Cites

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

Cited by

See all 1,191

Metadata

Authors
Ren, R., Mayer, B. J., Cicchetti, P., & Baltimore, D.
Venue
Science
Published
1993-02-19
Volume
259
Issue
5098
Pages
1157-1161
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2085140159
Cited by
1,191
References
0
FWCI
56.08
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

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Identification of a Ten-Amino Acid Proline-Rich SH3 Binding Site. https://app.cochat.ai/papers/10.1126/science.8438166
The paper
Ren, R., Mayer, B. J., Cicchetti, P., & Baltimore, D. (1993). Identification of a Ten-Amino Acid Proline-Rich SH3 Binding Site. Science. https://doi.org/10.1126/science.8438166

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.