Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 363

The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.

Assembly mechanism of recombinant spider silk proteins

Open access
Rammensee, S., Slotta, U., Scheibel, T., Bausch, A. R.·2008·Proceedings of the National Academy of Sciences

Abstract

Spider silk threads are formed by the irreversible aggregation of silk proteins in a spinning duct with dimensions of only a few micrometers. Here, we present a microfluidic device in which engineered and recombinantly produced spider dragline silk proteins eADF3 (engineered Araneus diadematus fibroin) and eADF4 are assembled into fibers. Our approach allows the direct observation and identification of the essential parameters of dragline silk assembly. Changes in ionic conditions and pH result in aggregation of the two proteins. Assembly of eADF3 fibers was induced only in the presence of an elongational flow component. Strikingly, eADF4 formed fibers only in combination with eADF3. On the basis of these results, we propose a model for dragline silk aggregation and early steps of fiber assembly in the microscopic regime.

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 · 10.1073/pnas.0709246105

Cites

20 of 20 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

Show all 20 references

Cited by

See all 363

Metadata

Authors
Rammensee, S., Slotta, U., Scheibel, T., & Bausch, A. R.
Venue
Proceedings of the National Academy of Sciences
Published
2008-05-06
Volume
105
Issue
18
Pages
6590-6595
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2151881328
Cited by
363
References
20
FWCI
11.70
Type
journal article
Language
en
Open access
green

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: Assembly mechanism of recombinant spider silk proteins. https://app.cochat.ai/papers/10.1073/pnas.0709246105
The paper
Rammensee, S., Slotta, U., Scheibel, T., & Bausch, A. R. (2008). Assembly mechanism of recombinant spider silk proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0709246105

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.