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Cited by 252

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Lamin-binding Proteins

Open access
Wilson, K. L., Foisner, R.·2010·Cold Spring Harbor Perspectives in Biology

Abstract

A- and B-type lamins are the major intermediate filaments of the nucleus. Lamins engage in a plethora of stable and transient interactions, near the inner nuclear membrane and throughout the nucleus. Lamin-binding proteins serve an amazingly diverse range of functions. Numerous inner-membrane proteins help anchor lamin filaments to the nuclear envelope, serving as part of the nuclear "lamina" network that is essential for nuclear architecture and integrity. Certain lamin-binding proteins of the inner membrane bind partners in the outer membrane and mechanically link lamins to the cytoskeleton. Inside the nucleus, lamin-binding proteins appear to serve as the "adaptors" by which the lamina organizes chromatin, influences gene expression and epigenetic regulation, and modulates signaling pathways. Transient interactions of lamins with key components of the transcription and replication machinery may provide an additional level of regulation or support to these essential events.

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Metadata

Authors
Wilson, K. L., & Foisner, R.
Venue
Cold Spring Harbor Perspectives in Biology
Published
2010-02-17
Volume
2
Issue
4
Pages
a000554-a000554
ISSN
1943-0264 (ISSN-L)
OpenAlex
W2153605484
Cited by
252
References
3
Type
posted content
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Lamin-binding Proteins. https://app.cochat.ai/papers/10.1101/cshperspect.a000554
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Wilson, K. L., & Foisner, R. (2010). Lamin-binding Proteins. Cold Spring Harbor Perspectives in Biology. https://doi.org/10.1101/cshperspect.a000554

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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.