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Cited by 198

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Binding of laminin to type IV collagen: a morphological study.

Open access
Charonis, A S, Tsilibary, E C, Yurchenco, P D, Furthmayr, H·1985·The Journal of cell biology

Abstract

A mixture of laminin and type IV collagen was analyzed by rotary shadowing using carbon/platinum and electron microscopy. Laminin was found to form distinct complexes with type IV collagen: one site of interaction is located 140 nm from the COOH-terminal, noncollagenous (NC1) domain and the other is located within the NH2-terminal region. The isolated NC1 fragment of type IV collagen does not appear to interact with laminin, while pepsin-treated type IV collagen, which lacks the NC1 domain, retains its ability to form complexes with laminin. Analysis of the laminin-type IV complexes indicates that laminin binds to type IV collagen via the globular regions of either of its four arms. This finding is supported by experiments using fragment P1 of laminin which lacks the globular regions and which does not bind to type IV collagen in a specific way. In addition, after heat-denaturation of laminin no specific binding is observed.

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Metadata

Authors
Charonis, A. S., Tsilibary, E. C., Yurchenco, P. D., & Furthmayr, H.
Venue
The Journal of cell biology
Published
1985-06-01
Volume
100
Issue
6
Pages
1848-1853
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2000236517
Cited by
198
References
1
FWCI
9.53
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Binding of laminin to type IV collagen: a morphological study. https://app.cochat.ai/papers/10.1083/jcb.100.6.1848
The paper
Charonis, A. S., Tsilibary, E. C., Yurchenco, P. D., & Furthmayr, H. (1985). Binding of laminin to type IV collagen: a morphological study. The Journal of cell biology. https://doi.org/10.1083/jcb.100.6.1848

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

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