The Stability of the Nuclear Lamina Polymer Changes with the Composition of Lamin Subtypes According to Their Individual Binding Strengths
Open Access
- 1 October 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (41) , 42811-42817
- https://doi.org/10.1074/jbc.m407705200
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- Neutrophil Extracellular Traps Kill BacteriaScience, 2004
- The quest for the function of simple epithelial keratinsBioEssays, 2003
- Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger–Huët anomaly)Nature Genetics, 2002
- Structure of the Globular Tail of Nuclear LaminJournal of Biological Chemistry, 2002
- Nuclear Envelope and Chromatin Compositional Differences Comparing Undifferentiated and Retinoic Acid- and Phorbol Ester-Treated HL-60 CellsExperimental Cell Research, 2001
- Tenascin-C Hexabrachion Assembly Is a Sequential Two-step Process Initiated by Coiled-coil α-HelicesJournal of Biological Chemistry, 1998
- Intermediate Filament Protein Polymerization: Molecular Analysis ofDrosophilaNuclear Lamin Head-to-Tail BindingJournal of Structural Biology, 1996
- S‐Phase phosphorylation of lamin B2FEBS Letters, 1995
- The role of the head and tail domain in lamin structure and assembly: Analysis of bacterially expressed chicken Lamin A and truncated B2 laminsJournal of Structural Biology, 1992
- Expression of chicken lamin B2 in Escherichia coli: characterization of its structure, assembly, and molecular interactions.The Journal of cell biology, 1991