Investigation of Protein–Protein Interactions within Flagellar Dynein Using Homobifunctional and Zero-Length Crosslinking Reagents
- 31 December 2000
- Vol. 22 (4), 365-371
- https://doi.org/10.1006/meth.2000.1088
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Cytoplasmic Dynein Contains a Family of Differentially Expressed Light ChainsBiochemistry, 1998
- Brain Cytoplasmic and Flagellar Outer Arm Dyneins Share a Highly Conserved Mr 8,000 Light ChainPublished by Elsevier ,1996
- Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles.The Journal of cell biology, 1996
- Differential Expression and Phosphorylation of the 74-kDa Intermediate Chains of Cytoplasmic Dynein in Cultured Neurons and GliaJournal of Biological Chemistry, 1996
- Affinity Chromatography Demonstrates a Direct Binding between Cytoplasmic Dynein and the Dynactin ComplexJournal of Biological Chemistry, 1995
- The 78,000-M(r) intermediate chain of Chlamydomonas outer arm dynein is a microtubule-binding protein.The Journal of cell biology, 1995
- Cell and Molecular Biology of Flagellar DyneinsInternational Review of Cytology, 1994
- The substructure of isolated and in situ outer dynein arms of sea urchin sperm flagella.The Journal of cell biology, 1985
- Structure and molecular weight of the dynein ATPaseThe Journal of cell biology, 1983
- Purification and polypeptide composition of dynein ATPases from chlamydomonas flagellaCell Motility, 1982