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clathrin coat

Known as: clathrin cage 
A membrane coat found on coated pits and some coated vesicles; consists of polymerized clathrin triskelions, each comprising three clathrin heavy… 
National Institutes of Health

Related topics

Related topics

3 relations

Narrower (2)

clathrin adaptor complexclathrin complex

Broader (1)

postsynaptic endocytic zone

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2005
Review
2005
Fusion pore regulation of transmitter release
Review
2002
Review
2002
Dimerization, ubiquitylation and endocytosis go together in growth hormone receptor function
2002
2002
HIP 1 and HIP 12 Display Differential Binding to F-actin , AP 2 , and Clathrin
Huntingtin-interacting protein 1 (HIP1) and HIP12 are orthologues of Sla2p, a yeast protein with essential functions in… 
2001
2001
Interactions between Adaptor Protein-1 of the Clathrin Coat and Microtubules via Type 1a Microtubule-associated Proteins*
The classical view suggests that adaptor proteins of the clathrin coat mediate the sorting of cargo protein passengers into… 
2000
2000
Purification of clathrin assembly protein from rat liver
Recently, the gene encoding clathrin assembly protein of lymphoid myeloid leukemia (CALM), which is homologous to the AP180, was… 
1994
1994
Post-embedding immunocytochemistry for adhesive proteins and clathrin in LR White- and LR Gold-embedded human platelets.
1991
1991
Fluid phase endocytosis investigated by fluorescence with trimethylamino‐diphenylhexatriene in L929 cells; the influence of temperature and of cytoskeleton depolymerizing drugs
1986
1986
Lipid bilayer dynamics in plasma and coated vesicle membranes from bovine adrenal cortex. Evidence of two types of coated vesicle involved in the LDL receptor traffic.
Highly Cited
1983
Highly Cited
1983
Fusion of coated vesicles with lysosomes: Measurement with a fluorescence assay
1981
1981
Involvement of smooth and coated vesicles in the function of the contractile vacuole complex of some cryptophycean flagellates.
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