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</script>pmid: 12121414
There is a complex network of protein–protein and protein–lipid interactions that underlie clathrin‐mediated vesicular traffic in all compartmentalized cells from yeast to man. Major progress has been made in the determination of the three‐dimensional structures of many of the components. Recently, there has been an explosion in the identification and characterization of clathrin binding partners. This review integrates the structural and biochemical information that is currently available to present a unified view of how many clathrin binding partners interact with clathrin.
Binding Sites, Sequence Homology, Amino Acid, Molecular Sequence Data, HSC70 Heat-Shock Proteins, Clathrin-Coated Vesicles, Models, Biological, Clathrin, Endocytosis, Protein Structure, Tertiary, Animals, Humans, HSP70 Heat-Shock Proteins, Amino Acid Sequence, Carrier Proteins
Binding Sites, Sequence Homology, Amino Acid, Molecular Sequence Data, HSC70 Heat-Shock Proteins, Clathrin-Coated Vesicles, Models, Biological, Clathrin, Endocytosis, Protein Structure, Tertiary, Animals, Humans, HSP70 Heat-Shock Proteins, Amino Acid Sequence, Carrier Proteins
| citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 99 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
