
pmid: 15469831
Three "endosomal sorting complexes required for transport," ESCRT-I, -II, and -III, mediate sorting of ubiquitinated membrane proteins into intraluminal endosomal vesicles that are destined for degradation in lysosomes. Two recent reports, one in Nature and one in this issue of Developmental Cell, reveal the crystal structure of the yeast form of ESCRT-II.
Models, Molecular, Membranes, Saccharomyces cerevisiae Proteins, Endosomal Sorting Complexes Required for Transport, Ubiquitin, Vesicular Transport Proteins, Membrane Proteins, Zinc Fingers, Endosomes, Saccharomyces cerevisiae, Crystallography, X-Ray, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Transport, Liposomes, Amino Acid Sequence, Carrier Proteins, Dimerization, Ubiquitins, Developmental Biology
Models, Molecular, Membranes, Saccharomyces cerevisiae Proteins, Endosomal Sorting Complexes Required for Transport, Ubiquitin, Vesicular Transport Proteins, Membrane Proteins, Zinc Fingers, Endosomes, Saccharomyces cerevisiae, Crystallography, X-Ray, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Transport, Liposomes, Amino Acid Sequence, Carrier Proteins, Dimerization, Ubiquitins, Developmental Biology
| selected citations These citations are derived from selected sources. 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). | 14 | |
| 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. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
