The ADF homology (ADF-H) domain: a highly exploited actin-binding module.
Lappalainen
P
P
Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202, USA.
Kessels
M M
MM
Cope
M J
MJ
Drubin
D G
DG
D051339:Actin Depolymerizing Factors; D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D019143:Evolution, Molecular; D005658:Fungi / Q000235:genetics; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry; D010802:Phylogeny; D017433:Protein Structure, Secondary; D011505:Protein-Tyrosine Kinases; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014714:Vertebrates / Q000235:genetics
D051339:Actin Depolymerizing Factors; D000199:Actins; D008840:Microfilament Proteins; D009479:Neuropeptides; D029701:Saccharomyces cerevisiae Proteins; C113980:TWF1 protein, S cerevisiae; C485188:TWF1 protein, human; C053386:drebrins; D011505:Protein-Tyrosine Kinases