PMID- 11911874
OWN - NLM
STAT- MEDLINE
DCOM- 20020507
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 513
IP  - 1
DP  - 2002 Feb 20
TI  - The ENTH domain.
PG  - 11-8
AB  - The epsin NH2-terminal homology (ENTH) domain is a membrane interacting module 
      composed by a superhelix of alpha-helices. It is present at the NH2-terminus of 
      proteins that often contain consensus sequences for binding to clathrin coat 
      components and their accessory factors, and therefore function as endocytic 
      adaptors. ENTH domain containing proteins have additional roles in signaling and 
      actin regulation and may have yet other actions in the nucleus. The ENTH domain 
      is structurally similar to the VHS domain. These domains define two families of 
      adaptor proteins which function in membrane traffic and whose interaction with 
      membranes is regulated, in part, by phosphoinositides.
FAU - De Camilli, Pietro
AU  - De Camilli P
AD  - Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, 
      CT 06510, USA. pietro.decamilli@yale.edu
FAU - Chen, Hong
AU  - Chen H
FAU - Hyman, Joel
AU  - Hyman J
FAU - Panepucci, Ezequiel
AU  - Panepucci E
FAU - Bateman, Alex
AU  - Bateman A
FAU - Brunger, Axel T
AU  - Brunger AT
LA  - eng
PT  - Journal Article
PT  - Review
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Membrane Proteins)
RN  - 0 (Ubiquitin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Consensus Sequence
MH  - Membrane Proteins/*chemistry
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Ubiquitin/chemistry
RF  - 81
EDAT- 2002/03/26 10:00
MHDA- 2002/05/08 10:01
CRDT- 2002/03/26 10:00
PHST- 2002/03/26 10:00 [pubmed]
PHST- 2002/05/08 10:01 [medline]
PHST- 2002/03/26 10:00 [entrez]
AID - S0014579301033063 [pii]
AID - 10.1016/s0014-5793(01)03306-3 [doi]
PST - ppublish
SO  - FEBS Lett. 2002 Feb 20;513(1):11-8. doi: 10.1016/s0014-5793(01)03306-3.