112 related articles for article (PubMed ID: 9651317)
1. A membrane setting for the sorting motifs present in the adenovirus E3-13.7 protein which down-regulates the epidermal growth factor receptor.
Vinogradova O; Carlin C; Sonnichsen FD; Sanders CR
J Biol Chem; 1998 Jul; 273(28):17343-50. PubMed ID: 9651317
[TBL] [Abstract][Full Text] [Related]
2. Two distinct transport motifs in the adenovirus E3/10.4-14.5 proteins act in concert to down-modulate apoptosis receptors and the epidermal growth factor receptor.
Hilgendorf A; Lindberg J; Ruzsics Z; Höning S; Elsing A; Löfqvist M; Engelmann H; Burgert HG
J Biol Chem; 2003 Dec; 278(51):51872-84. PubMed ID: 14506242
[TBL] [Abstract][Full Text] [Related]
3. Adenovirus RIDbeta subunit contains a tyrosine residue that is critical for RID-mediated receptor internalization and inhibition of Fas- and TRAIL-induced apoptosis.
Lichtenstein DL; Krajcsi P; Esteban DJ; Tollefson AE; Wold WS
J Virol; 2002 Nov; 76(22):11329-42. PubMed ID: 12388693
[TBL] [Abstract][Full Text] [Related]
4. Aqueous and micelle-bound structural characterization of the epidermal growth factor receptor juxtamembrane domain containing basolateral sorting motifs.
Choowongkomon K; Hobert ME; He C; Carlin CR; Sonnichsen FD
J Biomol Struct Dyn; 2004 Jun; 21(6):813-26. PubMed ID: 15107003
[TBL] [Abstract][Full Text] [Related]
5. Adenovirus E3 protein causes constitutively internalized epidermal growth factor receptors to accumulate in a prelysosomal compartment, resulting in enhanced degradation.
Hoffman P; Carlin C
Mol Cell Biol; 1994 Jun; 14(6):3695-706. PubMed ID: 8196613
[TBL] [Abstract][Full Text] [Related]
6. E3-13.7 integral membrane proteins encoded by human adenoviruses alter epidermal growth factor receptor trafficking by interacting directly with receptors in early endosomes.
Crooks D; Kil SJ; McCaffery JM; Carlin C
Mol Biol Cell; 2000 Oct; 11(10):3559-72. PubMed ID: 11029055
[TBL] [Abstract][Full Text] [Related]
7. Structurally related class I and class II receptor protein tyrosine kinases are down-regulated by the same E3 protein coded for by human group C adenoviruses.
Kuivinen E; Hoffman BL; Hoffman PA; Carlin CR
J Cell Biol; 1993 Mar; 120(5):1271-9. PubMed ID: 8094718
[TBL] [Abstract][Full Text] [Related]
8. Distinct domains in the adenovirus E3 RIDalpha protein are required for degradation of Fas and the epidermal growth factor receptor.
Zanardi TA; Yei S; Lichtenstein DL; Tollefson AE; Wold WS
J Virol; 2003 Nov; 77(21):11685-96. PubMed ID: 14557654
[TBL] [Abstract][Full Text] [Related]
9. A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor.
Choowongkomon K; Carlin CR; Sönnichsen FD
J Biol Chem; 2005 Jun; 280(25):24043-52. PubMed ID: 15840573
[TBL] [Abstract][Full Text] [Related]
10. Structural characterization and topology of the second potential membrane anchor region in the thromboxane A2 synthase amino-terminal domain.
Ruan KH; Li D; Ji J; Lin YZ; Gao X
Biochemistry; 1998 Jan; 37(3):822-30. PubMed ID: 9454571
[TBL] [Abstract][Full Text] [Related]
11. The adenovirus E3 14.5-kilodalton protein, which is required for down-regulation of the epidermal growth factor receptor and prevention of tumor necrosis factor cytolysis, is an integral membrane protein oriented with its C terminus in the cytoplasm.
Krajcsi P; Tollefson AE; Anderson CW; Wold WS
J Virol; 1992 Mar; 66(3):1665-73. PubMed ID: 1531370
[TBL] [Abstract][Full Text] [Related]
12. Sorting Motifs in the Cytoplasmic Tail of the Immunomodulatory E3/49K Protein of Species D Adenoviruses Modulate Cell Surface Expression and Ectodomain Shedding.
Windheim M; Höning S; Leppard KN; Butler L; Seed C; Ponnambalam S; Burgert HG
J Biol Chem; 2016 Mar; 291(13):6796-812. PubMed ID: 26841862
[TBL] [Abstract][Full Text] [Related]
13. NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles.
Papadopoulos E; Oglecka K; Mäler L; Jarvet J; Wright PE; Dyson HJ; Gräslund A
Biochemistry; 2006 Jan; 45(1):159-66. PubMed ID: 16388591
[TBL] [Abstract][Full Text] [Related]
14. The adenovirus E3 10.4K and 14.5K proteins, which function to prevent cytolysis by tumor necrosis factor and to down-regulate the epidermal growth factor receptor, are localized in the plasma membrane.
Stewart AR; Tollefson AE; Krajcsi P; Yei SP; Wold WS
J Virol; 1995 Jan; 69(1):172-81. PubMed ID: 7983708
[TBL] [Abstract][Full Text] [Related]
15. Flexibility of the PDZ-binding motif in the micelle-bound form of Jagged-1 cytoplasmic tail.
Popovic M; Zlatev V; Hodnik V; Anderluh G; Felli IC; Pongor S; Pintar A
Biochim Biophys Acta; 2012 Jul; 1818(7):1706-16. PubMed ID: 22465068
[TBL] [Abstract][Full Text] [Related]
16. The signal-anchor domain of adenovirus E3-6.7K, a type III integral membrane protein, can direct adenovirus E3-gp19K, a type I integral membrane protein, into the membrane of the endoplasmic reticulum.
Wilson-Rawls J; Deutscher SL; Wold WS
Virology; 1994 May; 201(1):66-76. PubMed ID: 8178490
[TBL] [Abstract][Full Text] [Related]
17. Micellar environments induce structuring of the N-terminal tail of the prion protein.
Renner C; Fiori S; Fiorino F; Landgraf D; Deluca D; Mentler M; Grantner K; Parak FG; Kretzschmar H; Moroder L
Biopolymers; 2004 Mar; 73(4):421-33. PubMed ID: 14991659
[TBL] [Abstract][Full Text] [Related]
18. Characterization of the adenovirus E3 protein that down-regulates the epidermal growth factor receptor. Evidence for intermolecular disulfide bonding and plasma membrane localization.
Hoffman P; Yaffe MB; Hoffman BL; Yei S; Wold WS; Carlin C
J Biol Chem; 1992 Jul; 267(19):13480-7. PubMed ID: 1377684
[TBL] [Abstract][Full Text] [Related]
19. Enhanced degradation of EGF receptors by a sorting nexin, SNX1.
Kurten RC; Cadena DL; Gill GN
Science; 1996 May; 272(5264):1008-10. PubMed ID: 8638121
[TBL] [Abstract][Full Text] [Related]
20. Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor.
Chin LS; Raynor MC; Wei X; Chen HQ; Li L
J Biol Chem; 2001 Mar; 276(10):7069-78. PubMed ID: 11110793
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
