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Journal Abstract Search
509 related items for PubMed ID: 14581457
1. The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. Fölsch H, Pypaert M, Maday S, Pelletier L, Mellman I. J Cell Biol; 2003 Oct 27; 163(2):351-62. PubMed ID: 14581457 [Abstract] [Full Text] [Related]
2. Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. Fölsch H, Pypaert M, Schu P, Mellman I. J Cell Biol; 2001 Feb 05; 152(3):595-606. PubMed ID: 11157985 [Abstract] [Full Text] [Related]
4. A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Fölsch H, Ohno H, Bonifacino JS, Mellman I. Cell; 1999 Oct 15; 99(2):189-98. PubMed ID: 10535737 [Abstract] [Full Text] [Related]
5. The polarized epithelia-specific mu 1B-adaptin complements mu 1A-deficiency in fibroblasts. Eskelinen EL, Meyer C, Ohno H, von Figura K, Schu P. EMBO Rep; 2002 May 15; 3(5):471-7. PubMed ID: 11964383 [Abstract] [Full Text] [Related]
6. The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin-Darby canine kidney cells. Ang AL, Fölsch H, Koivisto UM, Pypaert M, Mellman I. J Cell Biol; 2003 Oct 27; 163(2):339-50. PubMed ID: 14581456 [Abstract] [Full Text] [Related]
7. Analysis of three μ1-AP1 subunits during zebrafish development. Gariano G, Guarienti M, Bresciani R, Borsani G, Carola G, Monti E, Giuliani R, Rezzani R, Bonomini F, Preti A, Schu P, Zizioli D. Dev Dyn; 2014 Feb 27; 243(2):299-314. PubMed ID: 24123392 [Abstract] [Full Text] [Related]
8. Ubiquitously expressed secretory carrier membrane proteins (SCAMPs) 1-4 mark different pathways and exhibit limited constitutive trafficking to and from the cell surface. Castle A, Castle D. J Cell Sci; 2005 Aug 15; 118(Pt 16):3769-80. PubMed ID: 16105885 [Abstract] [Full Text] [Related]
9. The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane. Gan Y, McGraw TE, Rodriguez-Boulan E. Nat Cell Biol; 2002 Aug 15; 4(8):605-9. PubMed ID: 12105417 [Abstract] [Full Text] [Related]
10. Phosphatidylinositol 3,4,5-trisphosphate localization in recycling endosomes is necessary for AP-1B-dependent sorting in polarized epithelial cells. Fields IC, King SM, Shteyn E, Kang RS, Fölsch H. Mol Biol Cell; 2010 Jan 01; 21(1):95-105. PubMed ID: 19864464 [Abstract] [Full Text] [Related]
11. [Regulatory mechanisms of the clathrin adaptor molecules AP-1 and GGAs]. Kametaka S, Bonifacino JS. Tanpakushitsu Kakusan Koso; 2008 Dec 01; 53(16 Suppl):2046-52. PubMed ID: 21038583 [No Abstract] [Full Text] [Related]
12. Analyzing the role of AP-1B in polarized sorting from recycling endosomes in epithelial cells. Fölsch H. Methods Cell Biol; 2015 Dec 01; 130():289-305. PubMed ID: 26360041 [Abstract] [Full Text] [Related]
13. Clathrin terminal domain-ligand interactions regulate sorting of mannose 6-phosphate receptors mediated by AP-1 and GGA adaptors. Stahlschmidt W, Robertson MJ, Robinson PJ, McCluskey A, Haucke V. J Biol Chem; 2014 Feb 21; 289(8):4906-18. PubMed ID: 24407285 [Abstract] [Full Text] [Related]
14. Novel function for AP-1B during cell migration. Kell MJ, Ang SF, Pigati L, Halpern A, Fölsch H. Mol Biol Cell; 2020 Oct 15; 31(22):2475-2493. PubMed ID: 32816642 [Abstract] [Full Text] [Related]
15. Basolateral sorting of the Mg²⁺ transporter CNNM4 requires interaction with AP-1A and AP-1B. Hirata Y, Funato Y, Miki H. Biochem Biophys Res Commun; 2014 Dec 12; 455(3-4):184-9. PubMed ID: 25449265 [Abstract] [Full Text] [Related]
16. Basolateral Sorting of the Sodium/Iodide Symporter Is Mediated by Adaptor Protein 1 Clathrin Adaptor Complexes. Koumarianou P, Fernández-Méndez C, Fajardo-Delgado D, Mielu LM, Santisteban P, De la Vieja A. Thyroid; 2022 Oct 12; 32(10):1259-1270. PubMed ID: 35833460 [Abstract] [Full Text] [Related]
18. Sorting of H,K-ATPase beta-subunit in MDCK and LLC-PK cells is independent of mu 1B adaptin expression. Duffield A, Fölsch H, Mellman I, Caplan MJ. Traffic; 2004 Jun 12; 5(6):449-61. PubMed ID: 15117319 [Abstract] [Full Text] [Related]