Stability cluster links hydrofobic gate to K873 in ATP8A2

Autor: Stine Mikkelsen, Anna Lindeløv Vestergaard, Jonathan Allan Coleman, Bente Vilsen, Molday, Robert S., Jens Peter Andersen

Publikováno v: Mikkelsen, S, Vestergaard, A L, Coleman, J A, Vilsen, B, Molday, R S & Andersen, J P 2014, ' Stability cluster links hydrofobic gate to K873 in ATP8A2 ', Lunteren, Netherlands, 30/08/2014-05/09/2014, .
Aarhus University

ATP8A2 is a P4-type ATPase, a ”flippase” that translocates aminophospholipids such as phosphatidylserine (PS) and phosphatidylethanolamine (PE) from the exoplasmic to the cytoplasmic side of the plasma membrane. This flippase has similar mechanis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::d84747dd178a1b33d49c8f07506454b6
https://pure.au.dk/portal/da/publications/stability-cluster-links-hydrofobic-gate-to-k873-in-atp8a2(57ddc9bc-170d-432b-b82b-e2bad8af5c31).html

Biochemical Characterization of P4-ATPase Mutations Associated with Intrahepatic Cholestatic Disease

Autor: Rasmus Gantzel, Anna Lindeløv Vestergaard, Stine Mikkelsen, Molday, Robert S., Jens Peter Andersen

Publikováno v: Gantzel, R, Vestergaard, A L, Mikkelsen, S, Molday, R S & Andersen, J P 2014, ' Biochemical Characterization of P4-ATPase Mutations Associated with Intrahepatic Cholestatic Disease ', Na,K-ATPase and related transport ATPases, structure, mechanism, cell biology, health and disease, Lunteren, Netherlands, 30/08/2014-05/09/2014 .
Gantzel, R, Vestergaard, A L, Mikkelsen, S, Molday, R S & Andersen, J P 2015, ' Biochemical characterization of P4-ATPase mutations associated with Intrahepatic Cholestatic Disease ', Scandinavian Physiological Society Annual Meeting, Aarhus, Denmark, 17/09/2015-20/09/2015 .
Gantzel, R, Vestergaard, A L, Mikkelsen, S, S. Molday, R & Andersen, J P 2015, ' Biochemical Characterization of P4-ATPase Mutations Associated with Intrahepatic Cholestatic Disease ', 4th International Workshop on Expression, Structure and Function of Membrane Proteins, Firenze, Italy, 28/06/2015-02/07/2015 .
Aarhus University

The cholestatic disorders progressive familial intrahepatic cholestasis type 1 (PFIC1, also referred to as Byler’s disease) and benign recurrent intrahepatic cholestasis type 1 (BRIC1) are caused by mutation of the P4-ATPase ATP8B1. The substrate o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::16908308c47f06a3d6a93b607a0b0640
https://pure.au.dk/portal/da/publications/biochemical-characterization-of-p4atpase-mutations-associated-with-intrahepatic-cholestatic-disease(97066953-5481-4c54-a77c-9ca733737602).html

Analysis of amino acid residues of potential importance for phosphatidylserine specificity of P4-type ATPase ARP8A2

Autor: Louise Mogensen, Anna Lindeløv Vestergaard, Stine Mikkelsen, Jonathan Allan Coleman, Bente Vilsen, Molday, Robert S., Jens Peter Andersen

Publikováno v: Aarhus University
Mogensen, L, Vestergaard, A L, Mikkelsen, S, Coleman, J A, Vilsen, B, Molday, R S & Andersen, J P 2015, ' Analysis of amino acid residues of potential importance for phosphatidylserine specificity of P4-type ATPase ARP8A2 ', Firenze, Italy, 28/06/2015-02/07/2015, .

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::3be80e1543d45cecd59370167b581526
https://pure.au.dk/portal/en/publications/analysis-of-amino-acid-residues-of-potential-importance-for-phosphatidylserine-specificity-of-p4type-atpase-arp8a2(e939de64-2546-4e6b-bdd0-85fd7e2dd2aa).html

Analysis of Amino Acid Residues of Potential Importance for Phosphati-dylserine Specificity of P4-type ATPase ATP8A2

Autor: Louise Mogensen, Anna Lindeløv Vestergaard, Stine Mikkelsen, Jonathan Allan Coleman, Bente Vilsen, Molday, Robert S., Jens Peter Andersen

Publikováno v: Aarhus University
Mogensen, L, Vestergaard, A L, Mikkelsen, S, Coleman, J A, Vilsen, B, Molday, R S & Andersen, J P 2014, ' Analysis of Amino Acid Residues of Potential Importance for Phosphati-dylserine Specificity of P4-type ATPase ATP8A2 ', Lunteren, Netherlands, 30/08/2014-05/09/2014, .

The asymmetric structure of the plasma membrane is maintained through internalization of phos-pholipids by the family of P4-ATPases by a poorly characterized mechanism. Studies in yeast point towards a non-classical pathway involving important residu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::421278b1b2dba284b236d5a39add71e8
https://pure.au.dk/portal/en/publications/analysis-of-amino-acid-residues-of-potential-importance-for-phosphatidylserine-specificity-of-p4type-atpase-atp8a2(f27feb6d-dba3-4f33-bdab-44cad310f065).html