Phenylalanine

myristoylated alanine rich protein kinase C substrate ; Homo sapiens







9 Article(s)
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1 27166806 Determinants of Curvature-Sensing Behavior for MARCKS-Fragment Peptides. 2016 May 10 2
2 25195712 Biophysical investigations with MARCKS-ED: dissecting the molecular mechanism of its curvature sensing behaviors. 2014 Dec 1
3 18502797 The "electrostatic-switch" mechanism: Monte Carlo study of MARCKS-membrane interaction. 2008 Aug 1
4 12670959 Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer. 2003 Jun 13 4
5 14507707 Location of the myristoylated alanine-rich C-kinase substrate (MARCKS) effector domain in negatively charged phospholipid bicelles. 2003 Oct 1
6 10736562 MARCKS: a case of molecular exaptation? 2000 May 2
7 10956022 Membrane binding of peptides containing both basic and aromatic residues. Experimental studies with peptides corresponding to the scaffolding region of caveolin and the effector region of MARCKS. 2000 Aug 22 1
8 10504221 Interactions controlling the membrane binding of basic protein domains: phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces. 1999 Sep 28 2
9 9341159 Kinetics of interaction of the myristoylated alanine-rich C kinase substrate, membranes, and calmodulin. 1997 Oct 24 1