PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18502797-2	2008	The central domain of MARCKS is both basic (zeta = +13) and hydrophobic (five Phe residues), and is flanked with two long chains, one ending with the myristoylated N-terminus.	Phenylalanine	78-81	myristoylated alanine rich protein kinase C substrate	Homo sapiens	22-28	
27166806-4	2016	Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers.	Phenylalanine	64-67	myristoylated alanine rich protein kinase C substrate	Homo sapiens	16-22	
27166806-4	2016	Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers.	Phenylalanine	64-67	myristoylated alanine rich protein kinase C substrate	Homo sapiens	107-113	
25195712-6	2014	An atomistic molecular dynamics (MD) simulation suggested an important role played by the insertion of the Phe residues within MARCKS-ED.	Phenylalanine	107-110	myristoylated alanine rich protein kinase C substrate	Homo sapiens	127-133	
12670959-0	2003	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.	Phenylalanine	75-88	myristoylated alanine rich protein kinase C substrate	Homo sapiens	96-141	
14507707-4	2003	Two sets of data indicate that the phenylalanine residues of the MARCKS-ED are positioned within the membrane hydrocarbon a few angstroms from the aqueous-hydrocarbon interface.	Phenylalanine	35-48	myristoylated alanine rich protein kinase C substrate	Homo sapiens	65-71	
12670959-2	2003	Both the MARCKS protein and a peptide corresponding to the effector domain (an unstructured region that contains 13 basic residues and 5 phenylalanines), MARCKS-(151-175), laterally sequester the polyvalent lipid PI(4,5)P2 in the plane of a bilayer membrane with high affinity.	Phenylalanine	137-151	myristoylated alanine rich protein kinase C substrate	Homo sapiens	9-15	
12670959-2	2003	Both the MARCKS protein and a peptide corresponding to the effector domain (an unstructured region that contains 13 basic residues and 5 phenylalanines), MARCKS-(151-175), laterally sequester the polyvalent lipid PI(4,5)P2 in the plane of a bilayer membrane with high affinity.	Phenylalanine	137-151	myristoylated alanine rich protein kinase C substrate	Homo sapiens	154-160	
12670959-4	2003	Measurements of cross-relaxation rates in two-dimensional nuclear Overhauser enhancement spectroscopy NMR experiments show that the five Phe rings of MARCKS-(151-175) penetrate into the acyl chain region of phosphatidylcholine bilayers containing phosphatidylglycerol or PI(4,5)P2.	Phenylalanine	137-140	myristoylated alanine rich protein kinase C substrate	Homo sapiens	150-156	
10736562-1	2000	MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence.	Phenylalanine	232-246	myristoylated alanine rich protein kinase C substrate	Homo sapiens	0-6	
10956022-7	2000	Replacing the five Phe with five Ala residues in MARCKS(151-175) decreases the binding to 10:1 PC/PS vesicles only slightly (6-fold).	Phenylalanine	19-22	myristoylated alanine rich protein kinase C substrate	Homo sapiens	49-55	
10736562-1	2000	MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence.	Phenylalanine	232-246	myristoylated alanine rich protein kinase C substrate	Homo sapiens	8-53	
9341159-2	1997	Previous studies with a peptide corresponding to the effector region, MARCKS-(151-175), showed that the 13 basic residues interact electrostatically with acidic lipids and that the 5 hydrophobic phenylalanine residues penetrate the polar head group region of the bilayer.	Phenylalanine	195-208	myristoylated alanine rich protein kinase C substrate	Homo sapiens	70-76	
10504221-10	1999	As expected, MARCKS-Ala binds more weakly to membranes composed of PS/PC (1:9) than does the native MARCKS peptide; however, each phenylalanine contributes only 0.2 kcal/mol to the binding energy difference, far less than the 1.3 kcal/mol expected for the binding of phenylalanine to the membrane interface.	Phenylalanine	130-143	myristoylated alanine rich protein kinase C substrate	Homo sapiens	13-19	
10504221-10	1999	As expected, MARCKS-Ala binds more weakly to membranes composed of PS/PC (1:9) than does the native MARCKS peptide; however, each phenylalanine contributes only 0.2 kcal/mol to the binding energy difference, far less than the 1.3 kcal/mol expected for the binding of phenylalanine to the membrane interface.	Phenylalanine	267-280	myristoylated alanine rich protein kinase C substrate	Homo sapiens	13-19