PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1560011-1	1992	All 6 tryptophan residues in the human HepG2-type glucose transporter (Glut1) were individually altered by site-directed mutagenesis to investigate the role of these residues in transport function.	Tryptophan	6-16	solute carrier family 2 member 1	Homo sapiens	71-76	
12628696-2	2003	The permeabilities (10(-9) cm/s) of glucose transporter (GLUT1) proteoliposomes were estimated to be 4.6, 1.0, 1.4 and 2.1 for D-glucose, L-glucose, L-Tyr and L-Trp, respectively; 15, 3.3, 5.1 and 2.1 times higher than the corresponding permeabilities of liposomes.	Tryptophan	159-164	solute carrier family 2 member 1	Homo sapiens	57-62	
12628696-8	2003	Upon immobilized biomembrane affinity chromatography, Trp decreased the cytochalasin B retardation by GLUT1 only at levels far above the physiological Trp concentration.	Tryptophan	54-57	solute carrier family 2 member 1	Homo sapiens	102-107	
7779817-7	1995	Changes in the accessibility of aqueous soluble quenchers (I- and acrylamide) to GLUT-1 Trp and Tyr residues suggested that ligand binding causes interfacial fluorophores to move closer to ionic groups in the lipid head group region of the membrane.	Tryptophan	88-91	solute carrier family 2 member 1	Homo sapiens	81-87	
7779817-10	1995	Studies monitoring the change in quenching of membrane probes by GLUT-1 tryptophans and energy transfer of GLUT-1 tryptophans to membrane probes support this idea.	Tryptophan	72-83	solute carrier family 2 member 1	Homo sapiens	65-71	
7779817-10	1995	Studies monitoring the change in quenching of membrane probes by GLUT-1 tryptophans and energy transfer of GLUT-1 tryptophans to membrane probes support this idea.	Tryptophan	114-125	solute carrier family 2 member 1	Homo sapiens	107-113	
8496948-1	1993	The kinetics of the initial phases of D-glucose binding to the glucose transport protein (GLUT1) of the human red cell can be followed by stopped-flow measurements of the time course of tryptophan (trp) fluorescence enhancement.	Tryptophan	186-196	solute carrier family 2 member 1	Homo sapiens	90-95	
8496948-1	1993	The kinetics of the initial phases of D-glucose binding to the glucose transport protein (GLUT1) of the human red cell can be followed by stopped-flow measurements of the time course of tryptophan (trp) fluorescence enhancement.	Tryptophan	198-201	solute carrier family 2 member 1	Homo sapiens	90-95	
8496948-2	1993	A number of control experiments have shown that the trp fluorescence kinetics are the result of conformational changes in GLUT1.	Tryptophan	52-55	solute carrier family 2 member 1	Homo sapiens	122-127	
10825451-8	2000	Glucose, CB and phloretin can quench the fluorescence of tryptophan residues in the glucose transporter 1, GLUT1.	Tryptophan	57-67	solute carrier family 2 member 1	Homo sapiens	107-112	
10350483-3	1999	Cytochalasin B binding to the purified, human erythrocyte glucose transport protein (GLUT1) induces quenching of GLUT1 intrinsic tryptophan fluorescence.	Tryptophan	129-139	solute carrier family 2 member 1	Homo sapiens	85-90	
10350483-3	1999	Cytochalasin B binding to the purified, human erythrocyte glucose transport protein (GLUT1) induces quenching of GLUT1 intrinsic tryptophan fluorescence.	Tryptophan	129-139	solute carrier family 2 member 1	Homo sapiens	113-118	
30075419-2	2018	The PAMAM dendrimers were modified with L-tryptophan and N-acetyl glucosamine (NAG) for higher drug loading and to utilize GLUT transporters, respectively.	Tryptophan	40-52	solute carrier family 2 member 1	Homo sapiens	123-127	
30075419-13	2018	Taken together, conjugating tryptophan to parent dendrimer could significantly enhance cargo loading capacity and binding NAG could be an attractive therapeutic approach for GLUT transporters mediated delivery of anticancer drugs.	Tryptophan	28-38	solute carrier family 2 member 1	Homo sapiens	174-178	
26306809-6	2015	In silico analysis of rubusoside:protein interactions pinpointed a major difference in substrate cavity between these transporters, a residue that is a tryptophan in GLUT1 but an alanine in GLUT5.	Tryptophan	152-162	solute carrier family 2 member 1	Homo sapiens	166-171