PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18989812-6 2008 Our central idea was to inhibit the PLA(2) and Mel activities through histidine alkylation and or tryptophan oxidation (with pbb, para-bromo-phenacyl bromide, and/or NBS- N-bromosuccinimide, respectively) to make their encapsulations possible within stabilized liposomes. Tryptophan 98-108 phospholipase A2 group IB Homo sapiens 36-42 21435339-0 2011 Changes in PLA(2) activity after interacting with anti-inflammatory drugs and model membranes: evidence for the involvement of tryptophan residues. Tryptophan 127-137 phospholipase A2 group IB Homo sapiens 11-17 21435339-3 2011 The intrinsic fluorescence of PLA(2) tryptophan residues was further used to gain complementary information regarding the accessibility of these residues on the PLA(2) structure upon interaction with the NSAIDs tested; and to calculate the NSAIDs-PLA(2) binding constants. Tryptophan 35-47 phospholipase A2 group IB Homo sapiens 161-167 21435339-5 2011 Overall, results gathered in this study point to the conclusion that the studied NSAIDs inhibit PLA(2) activity due to a disturbance of the enzyme binding efficiency to membrane interface possibly by a shielding effect of the Trp residues required for the membrane interfacial binding step that precedes lipolysis process. Tryptophan 226-229 phospholipase A2 group IB Homo sapiens 96-102 17029399-3 2006 Increasing the anionic charge of membranes results in a blue shift of the fluorescence of Trp(3) of hIBPLA(2), a decrease in quenching by acrylamide, and an increase in enzyme activity, reflecting an enhancement in the membrane binding of PLA(2). Tryptophan 90-93 phospholipase A2 group IB Homo sapiens 103-109 17029400-2 2006 To understand the functional significance of amino acid residues at key positions, we have studied the effects of the substitution of Val(3) (membrane binding surface) and Phe(5) (substrate binding pocket) of human group IIA PLA(2) by tryptophan on the structure and function of the enzyme. Tryptophan 235-245 phospholipase A2 group IB Homo sapiens 225-231 17029400-8 2006 Although Trp(3) at the membrane binding face of PLA(2) facilitates the proper membrane binding of the enzyme, Trp(5) in the internal substrate binding site causes partial unwinding of the N-terminal helix in order to interact with the membrane. Tryptophan 9-12 phospholipase A2 group IB Homo sapiens 48-54 12755634-5 2003 As expected, resonance energy transfer from the tryptophan donor in PLA2 to an acceptor probe partitioned in E(#) shows a biphasic dependence as the probe coexisting with PLA2 is diluted at higher alkyl sulfate concentrations. Tryptophan 48-58 phospholipase A2 group IB Homo sapiens 68-72 12755634-5 2003 As expected, resonance energy transfer from the tryptophan donor in PLA2 to an acceptor probe partitioned in E(#) shows a biphasic dependence as the probe coexisting with PLA2 is diluted at higher alkyl sulfate concentrations. Tryptophan 48-58 phospholipase A2 group IB Homo sapiens 171-175 11966470-5 2002 Replacing Trp(61) with another aromatic residue [Trp(61)-->Tyr (W61Y)] resulted in an increase in all activities (14-157%), whereas replacing it with an aliphatic residue [Trp(61)-->Gly (W61G)] caused a dramatic loss of LCAT (-90%) and PLA(2) (-82%) activities, but not the esterase activity (-5%). Tryptophan 10-13 phospholipase A2 group IB Homo sapiens 242-248 11966470-5 2002 Replacing Trp(61) with another aromatic residue [Trp(61)-->Tyr (W61Y)] resulted in an increase in all activities (14-157%), whereas replacing it with an aliphatic residue [Trp(61)-->Gly (W61G)] caused a dramatic loss of LCAT (-90%) and PLA(2) (-82%) activities, but not the esterase activity (-5%). Tryptophan 49-52 phospholipase A2 group IB Homo sapiens 242-248 11966470-5 2002 Replacing Trp(61) with another aromatic residue [Trp(61)-->Tyr (W61Y)] resulted in an increase in all activities (14-157%), whereas replacing it with an aliphatic residue [Trp(61)-->Gly (W61G)] caused a dramatic loss of LCAT (-90%) and PLA(2) (-82%) activities, but not the esterase activity (-5%). Tryptophan 49-52 phospholipase A2 group IB Homo sapiens 242-248 8040067-4 1994 It also quenched the tryptophan fluorescence of Naja mocambique venom PLA2; almost 100% quenching being attained at a thielocin B3/enzyme molar ratio of 1.0. Tryptophan 21-31 phospholipase A2 group IB Homo sapiens 70-74 7702745-4 1994 Fluorescence enhancement of ANS in PLA2-ANS complex increased upon addition of Ca2+ or change of the buffer to acidic pH, resulting in a higher efficiency of energy transfer from Trp residues to ANS. Tryptophan 179-182 phospholipase A2 group IB Homo sapiens 35-39 1991096-1 1991 The fluorescence anisotropy decay of the single tryptophan residue in phospholipase A2 was studied by use of differential polarized phase fluorometry and computer simulations of protein dynamics. Tryptophan 48-58 phospholipase A2 group IB Homo sapiens 70-86 8354259-2 1993 The binding effect of enantiomeric substrate analogs under micellar form on the local conformation and dynamics of the N-terminal region of porcine pancreas phospholipase A2 was examined by time-resolved fluorescence measurements of its single tryptophan residue (Trp3). Tryptophan 244-254 phospholipase A2 group IB Homo sapiens 157-173 1888737-0 1991 Insight into the conformational dynamics of specific regions of porcine pancreatic phospholipase A2 from a time-resolved fluorescence study of a genetically inserted single tryptophan residue. Tryptophan 173-183 phospholipase A2 group IB Homo sapiens 83-99 1821781-2 1991 The new key elements required for PLA2 isolation were the maintenance of the fusion protein in solution after the initial solubilization and the use of a tryptophan cleavage procedure for regeneration of native PLA2 from the fusion protein. Tryptophan 154-164 phospholipase A2 group IB Homo sapiens 34-38 3219357-0 1988 Rotational dynamics of the single tryptophan of porcine pancreatic phospholipase A2, its zymogen, and an enzyme/micelle complex. Tryptophan 34-44 phospholipase A2 group IB Homo sapiens 67-83 2597672-5 1989 Interaction of purified snake venom phospholipase A2 (Naja mocambique) with PGBx resulted in dose-dependent quenching of the enzyme"s tryptophan fluorescence; 50% quench was noted with a molar ratio of PGBx/enzyme of 1.5. Tryptophan 134-144 phospholipase A2 group IB Homo sapiens 36-52 2752091-15 1989 The method was also applied to real phase/modulation data gathered on known fluorophores and their mixtures and on tryptophan fluorescence in phospholipase A2. Tryptophan 115-125 phospholipase A2 group IB Homo sapiens 142-158 2129000-7 1990 Inhibition was independent of substrate phospholipid concentration over a 24-fold range (5-120 microM) and PGBx quenched the tryptophan fluorescence of snake venom phospholipase A2 in a dose-dependent manner. Tryptophan 125-135 phospholipase A2 group IB Homo sapiens 164-180 34375468-0 2021 Singlet Oxygen-Induced Phospholipase A2 Inhibition: a Major Role for Interfacial Tryptophan Dioxidation. Tryptophan 81-91 phospholipase A2 group IB Homo sapiens 23-39 34375468-5 2021 A more detailed analysis of the plasma-treated PLA 2 identified tryptophan 128 as a hot spot, rich in double oxidation. Tryptophan 64-74 phospholipase A2 group IB Homo sapiens 47-52 2590165-1 1989 beta 1-Bungarotoxin has only one tryptophan residue, namely Trp-19 in the phospholipase A2 subunit. Tryptophan 60-63 phospholipase A2 group IB Homo sapiens 74-90 3707906-11 1986 The fluorescence emission spectrum of the single tryptophan of phospholipase A2 is a sensitive monitor of interfacial complex formation and shows that interaction of the protein with detergent micelles is strongly dependent on the presence of a negatively charged amphiphile. Tryptophan 49-59 phospholipase A2 group IB Homo sapiens 63-79 53-2 1975 The localization of the previously postulated interface recognition site (IRS) in porcine pancreatic phospholipase A2, required for a specific interaction between the enzyme and organized lipid-water interfaces, was investigated by ultraviolet difference spectroscopy, by measurements of the intrinsic fluorescence of the unique Trp residue, and by protection experiments against specific tryptic hydrolysis. Tryptophan 329-332 phospholipase A2 group IB Homo sapiens 101-117 19461-0 1977 Spectral perturbations of the histidine and tryptophan in cobra venom phospholipase A2 upon metal ion and mixed micelle binding. Tryptophan 44-54 phospholipase A2 group IB Homo sapiens 70-86 4084578-0 1985 Complex photophysics of the single tryptophan of porcine pancreatic phospholipase A2, its zymogen, and an enzyme/micelle complex. Tryptophan 35-45 phospholipase A2 group IB Homo sapiens 68-84 4084578-1 1985 The fluorescence emission of the single tryptophan in porcine pancreatic phospholipase A2, its zymogen, and a micellar complex of the enzyme with the nonhydrolyzable substrate analogue n-hexadecylphosphocholine has been studied by both steady-state and time-resolved techniques. Tryptophan 40-50 phospholipase A2 group IB Homo sapiens 73-89 4084578-8 1985 Formation of a complex between phospholipase A2 and micelles of n-hexadecylphospohocholine produces large changes in the tryptophan emission that are associated with transfer to a hydrophobic environment. Tryptophan 121-131 phospholipase A2 group IB Homo sapiens 31-47 6532565-3 1984 Prophospholipase binding is accompanied by a change in the environment of the single tryptophan residue qualitatively similar to that observed when the active enzyme, phospholipase A2 (PLA), binds to micelles. Tryptophan 85-95 phospholipase A2 group IB Homo sapiens 167-183 6532565-3 1984 Prophospholipase binding is accompanied by a change in the environment of the single tryptophan residue qualitatively similar to that observed when the active enzyme, phospholipase A2 (PLA), binds to micelles. Tryptophan 85-95 phospholipase A2 group IB Homo sapiens 185-188