PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7718893-7 1995 Measurement of EGTA-resistant gelsolin/actin complexes in HL-60 cells shows that 95% to 100% of complexes exist in the TSF-actin pool only. Egtazic Acid 15-19 gelsolin Homo sapiens 30-38 9826630-6 1998 The data suggest that binding of Ca2+ to the gelsolin-F-actin complex is the rate-limiting step for F-actin severing by gelsolin; this Ca2+ binding event is a committed step that results in a Ca2+ ion bound at a high-affinity, EGTA-resistant site. Egtazic Acid 227-231 gelsolin Homo sapiens 120-128 21072610-4 2003 Addition of EGTA could disassociate the actin-gelsolin complexes, reducing the ratio to 1.2+-0.23, and the addition of PIP(2) could further reduce the ratio to 0.8+-0.1. Egtazic Acid 12-16 gelsolin Homo sapiens 46-54 9826630-6 1998 The data suggest that binding of Ca2+ to the gelsolin-F-actin complex is the rate-limiting step for F-actin severing by gelsolin; this Ca2+ binding event is a committed step that results in a Ca2+ ion bound at a high-affinity, EGTA-resistant site. Egtazic Acid 227-231 gelsolin Homo sapiens 45-53 3040771-5 1987 The calcium-dependent actin filament-severing activity of platelet extracts, a function of free gelsolin, fell in concert with the formation of EGTA-stable actin/gelsolin complexes, and rose when the adsorption experiments indicated that free gelsolin was restored. Egtazic Acid 144-148 gelsolin Homo sapiens 162-170 7606806-5 1995 Actin pools were measured by NBDphallacidin binding and by gel scans and expressed relative to basal; gelsolin-actin interactions were measured as change in the amount of EGTA-resistant gelsolin:actin (G:A) complexes and by immunoblot quantification of gelsolin in actin pools. Egtazic Acid 171-175 gelsolin Homo sapiens 102-110 7606806-5 1995 Actin pools were measured by NBDphallacidin binding and by gel scans and expressed relative to basal; gelsolin-actin interactions were measured as change in the amount of EGTA-resistant gelsolin:actin (G:A) complexes and by immunoblot quantification of gelsolin in actin pools. Egtazic Acid 171-175 gelsolin Homo sapiens 186-194 7606806-5 1995 Actin pools were measured by NBDphallacidin binding and by gel scans and expressed relative to basal; gelsolin-actin interactions were measured as change in the amount of EGTA-resistant gelsolin:actin (G:A) complexes and by immunoblot quantification of gelsolin in actin pools. Egtazic Acid 171-175 gelsolin Homo sapiens 186-194 7606806-6 1995 In basal PMNs, 33% of PMN gelsolin is bound in 1:1 EGTA-resistant G:A complexes and TSF and TIF retain 30% and 0% of PMN gelsolin, respectively. Egtazic Acid 51-55 gelsolin Homo sapiens 26-34 7606806-8 1995 At maximum change (60 seconds), total F-actin (TIF + TSF) and TSF decrease and TIF increases by 25%; gelsolin is bound to both TSF and TIF (35% of total gelsolin in each pool), and 1:1 EGTA-resistant G:A complexes increase from 33% to 70%. Egtazic Acid 185-189 gelsolin Homo sapiens 101-109 8394694-0 1993 Definition of the EGTA-independent interface involved in the serum gelsolin-actin complex. Egtazic Acid 18-22 gelsolin Homo sapiens 67-75 8394694-2 1993 In the presence of EGTA, the N-terminal domain of gelsolin is known to be involved. Egtazic Acid 19-23 gelsolin Homo sapiens 50-58 1323562-4 1992 To obtain further information on the nucleotide binding properties of gelsolin, binding studies were done in the presence of EGTA with GTP, ADP, and GDP by equilibrium dialysis. Egtazic Acid 125-129 gelsolin Homo sapiens 70-78 8082657-5 1994 The gelsolin staining of myofibrils was EGTA-resistant; it persisted after glycerol extraction and extensive washing. Egtazic Acid 40-44 gelsolin Homo sapiens 4-12 8386174-5 1993 At pH below 6.0, gelsolin no longer requires Ca2+ for activity and severs actin filaments, binds two actin monomers, and nucleates filament formation in EGTA-containing solutions. Egtazic Acid 153-157 gelsolin Homo sapiens 17-25 1337290-1 1992 In vitro Ca++ activates gelsolin to sever F-actin and form a gelsolin-actin (GA) complex at the+end of F-actin that is not dissociated by ethylene glycol-bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) but is separated by EGTA+PIP/PIP2. Egtazic Acid 209-213 gelsolin Homo sapiens 24-32 1337290-1 1992 In vitro Ca++ activates gelsolin to sever F-actin and form a gelsolin-actin (GA) complex at the+end of F-actin that is not dissociated by ethylene glycol-bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) but is separated by EGTA+PIP/PIP2. Egtazic Acid 209-213 gelsolin Homo sapiens 61-69 1337290-1 1992 In vitro Ca++ activates gelsolin to sever F-actin and form a gelsolin-actin (GA) complex at the+end of F-actin that is not dissociated by ethylene glycol-bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) but is separated by EGTA+PIP/PIP2. Egtazic Acid 235-239 gelsolin Homo sapiens 24-32 1337290-1 1992 In vitro Ca++ activates gelsolin to sever F-actin and form a gelsolin-actin (GA) complex at the+end of F-actin that is not dissociated by ethylene glycol-bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) but is separated by EGTA+PIP/PIP2. Egtazic Acid 235-239 gelsolin Homo sapiens 61-69 2161855-3 1990 The rate of dissociation of EGTA resistant, 1:1 gelsolin-actin complexes is more rapid in cells exposed to 10(-7) M fmlp than in cells exposed to 10(-9) M fmlp, and the extent of dissociation 10 s after activation depends upon the fmlp concentration. Egtazic Acid 28-32 gelsolin Homo sapiens 48-56 2161855-4 1990 Furthermore, 300 s after fmlp activation when F-actin content is decreasing, gelsolin reassociates with actin as evidenced by an increase in the amount of EGTA resistant, 1:1 gelsolin-actin complex. Egtazic Acid 155-159 gelsolin Homo sapiens 77-85 2161855-4 1990 Furthermore, 300 s after fmlp activation when F-actin content is decreasing, gelsolin reassociates with actin as evidenced by an increase in the amount of EGTA resistant, 1:1 gelsolin-actin complex. Egtazic Acid 155-159 gelsolin Homo sapiens 175-183 3040771-5 1987 The calcium-dependent actin filament-severing activity of platelet extracts, a function of free gelsolin, fell in concert with the formation of EGTA-stable actin/gelsolin complexes, and rose when the adsorption experiments indicated that free gelsolin was restored. Egtazic Acid 144-148 gelsolin Homo sapiens 162-170 3025333-2 1987 We have developed an immunoadsorption technique for quantitating EGTA-resistant gelsolin/actin complexes in macrophages extracted with Triton X-100. Egtazic Acid 65-69 gelsolin Homo sapiens 80-88 3025333-7 1987 Therefore, our results suggest that macrophages possess a mechanism, not directly involving Ca2+, for dissociating actin/gelsolin EGTA-resistant complexes. Egtazic Acid 130-134 gelsolin Homo sapiens 121-129 3021456-7 1986 The gelsolin-actin complex was found to bind fourfold faster to the barbed ends in the presence of Ca2+ (10 X 10(6) M-1 s-1) than in excess EGTA (2.5 X 10(6) M-1 s-1). Egtazic Acid 140-144 gelsolin Homo sapiens 4-12 2999102-2 1985 However, the 1:2 complex dissociated into a 1:1 gelsolin:actin complex and monomeric actin when excess EGTA was added. Egtazic Acid 103-107 gelsolin Homo sapiens 48-56 3001099-13 1986 Elution with 4 mM EGTA released material that gel filtration showed to be the EGTA-stable 130,000-mol-wt gelsolin-actin complex, GA1Ca1. Egtazic Acid 18-22 gelsolin Homo sapiens 105-113 3001099-13 1986 Elution with 4 mM EGTA released material that gel filtration showed to be the EGTA-stable 130,000-mol-wt gelsolin-actin complex, GA1Ca1. Egtazic Acid 78-82 gelsolin Homo sapiens 105-113 3002792-3 1986 Complex formation has been studied by high-performance gel permeation chromatography; plasma gelsolin alone elutes at an Mr of about 77000 and a Stokes radius of 3.7 nm; complex formation occurs in the presence of Ca2+: by chromatography in the presence of EGTA, a binary complex is obtained with an Mr of 134000 and a Stokes radius of 4.7 nm; and by chromatography in the presence of Ca2+, a ternary complex is obtained with an Mr of 173000 and a Stokes radius of 5.2 nm. Egtazic Acid 257-261 gelsolin Homo sapiens 93-101 3001099-19 1986 Similarly, preformed brevin-actin-Ca2+ complex, equilibrated with EGTA, was retained by 4F8 IgA-Sepharose. Egtazic Acid 66-70 gelsolin Homo sapiens 21-27 3001100-11 1986 Brevin binding occurs in either Ca2+ or EGTA, but is slightly more intense in EGTA suggesting some severing and filament removal may occur in Ca2+. Egtazic Acid 40-44 gelsolin Homo sapiens 0-6 3001100-11 1986 Brevin binding occurs in either Ca2+ or EGTA, but is slightly more intense in EGTA suggesting some severing and filament removal may occur in Ca2+. Egtazic Acid 78-82 gelsolin Homo sapiens 0-6 2999102-3 1985 Plasma gelsolin bound tightly to the barbed ends of actin filaments and also severed filaments in the presence of Ca2+ and bound weakly to the filament barbed end in the presence of EGTA. Egtazic Acid 182-186 gelsolin Homo sapiens 7-15 2994715-5 1985 In this paper, the interactions with actin of the ethylene glycol bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) stable 1:1 gelsolin-actin complexes are compared with those of free gelsolin. Egtazic Acid 50-119 gelsolin Homo sapiens 138-146 2994715-5 1985 In this paper, the interactions with actin of the ethylene glycol bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) stable 1:1 gelsolin-actin complexes are compared with those of free gelsolin. Egtazic Acid 121-125 gelsolin Homo sapiens 138-146 2994715-5 1985 In this paper, the interactions with actin of the ethylene glycol bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) stable 1:1 gelsolin-actin complexes are compared with those of free gelsolin. Egtazic Acid 121-125 gelsolin Homo sapiens 195-203 2994715-6 1985 The abilities of free or complexed gelsolin to sever actin filaments, nucleate filament assembly, bind to the fast growing (+) filament ends, and lower the filament size distribution in the presence of either Ca2+ or EGTA were examined. Egtazic Acid 217-221 gelsolin Homo sapiens 35-43 2994715-8 1985 The gelsolin-actin complexes, however, differ from free gelsolin in that they have a higher affinity for (+) filament ends in EGTA and they cannot sever filaments in calcium. Egtazic Acid 126-130 gelsolin Homo sapiens 4-12 2994715-8 1985 The gelsolin-actin complexes, however, differ from free gelsolin in that they have a higher affinity for (+) filament ends in EGTA and they cannot sever filaments in calcium. Egtazic Acid 126-130 gelsolin Homo sapiens 56-64 6204208-7 1984 In the presence of EGTA, gelsolin has no effect on the movement of membranous organelles, but in the presence of 10 microM Ca2+ it completely blocks transport of all membranous organelles. Egtazic Acid 19-23 gelsolin Homo sapiens 25-33 6330059-7 1984 We have shown previously that the Mr = 130,000 species is an EGTA-stable binary complex of one actin and one gelsolin. Egtazic Acid 61-65 gelsolin Homo sapiens 109-117