PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33986363-1 2021 Nuclear and cytoplasmic actin-cofilin rods are formed transiently under stress conditions to reduce actin filament turnover and ATP hydrolysis. Adenosine Triphosphate 128-131 cofilin 1 Homo sapiens 30-37 4096896-0 1985 Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5"-triphosphate. Adenosine Triphosphate 95-120 cofilin 1 Homo sapiens 20-27 4096896-1 1985 Cofilin, an actin-binding protein isolated from porcine brain that reacts with actin in a 1:1 molar ratio [Nishida, E., Maekawa, S., & Sakai, H. (1984) Biochemistry 23, 5307-5313], decreases the rate of exchange of ATP bound to G-actin with 1,N6-ethenoadenosine 5"-triphosphate in solution. Adenosine Triphosphate 219-222 cofilin 1 Homo sapiens 0-7 27762277-2 2016 Fluorescence microscopy demonstrated that HMM-GFP and cofilin-mCherry each bound cooperatively to different parts of actin filaments when they were added simultaneously in 0.2 muM ATP, indicating that the two cooperative bindings are mutually exclusive. Adenosine Triphosphate 180-183 cofilin 1 Homo sapiens 54-61 31558701-3 2019 Simultaneous inhibition of ALDOA activity and interaction with F-actin cytoskeleton using ALDOA slow-binding inhibitor UM0112176 leads to a rapid cofilin-dependent loss of F-actin stress fibers which is associated with elevated ROS production, inhibition of ATP synthesis, increase in calcium levels, caspase activation and arrested cellular proliferation. Adenosine Triphosphate 258-261 cofilin 1 Homo sapiens 146-153 28513458-12 2017 Stable actin-cofilin rods save cellular ATP, which is not used during active polymerization process. Adenosine Triphosphate 40-43 cofilin 1 Homo sapiens 13-20 28303963-3 2017 Cofilin preferentially interacts with older filaments by recognizing time-dependent changes in F-actin structure associated with the hydrolysis of ATP and release of inorganic phosphate (Pi) from the nucleotide cleft of actin. Adenosine Triphosphate 147-150 cofilin 1 Homo sapiens 0-7 31189606-8 2019 They also demonstrate that polymer activity, in the form of ATP hydrolysis on F-actin coupled to nucleotide-dependent cofilin binding, is sufficient to generate a form of active matter wherein asymmetric filament disassembly preserves filament number despite sustained severing. Adenosine Triphosphate 60-63 cofilin 1 Homo sapiens 118-125 27762277-3 2016 In 0.1 mM ATP, the motor domain of myosin (S1) strongly inhibited the formation of cofilin clusters along actin filaments. Adenosine Triphosphate 10-13 cofilin 1 Homo sapiens 83-90 24696143-6 2014 In addition, RhoA GTPase was activated within 15 min after the onset of FSS or ATP treatment and mediated ASFF following P2Y2R activation via the Rho kinase (ROCK)1/LIM kinase 2/cofilin pathway. Adenosine Triphosphate 79-82 cofilin 1 Homo sapiens 178-185 19289059-5 2009 The experiments revealed that in the presence of ADF/cofilin the accessibility of the bound epsilon-ATP decreased, indicating a closed and more compact ATP-binding pocket induced by the binding of ADF/cofilin. Adenosine Triphosphate 100-103 cofilin 1 Homo sapiens 53-60 24813767-4 2014 In both cases, ATP depletion associated with the presence of reactive species and other stressors regulate cofilin-1 by inducing the formation of aggregates composed primarily by actin and cofilin-1, known as cofilin/actin rods. Adenosine Triphosphate 15-18 cofilin 1 Homo sapiens 107-116 24813767-4 2014 In both cases, ATP depletion associated with the presence of reactive species and other stressors regulate cofilin-1 by inducing the formation of aggregates composed primarily by actin and cofilin-1, known as cofilin/actin rods. Adenosine Triphosphate 15-18 cofilin 1 Homo sapiens 189-198 24813767-4 2014 In both cases, ATP depletion associated with the presence of reactive species and other stressors regulate cofilin-1 by inducing the formation of aggregates composed primarily by actin and cofilin-1, known as cofilin/actin rods. Adenosine Triphosphate 15-18 cofilin 1 Homo sapiens 107-114 23212920-5 2013 The deficiency in cofilin binding can be explained by rapid exchange of bound nucleotide with ATP in solution, because cofilin does not bind ATP-bound actin. Adenosine Triphosphate 94-97 cofilin 1 Homo sapiens 18-25 23212920-5 2013 The deficiency in cofilin binding can be explained by rapid exchange of bound nucleotide with ATP in solution, because cofilin does not bind ATP-bound actin. Adenosine Triphosphate 94-97 cofilin 1 Homo sapiens 119-126 23267414-2 2012 Upon stress, the rapidly activated cofilin saturates actin filaments causing them to bundle into rod structures in either the nucleus or cytoplasm, halting actin polymerization and thus freeing ATP. Adenosine Triphosphate 194-197 cofilin 1 Homo sapiens 35-42 19289059-5 2009 The experiments revealed that in the presence of ADF/cofilin the accessibility of the bound epsilon-ATP decreased, indicating a closed and more compact ATP-binding pocket induced by the binding of ADF/cofilin. Adenosine Triphosphate 152-155 cofilin 1 Homo sapiens 53-60 15671020-4 2005 The Ca2+ ionophore A23187 and Ca2+-mobilizing agonists, ATP and histamine, induced SSH1L activation and cofilin dephosphorylation in cultured cells. Adenosine Triphosphate 56-59 cofilin 1 Homo sapiens 104-111 19000834-0 2008 Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation. Adenosine Triphosphate 23-26 cofilin 1 Homo sapiens 49-56 19000834-0 2008 Chronophin mediates an ATP-sensing mechanism for cofilin dephosphorylation and neuronal cofilin-actin rod formation. Adenosine Triphosphate 23-26 cofilin 1 Homo sapiens 88-95 19000834-5 2008 We demonstrate the ATP-sensitive interaction of the cofilin phosphatase chronophin (CIN) with the chaperone hsp90 to form a biosensor that mediates cofilin/actin rod formation. Adenosine Triphosphate 19-22 cofilin 1 Homo sapiens 52-59 19000834-5 2008 We demonstrate the ATP-sensitive interaction of the cofilin phosphatase chronophin (CIN) with the chaperone hsp90 to form a biosensor that mediates cofilin/actin rod formation. Adenosine Triphosphate 19-22 cofilin 1 Homo sapiens 148-155 19000834-6 2008 Our results suggest a model whereby attenuated interactions between CIN and hsp90 during ATP depletion enhance CIN-dependent cofilin dephosphorylation and consequent rod assembly, thereby providing a mechanism for the formation of pathological actin/cofilin aggregates during neurodegenerative energy flux. Adenosine Triphosphate 89-92 cofilin 1 Homo sapiens 125-132 19000834-6 2008 Our results suggest a model whereby attenuated interactions between CIN and hsp90 during ATP depletion enhance CIN-dependent cofilin dephosphorylation and consequent rod assembly, thereby providing a mechanism for the formation of pathological actin/cofilin aggregates during neurodegenerative energy flux. Adenosine Triphosphate 89-92 cofilin 1 Homo sapiens 250-257 18065447-8 2008 Moreover, ADF/cofilin fragmentation while modulating filament length keeps filaments in a high molar ratio of ATP- or ADP-P(i) versus ADP-bound subunits. Adenosine Triphosphate 110-113 cofilin 1 Homo sapiens 14-21 16738008-0 2006 Formation of actin-ADF/cofilin rods transiently retards decline of mitochondrial potential and ATP in stressed neurons. Adenosine Triphosphate 95-98 cofilin 1 Homo sapiens 23-30 12600310-5 2003 After filaments have aged by hydrolysis of their bound ATP and dissociation of the gamma phosphate, ADF/cofilin proteins promote debranching and depolymerization. Adenosine Triphosphate 55-58 cofilin 1 Homo sapiens 104-111 11812157-6 2002 Complexes between actin.ADP and ADF or cofilin associate with both barbed and pointed ends of filaments at similar rates (close to those of actin.ATP and much higher than those of actin.ADP). Adenosine Triphosphate 146-149 cofilin 1 Homo sapiens 39-46 11812157-8 2002 The major difference between the two proteins is that the nucleating activity of cofilin-actin.ADP complexes is twice that of ADF-actin.ADP complexes and this, in turn, is twice that of actin.ATP alone. Adenosine Triphosphate 192-195 cofilin 1 Homo sapiens 81-88 11271505-0 2000 The role of ATP, ADP and divalent cations in the formation of binary and ternary complexes of actin, cofilin and DNase I. Actin is the major cytoskeletal protein of virtually all eukaryotic cells. Adenosine Triphosphate 12-15 cofilin 1 Homo sapiens 101-108 11271505-5 2000 Preferential conditions for the formation of the binary actin-cofilin complex are: ADP-Mg2+ > or = ADP-Ca2+ >> ATP-Ca2+ approximately equals ATP-Mg2+ approximately equals ADP-No Me2+ approximately equals ATP-No Me2+. Adenosine Triphosphate 120-123 cofilin 1 Homo sapiens 62-69 11271505-8 2000 Finally, the conditions which favour the formation of a ternary complex of cofilin-actin-DNase I resemble the actin-DNase I, namely: ATP-Ca2+ approximately equals ADP-Ca2+ approximately equals ADP-Mg2+ approximately equals ATPMg2+ ADP (no Me2+) > ATP-(no Me2+). Adenosine Triphosphate 133-137 cofilin 1 Homo sapiens 75-82 10098971-6 1999 Cofilin greatly speeds up treadmilling, which requires ATP hydroysis, by increasing the rate constant of depolymerization. Adenosine Triphosphate 55-58 cofilin 1 Homo sapiens 0-7