PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 20926618-10 2010 Other nonmutually exclusive potential reasons for the cry1-L407F gain of function are the location of phenylalanine-407 close to three conserved tryptophans, which could change cry1"s photochemical properties, and stabilization of ATP binding, which could extend the lifetime of the signaling state of cry1. Adenosine Triphosphate 231-234 cryptochrome 1 Arabidopsis thaliana 54-58 20926618-10 2010 Other nonmutually exclusive potential reasons for the cry1-L407F gain of function are the location of phenylalanine-407 close to three conserved tryptophans, which could change cry1"s photochemical properties, and stabilization of ATP binding, which could extend the lifetime of the signaling state of cry1. Adenosine Triphosphate 231-234 cryptochrome 1 Arabidopsis thaliana 177-181 20926618-10 2010 Other nonmutually exclusive potential reasons for the cry1-L407F gain of function are the location of phenylalanine-407 close to three conserved tryptophans, which could change cry1"s photochemical properties, and stabilization of ATP binding, which could extend the lifetime of the signaling state of cry1. Adenosine Triphosphate 231-234 cryptochrome 1 Arabidopsis thaliana 177-181 17073458-3 2006 Recently, it was found that Arabidopsis cryptochrome 1 (AtCry1) binds ATP and exhibits autokinase activity that is simulated by blue light. Adenosine Triphosphate 70-73 cryptochrome 1 Arabidopsis thaliana 40-54 19327354-3 2009 Here we show in purified preparations of Arabidopsis cry1 that ATP binding induces conformational change independently of light and increases the amount and stability of light-induced flavin radical formation. Adenosine Triphosphate 63-66 cryptochrome 1 Arabidopsis thaliana 53-57 17073458-3 2006 Recently, it was found that Arabidopsis cryptochrome 1 (AtCry1) binds ATP and exhibits autokinase activity that is simulated by blue light. Adenosine Triphosphate 70-73 cryptochrome 1 Arabidopsis thaliana 56-62 12846824-3 2003 Here, we report a novel ATP binding and autophosphorylation activity associated with Arabidopsis cry1 protein purified from a baculovirus expression system. Adenosine Triphosphate 24-27 cryptochrome 1 Arabidopsis thaliana 97-101 15299148-7 2004 Previous in vitro experiments established that the photolyase-like domain of CRY-1 can bind Mg.ATP, and we observe a single molecule of an ATP analog bound in the aforementioned surface cavity, near the bound FAD cofactor. Adenosine Triphosphate 95-98 cryptochrome 1 Arabidopsis thaliana 77-82 15299148-7 2004 Previous in vitro experiments established that the photolyase-like domain of CRY-1 can bind Mg.ATP, and we observe a single molecule of an ATP analog bound in the aforementioned surface cavity, near the bound FAD cofactor. Adenosine Triphosphate 139-142 cryptochrome 1 Arabidopsis thaliana 77-82 24898692-3 2014 We have studied effects of pH and ATP on the functionally relevant photoreduction of the oxidized FAD cofactor to the semi-reduced FADH( ) radical in isolated Arabidopsis cryptochrome 1 by transient absorption spectroscopy on nanosecond to millisecond timescales. Adenosine Triphosphate 34-37 cryptochrome 1 Arabidopsis thaliana 171-185 32935701-0 2020 ATP binding promotes light-induced structural changes to the protein moiety of Arabidopsis cryptochrome 1. Adenosine Triphosphate 0-3 cryptochrome 1 Arabidopsis thaliana 91-105 32935701-3 2020 Studies have shown that cryptochrome 1 from Arabidopsis thaliana (AtCRY1) can bind ATP at its photolyase homology region (PHR), resulting in accumulation of FADH form. Adenosine Triphosphate 83-86 cryptochrome 1 Arabidopsis thaliana 24-38 32935701-3 2020 Studies have shown that cryptochrome 1 from Arabidopsis thaliana (AtCRY1) can bind ATP at its photolyase homology region (PHR), resulting in accumulation of FADH form. Adenosine Triphosphate 83-86 cryptochrome 1 Arabidopsis thaliana 66-72 32935701-4 2020 This study used light-induced difference Fourier transform infrared spectroscopy to investigate how ATP influences structural changes in AtCRY1-PHR during the photoreaction. Adenosine Triphosphate 100-103 cryptochrome 1 Arabidopsis thaliana 137-143 30044014-3 2018 The two Arabidopsis thaliana cryptochromes, cry1 and cry2, and the plant-type cryptochrome CPH1 from Chlamydomonas rheinhardtii bind ATP and other nucleotides. Adenosine Triphosphate 133-136 cryptochrome 1 Arabidopsis thaliana 44-48 28634231-0 2017 Hyperactivity of the Arabidopsis cryptochrome (cry1) L407F mutant is caused by a structural alteration close to the cry1 ATP-binding site. Adenosine Triphosphate 121-124 cryptochrome 1 Arabidopsis thaliana 47-51 28634231-0 2017 Hyperactivity of the Arabidopsis cryptochrome (cry1) L407F mutant is caused by a structural alteration close to the cry1 ATP-binding site. Adenosine Triphosphate 121-124 cryptochrome 1 Arabidopsis thaliana 116-120 28634231-5 2017 The previously characterized L407F mutant allele of Arabidopsis cry1 is biologically hyperactive and seems to mimic the ATP-bound state of cry1, but the reason for this phenotypic change is unclear. Adenosine Triphosphate 120-123 cryptochrome 1 Arabidopsis thaliana 64-68 28634231-5 2017 The previously characterized L407F mutant allele of Arabidopsis cry1 is biologically hyperactive and seems to mimic the ATP-bound state of cry1, but the reason for this phenotypic change is unclear. Adenosine Triphosphate 120-123 cryptochrome 1 Arabidopsis thaliana 139-143 28634231-6 2017 Here, we show that cry1L407F can still bind ATP, has less pronounced photoreduction and formation of FADH than wild-type cry1, and has a dark reversion rate 1.7 times lower than that of the wild type. Adenosine Triphosphate 44-47 cryptochrome 1 Arabidopsis thaliana 19-23 28634231-8 2017 Moreover, we show that ATP binds to cry1 in both the dark and the lit states. Adenosine Triphosphate 23-26 cryptochrome 1 Arabidopsis thaliana 36-40 28634231-10 2017 Finally, we show that a recently discovered chemical inhibitor of cry1, 3-bromo-7-nitroindazole, competes for ATP binding and thereby diminishes FADH formation, which demonstrates that both processes are important for cry1 function. Adenosine Triphosphate 110-113 cryptochrome 1 Arabidopsis thaliana 66-70 28634231-10 2017 Finally, we show that a recently discovered chemical inhibitor of cry1, 3-bromo-7-nitroindazole, competes for ATP binding and thereby diminishes FADH formation, which demonstrates that both processes are important for cry1 function. Adenosine Triphosphate 110-113 cryptochrome 1 Arabidopsis thaliana 219-223