MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Alt a 1 from Alternaria interacts with PR5 thaumatin-like proteins. Alt a 1 from Alternaria interacts with PR5 thaumatin-like proteins. FEBS Lett. (0014-5793) 2014 imex curation Gómez-Casado C., Murua-García A., Garrido-Arandia M., González-Melendi P., Sánchez-Monge R., Barber D., Pacios L.F., Díaz-Perales A. araceli.diaz@upm.es 02-Apr-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot araceli.diaz@upm.es Accepted 2014-FEB-21 by LUANA 2014 imex curation Alt a 1 from Alternaria interacts with PR5 thaumatin-like proteins. Alt a 1 from Alternaria interacts with PR5 thaumatin-like proteins. FEBS Lett. (0014-5793) 2014 imex curation Gómez-Casado C., Murua-García A., Garrido-Arandia M., González-Melendi P., Sánchez-Monge R., Barber D., Pacios L.F., Díaz-Perales A. araceli.diaz@upm.es 02-Apr-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down ms participant Identification by mass spectrometry ms participant araceli.diaz@upm.es Accepted 2014-FEB-21 by LUANA 2014 imex curation b6cqt3_9rosa Pru p 2.02 protein protein prunus dulcis x prunus persica Prunus dulcis x Prunus persica MMKTLVAVLSLSLTLLSFGGAHAATMSFKNNCPYTVWPASFGNPQLSTTGFELASQASFQLDTPVPWSGRFWARTRCSTDASGKFVCETADCDSGQLMCNGKTGIPPATLAEFTIAAGGGQDFYDVSLVDGFNLPMSVTPQGGTGTCKMGSCAANVNLVCPSELQKIGSDGSVVACLSACVKFGEPQYCCTPPQETKEKCPPTNYSQIFHEQCPDAYSYAFDDNKGLFTCSGGPNYLITFCP F88D6316FC1E6DBC alta1_altal Major allergen Alt a 1 ALTA1 protein protein altal Alternaria alternata MQFTTIASLFAAAGLAAAAPLESRQDTASCPVTTEGDYVWKISEFYGRKPEGTYYNSLGFNIKATNGGTLDFTCSAQADKLEDHKWYSCGENSFMDFSFDSDRSGLLLKQKVSDDITYVATATLPNYCRAGGNGPKDFVCQGVADAYITLVTLPKSS AAC20D0819198246 i3rtu5_musac Thau protein protein musac Musa acuminata MVSSTILSFLLFALLLALSRAVTFEIVNGCPFTVWPAAVPGGGLQLDQGQTWVLDVNPGTTGGRIWARTGCSFDGSGSGSCQTGDCGGVLDCKGYGSPPNTVAEFAVGQFNNFDVSLVDGFNVPMEFGSCRAIRCSADINGRCPAELRTPGGCNNPCTVFKTDEYCCTSGSCGPTTYSKFFKSNCPDAYSYPKDDATSTFTCPGNGDYKVIFCPSVSSLPADGYPTRFGRIAVSFVIPKASGT 81024CFE6D581164 tlp_actde Thaumatin-like protein tlp protein protein actde Actinidia deliciosa MSTFKSLSLSALLFIAFLFTCARGATFNIINNCPFTVWAAAVPGGGKRLDRGQNWIINPGAGTKGARVWPRTGCNFDGAGRGKCQTGDCNGLLQCQAFGQPPNTLAEYALNQFNNLDFFDISLVDGFNVAMEFSPTSGGCTRGIKCTADINGQCPNELRAPGGCNNPCTVFKTDQYCCNSGNCGLTNFSKFFKDRCPDAYSYPKDDQTSTFTCPAGTNYKVVFCP 229DABF722E7B961 alta1-tlp-2 1 PR5-thaumatin- like protein 6 western blot western blot Immuno blot Immuno blot western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey purified purified Alt a 1 4 western blot western blot Immuno blot Immuno blot western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified direct interaction direct interaction f2a Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5). alta1-tlp-1 2 Alt a 1 4 predetermined predetermined participant predetermined ms participant Identification by mass spectrometry ms participant unspecified role unspecified role bait bait purified purified PR5-thaumatin- like protein 6 ms participant Identification by mass spectrometry ms participant ms participant Identification by mass spectrometry ms participant unspecified role unspecified role prey prey cell lysate cell lysate physical association physical association f2a Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5). alta1-tlp-3 1 peach PR5 3 western blot western blot Immuno blot Immuno blot western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey purified purified Alt a 1 4 western blot western blot Immuno blot Immuno blot western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified direct interaction direct interaction f2a Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5). alta1-pru_p_2_02 1 banana PR5 5 western blot western blot Immuno blot Immuno blot western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey purified purified Alt a 1 4 western blot western blot Immuno blot Immuno blot western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified direct interaction direct interaction f2a Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5). tlp-alta1 1 Alt a 1 4 ms participant Identification by mass spectrometry ms participant western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey purified purified PR5-thaumatin- like protein 6 western blot western blot Immuno blot Immuno blot western blot western blot Immuno blot Immuno blot unspecified role unspecified role bait bait purified purified direct interaction direct interaction f2b Pull down assays were carried out to find potential plant receptors for Alt a 1. Dynabeads® M-280 Tosylactivated (Invitrogen, Oslo, Norway) were coated with Alt a 1 (Bial 172 Aristegui, Bilbao Spain) and incubated with a kiwifruit protein extract (Figure 2A). A principal band around 26 kDa was observed when the immunoprecipitated proteins were separated by SDS-PAGE and stained with Coomassie. This band was identified by mass fingerprinting as the 175 PR5-thaumatin like protein (P81370). The accuracy of the retained protein identification was further supported by immunodetection using specific polyclonal antibodies against PR5 (Anti- PR5).