#Findy sign license
Typically the way that we prove our identity in order to be given the right to do something is still done with plastic and paper, such as using a driver’s license as a personal ID when picking up a parcel. For example, my driver’s license sits with the Finnish authorities, my banking data is with my bank and my shopping data is with supermarket loyalty programmes. Today our data is distributed in many, many different places. I would rather consider this as verified data sharing from a broader perspective. Ville says: “Identity is just one small part of Findy. It is hoped that the establishment of the Findy network will create a robust framework for sharing reliable data digitally in Finland.
#Findy sign Offline
Currently, verifying the validity of online data in terms of its authenticity of origin and integrity of content in the same way as can be achieved offline remains a time consuming and inefficient process. A self-sovereign individual is able to share their credentials wherever they like without requiring permission from a third party.
The concept of self-sovereign identity relates to an individual or company maintaining control of all of the credentials used to establish their own digital identity. The reason for the local dimension is that we needed to establish trust from the ground up instead of bringing in a global system to do the same,” adds Ville. We also wanted to make sure that we have uniform architecture with other similar initiatives globally so that we can ultimately create interoperability. The idea was to build a similar network but with local governance tied to local laws, local trust systems and local regulations. “Therefore we took most of the principles of these global self-sovereign identity data networks and transferred them to a local Finnish setting. Delivering these requirements from global organisations and global networks creates a huge challenge.”
We are not able to really use data from global networks unless we have a governing rule book and contractual framework that guarantees the source of that data. At that time, after discussing the feasibility of joining international self-sovereign identity network initiatives, we quickly realised that global networks face challenges when it comes to scaling them to the local level. Ville Sointu, Head of Emerging Technology at Nordea, says: “Findy began in 2018 and has existed as a consortium project from then on. The Findy network aims to go live in 2022, with widespread adoption in Finland occurring during 2023. Findy is governed in collaboration by the consortium members and a formal co-operative was established in May 2021, resulting in Findy becoming a legal entity. Thus, this study demonstrates the direct interaction between the DYRK1A kinase domain and FINDY, paving the way for structural determination of the complex.The Findy (Finnish Hyperledger Indy) network is owned by a non-profit group of members from both the public and private sectors that has grown to include Nordea, OP Bank, the Finnish Tax Administration, Kela (the Social Insurance Institution of Finland), Nixu, Finnish Post, TietoEVRY and the Vastuu Group. The eluate contained FINDY with the ratio of FINDY to DYRK1A protein being 0.15 in quadruplicate experiments. The amount of FINDY in the elution fraction was measured by UV absorbance specific for FINDY.
The cell pellets were gently extracted on ice and subjected to immobilized-metal affinity chromatography. The DYRK1A kinase domain was expressed as a fusion protein with a hexahistidine tag and ZZ-domain (His-ZZ-DYRK1A) at 6 ☌ by using a cold shock induction system in Escherichia coli cells. In this study, we successfully expressed and purified the kinase domain of DYRK1A in complex with FINDY. Although evidence has suggested that FINDY targets the ATP-binding pocket of DYRK1A, it remains elusive as to whether the DYRK1A kinase domain could be purified as a complex with FINDY. In the previous study, we identified a small molecule, designated as FINDY, that selectively inhibits the folding intermediate of DYRK1A. Once the folding process of DYRK1A has completed, it can no longer catalyzes the intramolecular reaction, suggesting that a transitional intermediate state that catalyzes the autophosphorylation exists. DYRK1A also phosphorylates its own residues on key elements intramolecularly to activate and stabilize itself during the folding process. The kinase DYRK1A phosphorylates substrate proteins that are involved in the progression of many diseases.
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