In order to enable an iCal export link, your account needs to have an API key created. This key enables other applications to access data from within Indico even when you are neither using nor logged into the Indico system yourself with the link provided. Once created, you can manage your key at any time by going to 'My Profile' and looking under the tab entitled 'HTTP API'. Further information about HTTP API keys can be found in the Indico documentation.
Additionally to having an API key associated with your account, exporting private event information requires the usage of a persistent signature. This enables API URLs which do not expire after a few minutes so while the setting is active, anyone in possession of the link provided can access the information. Due to this, it is extremely important that you keep these links private and for your use only. If you think someone else may have acquired access to a link using this key in the future, you must immediately create a new key pair on the 'My Profile' page under the 'HTTP API' and update the iCalendar links afterwards.
Permanent link for public information only:
Permanent link for all public and protected information:
Mainly structural but also some functional insights into the unique CBS–CP12 fusion protein family in cyanobacteria
Cyanobacteria are important photosynthetic organisms inhabiting a range of dynamic environments. This phylum is distinctive among photosynthetic organisms in containing genes encoding uncharacterized cystathionine β-synthase (CBS)–chloroplast protein (CP12) fusion proteins. These consist of two domains, each recognized as stand-alone photosynthetic regulators with different functions described in cyanobacteria (CP12) and plants (CP12 and CBSX). In our study focusing on a CBS–CP12 from Microcystis aeruginosa, we reveal that the domain fusion led to the formation of a hexameric protein. We show that the CP12 domain contains an ordered, previously structurally uncharacterized N-terminal region. We provide evidence that CBS–CP12, while combining properties of both regulatory domains, behaves different from CP12 and plant CBSX. It does not form a ternary complex with phosphoribulokinase (PRK) and glyceraldehyde-3-phosphate dehydrogenase. Instead, CBS–CP12 decreases the activity of PRK in an AMP-dependent manner. We propose that the novel domain architecture and oligomeric state of CBS–CP12 expand its regulatory function beyond those of CP12 in cyanobacteria.
1) Hackenberg C., Hakanpää J., Cai F., Antonyuk S., Eigner C., Meissner S., Laitaoja M., Jänis J., Kerfeld C.A., Dittmann E., Lamzin V.S. (2018) Proc Natl Acad Sci 115 7141-7146.