prosper.erc.monash.edu.au
PROSPER: Protease substrate specificity webserver
https://prosper.erc.monash.edu.au/help.html
The PROSPER webserver can be accessed at https:/ prosper.erc.monash.edu.au. The web interface is fairly straightforward to use: the user only needs to input the one-letter FASTA format of the query sequence. A typical task for a query sequence with 500 residues long will roughly take 8-12 minutes. Once the prediction task is completed, the results will be returned to the screen. First input the query sequence in the FASTA format such as:. In the result webpage, its first part is the input sequence, with ...
prosper.erc.monash.edu.au
PROSPER: Protease substrate specificity webserver
https://prosper.erc.monash.edu.au/webserver.html
PROSPER is an integrated feature-based webserver for. Prediction of protease substrates and their cleavage sites for twenty-four different protease types, covering four major protease families- Aspartic (A), Cysteine (C), Metallo (M) and Serine (S). You have been redirected from. Http:/ lightning.med.monash.edu.au/PROSPER. To this new PROSPER server. Kindly update your bookmarks to: https:/ prosper.erc.monash.edu.au. ID: (optional, your given name of the sequence). Song J, Tan H, Perry AJ, Akutsu T, Webb...
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https://cycling4cancer.wordpress.com/the-journey
CYCLING 45 000KM ACROSS THE WORLD IN AID OF INTERNATIONAL CANCER RESEARCH. Weekly Camden Narellan Advertiser Articles. By the time I rode into my hometown in Sydney I had covered a distance greater than the length of the equator! 65 comments on “ Route. January 15, 2012 at 8:32 pm. First words on this blog, first comment but many will follow to accompany you along this fabulous trip! Such a great project which inspires a lot! All the best for this amazing experience! January 25, 2012 at 11:42 am. All the...
prosper.erc.monash.edu.au
PROSPER: Protease substrate specificity webserver
https://prosper.erc.monash.edu.au/downloads.html
The following table describes the statistics of the substrate datasets we have extracted from MEROPS to develop the PROSPER tool for predicting cleavage sites of multiple proteases. Each substrate dataset can be downloaded by clicking the hyperlink associated with each MEROPS ID of protease family in this table. All of these substrate data were mainly derived from the MEROPS. Database, an online information resource for proteases and their inhibitors (Rawlings. Protease subfamily (MEROPS ID). 2) The seco...
prosper.erc.monash.edu.au
PROSPER: Protease substrate specificity webserver
https://prosper.erc.monash.edu.au/gallery.html
We have mapped the substrates deposited in MEROPS onto the structural database PDB and obtained a subset of protein substrates with experimentally solved 3D structures. The subset of these substrate PDB structures for the major proteases families are listed in the following. Protease A01.001: Pepsin A (292 entries). Protease A01.009: Cathepsin D (122 entries). Protease A01.010: Cathepsin E (113 entries). Protease A01.012: Rhizopuspepsin (192 entries). Protease A01.016: Aspergillopepsin I (128 entries).
prosper.erc.monash.edu.au
PROSPER: Protease substrate specificity webserver
https://prosper.erc.monash.edu.au/links.html
This table provides detailed links and descriptions with respect to previously developed servers or softwares for protease substrate cleavage sites prediction. Note that among them, three are general cleavage site prediction servers (PeptideCutter, PoPS and SitePrediction), the others are family-specific servers that were specifically designed to model and predict the substrate specificity for a particular protease, such as PEPS, CasPredictor, GraBCas, CASVM and Cascleave. Predict Caspase cleavage sites.
prosper.erc.monash.edu.au
PROSPER: Protease substrate specificity webserver
https://prosper.erc.monash.edu.au/home.html
Proteases are enzymes that hydrolyze protein peptide bonds at specific recognition sites in their substrates and play a central role in "life and death" processes, such as neural, endocrine and cardiovascular signalling, digestion, degrading misfolded or unwanted proteins, immunity, cell division, and apoptosis. To address this problem, we developed PROSPER (PROtease Specificity Prediction servER). Identification of protease cleavage sites.
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