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Our recent work on predicting the #cancer driver #mutations combining the evolutionary information and protein language model (#plm) is out in Biorxiv.
biorxiv.org/content/10.1101/…
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Spatial proteomics in the context of #protein #modifications, #structure #function and #dynamics. Visit @Pathmanaban_'s poster this evening at the #BSPREUPA2023 Congress.
18 Jul 2023
Working in #spatial #proteomics?
Like to know how the post-translational modifications (#ptms) of #proteins varies between and within #tissue types?
Wondering how does that compare with the protein #behavior?
Find the answers at my poster (# 152) in #BSPREUPA2023 conference.
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Bio2Byte retweeted
6 Jun 2023
At #ASMS2023 and interested in Post-translational modifications of proteins? Feel free to join me this afternoon where I will be talking about my recent work on #tissue specific #PTM maps in #human #proteome. Especially on tissue specific protein #phosphorylation.
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Registrations are open! Check the link below. #Challenges and #opportunities in #AI based research in #hospitals.
21 Sep 2022
🔥Join us on October 6th🆓Register now!👉insightz.io/content/275/icit…
🖥 Wim Vranken will present the TumorScope project, which strives to overcome the amount, complexity, & protection of health-related data & to stimulate innovation in the #AI-driven interpretation of #patientdata.
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Hello #ECCB2022. Don't forget to check Sophie's poster this evening. Sophie will present her poster on "Using #AlphaFold2-generated #structural information to improve detection of #evolutionary adaptations in #proteins".
Poster number: P150-T
Track: Genomes
@ECCBinfo
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At #ECCB2022? Check @GavaldaGarcia's poster P181-M.
Jose from our group will present ConforMine, a predictor of protein #Conformational
Variability from amino acid #sequence. His poster features an explanation of both the #biophysical basis and the estimator for this metric.
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Hello #ECCB2022, In today's Session#1 under #ELIXIR @ELIXIREurope track, Wim Vranken will be talking about the resources and synergies between three ELIXIR communities; #proteomics, Intrinsically disordered proteins(#IDPs) and 3D-#Bioinfo at Auditorium Anna Tramontano at 10 AM.
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#Scop3P an @ELIXIRnodeBE service developed by @Pathmanaban_ in collaboration with @compomics, links human phosphorylation sites with protein structures and biophysical characteristics. Check the link below and give it a try! Feedbacks are welcome.
12 Sep 2022
📢Scop3P provides a unique and powerful resource for researchers to explore and understand the impact of phospho-sites on human protein structure and function.
✅Why not try it out? bit.ly/3Ca31HE 🔗
#bioinformatics #openscience #opensource #DataScience @ResearchSoft
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Another interesting perspective on highly dynamic and/or structurally ambiguous behavior of protein regions and the challenges involved in describing these ambiguous regions from the biophysical aspects.
9 Aug 2022
We're glad to share our latest publication on the challenges in describing the conformation and dynamics of proteins with ambiguous behavior, authored among others by @JoelRockM @LazTamas @GavaldaGarcia @KTzavella @Pathmanaban_ @Grau_Isel and @Wim_Vranken:
frontiersin.org/articles/10.…
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RNAct conference tailoring RNA binding proteins and RNA targeting. September 14 and 15 in Valencia, Spain. Register here: rnact.eu/FinalConference/#re…
9 Aug 2022
Protein-RNA interactions are essential - the RNAct MSCA-ITN conference (14-15/09/22, Valencia, Spain), focusses on how proteins bind RNA, and how we can tailor RNA binding proteins for synthetic biology and biosensor development - register at rnact.eu/FinalConference/! @eu_rnact
Bio2Byte retweeted
29 Jul 2022
Using the wealth of available phospho-proteomics #MassSpec data, the @compomics & @Bio2Byte labs demonstrate the advantage of data reprocessing for a more reliable & comprehensive view of proteome-wide P-sites. pubs.acs.org/doi/10.1021/acs…
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Our recent work shows an interesting view on the reliability of #protein #phosphorylation sites from other gold standard resources when compared to re-processed data from #Scop3p. Also shows their possible impact on #structures, functional #domains and #biophysical properties.
9 Jul 2022
Are you working on #protein #phosphorylations (#PTMs)? Ever wondered where these modifications are occurring on protein #structures and how that would affect their biophysical properties, structural transitions and #mutations?
Then this is for you!
pubs.acs.org/doi/10.1021/acs…
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Workshop on AI based solutions for health care. Together with @imec_smit. More details in the thread.
18 May 2022
What are challenges around the #development and #implementation of clinical #AI solutions? 🏥
SMIT researcher Lawrence Van den Bogaert will present on #AI for #healthcare on the 15th of June.
Registration link : bit.ly/TumorScope
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Excellent work from one of our PhD student @Pathmanaban_ showing how re-processing of public #proteomics data can help identify reliable P-sites and the possible dynamics involved in protein phosphorylation.
10 Mar 2022
We present a large scale integrated approach to understand the #human phosphosites and phosphoproteins by placing them in a variety of possible contexts such as #sequence, #structure, #disorderedness and #biophysical properties.
biorxiv.org/content/10.1101/…
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Bio2Byte retweeted
23 Jul 2021
This will change the history of structural biology research. Great effort from @DeepMind @uniprot @PDBeurope.
A historic moment in the world of molecular structural research. #AlphaFold structure predictions for 22 species made freely available by @deepmind, access through @uniprot and @PDBeurope. Learn more at insideuniprot.blogspot.com/
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!!! We are hiring !!!
Two open positions (PhD and a software developer) available immediately to work on the relation between post translational modifications (PTMs), protein dynamics and cellular localization of proteins.
Check the link for more:
bio2byte.be/opportunities
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Bio2Byte retweeted
14 Dec 2020
The 2nd issue of the #RNAct Newsletter is online! Read it online at rnact.eu/newsletter/ and make sure to subscribe to receive future updates. We hope you enjoy the reading!
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