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Saturday morning and it’s raining? Time to course of some UVPD data! This time, nonetheless, I am up early on a Saturday cause I’ve bought the Raw data recordsdata from it! Now you’ll be able to have them too! They’re at Proteome Xchange underneath PXD003904. So it’s one other Science Saturday! Take a look at that image! Usually we’re simply worrying about b/y ions. For these of you who’ve bribed pals with superior engineering degrees to help you set this up in your instruments, what do you get in your troubles? Now you get to fret about b ions, y ions, a ions, x ions, c ions AND z ions in each MS/MS spectra! This seems to be like MASSIVELY more search area. Just what y’all needed, proper? Okay — so I am going to start out with just one file from this dataset. All of the fans are working. DISCLAIMER: This might not be the neatest technique to run this. I am half-awake, considerably annoyed, and not a professional scientist. That is how I set it up, and I’m super impressed with the information. Used a standard Uniprot database (from 2011, LOL!) used a tight mass tolerance cutoff after which allowed SequestHT to have equal weighting on all the fragment ions.
Within the pursuits of transparency, eLife consists of the editorial choice letter and accompanying author responses. A frivolously edited version of the letter despatched to the authors after peer review is proven, indicating the most substantive considerations; minor comments are not usually included. Thanks for sending your article entitled “A novel pH-dependent membrane peptide that binds to EphA2 and inhibits cell migration” for peer overview at eLife. Your article is being evaluated by three peer reviewers, and the evaluation is being overseen by a Reviewing Editor and Jonathan Cooper as the Senior Editor. This manuscript describes an intensive investigation of a novel peptide that inhibits migration of malignant cells by its binding to the transmembrane section (TMS) of the receptor tyrosine kinase EphA2. Thorough biophysical research of peptide structure, membrane integration and binding are juxtaposed with a comprehensive cell biological evaluation of the results the pH-dependent TYPE2 binding to EphA2. The invention of a peptide that can be utilized to activate EphA2 by means of an unconventional mechanism is interesting for potential therapeutic purposes.
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