Proteome science plc

London, United Kingdom

Proteome science plc

London, United Kingdom
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Rigdova K.,University of Swansea | Wang Y.,University of Swansea | Ward M.,Proteome science Plc | Griffiths W.J.,University of Swansea
Biochemical and Biophysical Research Communications | Year: 2014

Here we report a new method for oxosteroid identification utilizing "tandem mass tag hydrazine" (TMTH) carbonyl-reactive derivatisation reagent. TMTH is a reagent with a chargeable tertiary amino group attached through a linker to a carbonyl-reactive hydrazine group. Thirty oxosteroids were analysed after derivatisation with TMTH by electrospray ionization mass spectrometry (ESI-MS) and were found to give high ion-currents compared to underivatised molecules. ESI-tandem mass spectrometry (MS/MS) analysis of the derivatives yielded characteristic fragmentation patterns with specific mass reporter ions derived from the TMT group. A shotgun ESI-MS method incorporating TMTH derivatisation was applied to a urine sample. © 2014 The Authors. Published by Elsevier Inc.


Patent
PROTEOME science PLC and King's College London | Date: 2013-02-27

Methods and compositions relating to Alzheimers disease are provided. Specifically, proteins that are differentially expressed in the Alzheimers disease state relative to their expression in the normal state are provided. Proteins associated with Alzheimers disease are identified and described. Methods of diagnosis of Alzheimers disease using the differentially expressed proteins are also provided, as are methods for the identification and therapeutic use of compounds for the prevention and treatment of Alzheimers disease.


Patent
King's College London and PROTEOME science PLC | Date: 2012-11-21

The present invention provides materials and methods relating to screening for compounds useful in the treatment of Alzheimers disease and related conditions. In particular, screening methods using tyrosine kinases are provided, as are methods relating to the role of tyrosine kinases as therapeutic targets.


Patent
Proteome science PLC and King's College London | Date: 2014-07-24

Methods of screening for candidate compounds capable of inhibiting activity of fyn in phosphorylating tau protein at Y394 or binding to fyn to inhibit interaction with tau protein at Y394, including determining whether, and optionally the extent, the candidate compounds have these capabilities under conditions where fyn has these capabilities in the absence of the candidate compound. Methods of screening for substances capable of promoting dephosphorylation of tau protein by a phosphatase at a site of tau protein including contacting a candidate substance, the tau protein and a phosphatase capable of dephosphorylating the tau protein under conditions where the phosphatase is capable of dephosphorylating the site in absence of the candidate substance, where the kinase is fyn; determining whether, and optionally the extent, the candidate substance promotes dephosphorylation of the tau protein at the site; and selecting the candidate substance which promotes dephosphorylation of the tau protein the sites.


Patent
PROTEOME science PLC and King's College London | Date: 2012-04-18

The present invention provides materials and methods relating to screening for compounds useful in the treatment of Alzheimers disease and related conditions. In particular, screening methods using tyrosine kinases are provided, as are methods relating to the role of tyrosine kinases as therapeutic targets.


Patent
PROTEOME science PLC and King's College London | Date: 2011-08-10

Methods and compositions relating to Alzheimers disease are provided. Specifically, proteins that are differentially expressed in the Alzheimers disease state relative to their expression in the normal state are provided. Proteins associated with Alzheimers disease are identified and described. Methods of diagnosis of Alzheimers disease using the differentially expressed proteins are also provided, as are methods for the identification and therapeutic use of compounds for the prevention and treatment of Alzheimers disease.


Patent
Proteome science plc and King's College London | Date: 2015-08-17

The present invention provides materials and methods relating to screening for compounds useful in the treatment of Alzheimers disease and related conditions. In particular, screening methods using tyrosine kinases are provided, as are methods relating to the role of tyrosine kinases as therapeutic targets.


Russell C.L.,Proteome science R&D GmbH & Co. KG | Russell C.L.,Proteome science plc
Journal of Alzheimer's disease : JAD | Year: 2014

The ability to detect and diagnose Alzheimer's disease (AD) early is an ever pressing issue, and the development of markers of disease progression that are able to distinguish AD patients from normal aging and patients with alternative forms of dementia, is at the center of the issue. Protein markers of disease, or biomarkers, can be used not only to monitor the progression of AD, but also allow identification of patients suitable for potential therapy, and the response to therapy to be monitored. Cerebrospinal fluid protein biomarkers are important in this early AD diagnosis, and three such biomarkers have been extensively studied and are reviewed here. In addition, post translational protein modifications of proteins important in AD pathology are also discussed. If additional biomarkers can be identified and thoroughly understood, potential therapeutic agents can be better designed, and the effects of therapeutic intervention on disease progression can be monitored.


McAlister G.C.,Harvard University | Huttlin E.L.,Harvard University | Haas W.,Harvard University | Ting L.,Harvard University | And 7 more authors.
Analytical Chemistry | Year: 2012

Quantitative mass spectrometry methods offer near-comprehensive proteome coverage; however, these methods still suffer with regards to sample throughput. Multiplex quantitation via isobaric chemical tags (e.g., TMT and iTRAQ) provides an avenue for mass spectrometry-based proteome quantitation experiments to move away from simple binary comparisons and toward greater parallelization. Herein, we demonstrate a straightforward method for immediately expanding the throughput of the TMT isobaric reagents from 6-plex to 8-plex. This method is based upon our ability to resolve the isotopic shift that results from substituting a 15N for a 13C. In an accommodation to the preferred fragmentation pathways of ETD, the TMT-127 and -129 reagents were recently modified such that a 13C was exchanged for a 15N. As a result of this substitution, the new TMT reporter ions are 6.32 mDa lighter. Even though the mass difference between these reporter ion isotopologues is incredibly small, modern high-resolution and mass accuracy analyzers can resolve these ions. On the basis of our ability to resolve and accurately measure the relative intensity of these isobaric reporter ions, we demonstrate that we are able to quantify across eight samples simultaneously by combining the 13C- and 15N-containing reporter ions. Considering the structure of the TMT reporter ion, we believe this work serves as a blueprint for expanding the multiplexing capacity of the TMT reagents to at least 10-plex and possibly up to 18-plex. © 2012 American Chemical Society.


Patent
PROTEOME science PLC | Date: 2010-07-28

A method of diagnosis of a transmissible spongiform encephalopathy (TSE) or the possibility thereof in a subject suspected of suffering from the TSE, which comprises determining a test amount of a polypeptide in a sample of body fluid taken from the subject, wherein the polypeptide is differentially contained in the body fluid of TSE-infcctcd subjects and non-TSE-infcctcd subjects, and is Cystatin C; and determining whether the test amount is consistent with a diagnosis of TSE.

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