scholarly journals Studies on interaction of oligoadenylates with proteins in vitro by MALDI-TOF mass spectrometry

2013 ◽  
Vol 29 (1) ◽  
pp. 42-48 ◽  
Author(s):  
S. M. Levchenko ◽  
A. V. Rebriev ◽  
V. V. Tkachuk ◽  
L. V. Dubey ◽  
I. Ya. Dubey ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof

Application of MALDI-TOF mass spectrometry for in vitro identification of wood decay polypores

2017 ◽  
Vol 47 (5) ◽  
pp. e12352 ◽  
Author(s):  
P. Pristaš ◽  
S. Kvasnová ◽  
S. Gáperová ◽  
T. Gašparcová ◽  
J. Gáper
Keyword(s):  
Mass Spectrometry ◽  
Wood Decay ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof

scholarly journals Interaction between Retinoschisin and Norrin: Physical or Functional Relationship?

2018 ◽  
Author(s):  
Dhandayuthapani Sudha ◽  
Subbulakshmi Chidambaram ◽  
Jayamuruga Pandian Arunachalam
Keyword(s):  
Mass Spectrometry ◽  
Functional Relationship ◽  
Direct Interaction ◽  
Physical Interaction ◽  
Knock Out ◽  
Functional Association ◽  
Norrie Disease ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof

ABSTRACTBackgroundRetinoschisis and Norrie disease are X-linked recessive retinal disorders caused by mutations in RS1 and NDP genes respectively. Both are likely to be monogenic and no locus heterogeneity has been reported. However, there are reports showing overlapping clinical features of Norrie disease and retinoschisis in a NDP knock-out mouse model and also the involvement of both the genes in retinoschisis patients. Yet, the exact molecular mechanism and relationship between the two disorders have still not been understood.ObjectiveIn this study, we aim to investigate the association between retinoschisin (RS1) and norrin (NDP) using in vitro and in silico approaches.MethodSpecific protein-protein interaction between RS1 and NDP was determined in human retina by co-immunoprecipitation assay and immunoblotting. The immunoprecipitated complexes of RS1 and NDP were analyzed using MALDI-TOF mass spectrometry to validate the findings. STRING database was used to explore the functional relationship.ResultsCo-immunoprecipitation and immunoblotting demonstrated lack of a direct interaction between RS1 and NDP. This was further substantiated by analyzing the immunoprecipitation complexes using MALDI-TOF mass spectrometry. STRING did not reveal any direct functional association between the two proteins.ConclusionWhile literature suggest the existence of digenic involvement of RS1 and NDP in the pathophysiology of retinoschisis and Norrie disease, our data provides evidence for lack of a physical interaction between the two proteins. However, we cannot exclude the possibility of an indirect functional association as our analyses point to MAP kinase signaling pathway, which is presumed to be the link between them.

scholarly journals Identifying Inhibitors of Inflammation: A Novel High-Throughput MALDI-TOF Screening Assay for Salt-Inducible Kinases (SIKs)

2017 ◽  
Vol 22 (10) ◽  
pp. 1193-1202 ◽  
Author(s):  
Rachel E. Heap ◽  
Anthony G. Hope ◽  
Lesley-Anne Pearson ◽  
Kathleen M. S. E. Reyskens ◽  
Stuart P. McElroy ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
High Throughput ◽  
High Speed ◽  
Kinase Assay ◽  
Label Free ◽  
Promising Alternative ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof ◽  
Free Data

Matrix-assisted laser desorption/ionization time-of-flight (MALDI TOF) mass spectrometry has become a promising alternative for high-throughput drug discovery as new instruments offer high speed, flexibility and sensitivity, and the ability to measure physiological substrates label free. Here we developed and applied high-throughput MALDI TOF mass spectrometry to identify inhibitors of the salt-inducible kinase (SIK) family, which are interesting drug targets in the field of inflammatory disease as they control production of the anti-inflammatory cytokine interleukin-10 (IL-10) in macrophages. Using peptide substrates in in vitro kinase assays, we can show that hit identification of the MALDI TOF kinase assay correlates with indirect ADP-Hunter kinase assays. Moreover, we can show that both techniques generate comparable IC50 data for a number of hit compounds and known inhibitors of SIK kinases. We further take these inhibitors to a fluorescence-based cellular assay using the SIK activity-dependent translocation of CRTC3 into the nucleus, thereby providing a complete assay pipeline for the identification of SIK kinase inhibitors in vitro and in cells. Our data demonstrate that MALDI TOF mass spectrometry is fully applicable to high-throughput kinase screening, providing label-free data comparable to that of current high-throughput fluorescence assays.

scholarly journals MALDI-TOF mass spectrometry methods for evaluation of in vitro aminoacyl tRNA production

RNA ◽  
2002 ◽  
Vol 8 (4) ◽  
pp. 542-547 ◽  
Author(s):  
E. JAMES PETERSSON ◽  
MONA SHAHGHOLI ◽  
HENRY A. LESTER ◽  
DENNIS A. DOUGHERTY
Keyword(s):  
Mass Spectrometry ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof

Use of MALDI-TOF mass spectrometry to explore the peptidome and proteome of in-vitro produced bovine embryos pre-exposed to oviduct fluid

2021 ◽  
Vol 21 (4) ◽  
pp. 100545
Author(s):  
Charles Banliat ◽  
Valérie Labas ◽  
Daniel Tomas ◽  
Ana-Paula Teixeira-Gomes ◽  
Benoît Guyonnet ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Bovine Embryos ◽  
Maldi Tof Mass Spectrometry ◽  
Maldi Tof ◽  
Oviduct Fluid
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