Journal Title
Title of Journal: Biomol NMR Assign
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Abbravation: Biomolecular NMR Assignments
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Publisher
Springer Netherlands
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Authors: Navratna Vajpai AnneKathrin Schott Martin Vogtherr Alexander L Breeze
Publish Date: 2013/01/17
Volume: 8, Issue: 1, Pages: 85-88
Abstract
Members of the fibroblast growth factor receptor tyrosine kinase family FGFR1–4 play an important role in many signalling cascades Although tightly regulated aberrant activity of these enzymes may lead to or become features of disease pathologies including cancer FGFR isoforms have been the subject of drug discovery programmes with a number of kinasedomain inhibitors in preclinical and clinical development Here we present the first 83 complete backbone resonance assignments of apoFGFR1 kinase
Keywords:
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Other Papers In This Journal:
- Letter to the Editor: Resonance assignment of SlyD from E. coli
- A complete NMR spectral assignment of the lipid-free mouse apolipoprotein A-I (apoAI) C-terminal truncation mutant, apoAI(1-216)
- 1 H, 13 C, 15 N resonance assignment of the chitin-binding protein CBP21 from Serratia marcescens
- Backbone nuclear magnetic resonance assignment of human deoxyuridine 5′-triphosphate nucleotidohydrolase (dUTPase)
- 1 H, 13 C, and 15 N assignment of the muscular LIM protein MLP/CRP3
- Backbone and sidechain 1 H, 13 C and 15 N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid
- 1 H, 13 C and 15 N assignment of the C-terminal domain of GNA2132 from Neisseria meningitidis
- 1 H, 13 C, 15 N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the Hv GR-RBP1 protein involved in the regulation of barley ( Hordeum vulgare L.) senescence
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