Publication date: 16 February 2016 Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1
Author(s): Adak N. Karamafrooz, Jonggul Kim, Geoffrey Li, Sanford M. Simon, Susan S. Taylor, Gianluigi Veglia
[NMR paper] Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
FEBS Lett. 2014 Apr 3;
Authors: Sommer LA, Dames SA
...
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[NMR paper] NMR-based functional profiling of RASopathies and oncogenic RAS mutations.
NMR-based functional profiling of RASopathies and oncogenic RAS mutations.
Related Articles NMR-based functional profiling of RASopathies and oncogenic RAS mutations.
Proc Natl Acad Sci U S A. 2013 Mar 4;
Authors: Smith MJ, Neel BG, Ikura M
Abstract
Defects in the RAS small G protein or its associated network of regulatory proteins that disrupt GTPase cycling are a major cause of cancer and developmental RASopathy disorders. Lack of robust functional assays has been a major hurdle in RAS pathway-targeted drug development. We used NMR to...
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[NMR paper] Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (3
Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (31)P NMR spectroscopy.
Related Articles Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (31)P NMR spectroscopy.
Biochemistry. 2002 May 14;41(19):5968-77
Authors: Seifert MH, Breitenlechner CB, Bossemeyer D, Huber R, Holak TA, Engh RA
Cell signaling pathways rely on phosphotransfer reactions that are catalyzed by protein kinases. The protein kinases themselves are typically regulated by phosphorylation and concurrent structural...
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[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro
Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
J Pept Res. 1997 Mar;49(3):210-20
Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS
Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...
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08-22-2010 03:31 PM
[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro
Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics.
J Pept Res. 1997 Mar;49(3):210-20
Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS
Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...
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08-22-2010 03:03 PM
[NMR paper] Tumor suppressor p16INK4A: structural characterization of wild-type and mutant protei
Tumor suppressor p16INK4A: structural characterization of wild-type and mutant proteins by NMR and circular dichroism.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Tumor suppressor p16INK4A: structural characterization of wild-type and mutant proteins by NMR and circular dichroism.
Biochemistry. 1996 Jul 23;35(29):9475-87
Authors: Tevelev A, Byeon IJ, Selby T, Ericson K, Kim HJ, Kraynov V, Tsai MD
The tumor suppressor p16INK4A with eight N-terminal amino acids deleted (p16/delta 1-8)...
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[NMR paper] Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequen
Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and structure of cGMP-dependent protein kinase I alpha-(546-576)-peptide amide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and...
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[NMR paper] Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequen
Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and structure of cGMP-dependent protein kinase I alpha-(546-576)-peptide amide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Stimulation of cGMP-dependent protein kinase I alpha by a peptide from its own sequence. An investigation by enzymology, circular dichroism and 1H NMR of the activity and...
NMR Structural/Functional Characterization of an Oncogenic Mutant of cAMP-Dependent Protein Kinase A: PRKACA-DNAJB1
Linear Mode
