[NMR paper] NMR Structure of Calmodulin Complexed to An N-terminally Acetylated ?-Synuclein Peptide.
NMR Structure of Calmodulin Complexed to An N-terminally Acetylated ?-Synuclein Peptide.
Related Articles NMR Structure of Calmodulin Complexed to An N-terminally Acetylated ?-Synuclein Peptide.
Biochemistry. 2013 Apr 22;
Authors: Gruschus JM, Yap TL, Pistolesi S, Maltsev AS, Lee JC
Abstract
Calmodulin (CaM) is a calcium binding protein that plays numerous roles in Ca-dependent cellular processes, including uptake and release of neurotransmitters in neurons. ?-Synuclein (?-syn), one of the most abundant proteins in central nervous system...
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[NMR paper] Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization.
PLoS One. 2013;8(1):e53487
Authors: ...
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[NMR paper] NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed wi
NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers.
Related Articles NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers.
Biochemistry. 2003 Apr 22;42(15):4333-48
Authors: Mercier P, Ferguson RE, Irving M, Corrie JE, Trentham DR, Sykes BD
The structure...
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[NMR paper] NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed
NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site.
Related Articles NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site.
Biochemistry. 2000 Dec 26;39(51):15860-9
Authors: Weber T, Schaffhausen B, Liu Y, Günther UL
The N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K) has a...
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[NMR paper] NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+
NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Related Articles NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.
Biochemistry. 1999 Sep 21;38(38):12320-32
Authors: Elshorst B, Hennig M, Försterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E
The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the...
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11-18-2010 08:31 PM
[NMR paper] NMR-derived three-dimensional solution structure of protein S complexed with calcium.
NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Related Articles NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Structure. 1994 Feb 15;2(2):107-22
Authors: Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M
BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is...
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[NMR paper] NMR-derived three-dimensional solution structure of protein S complexed with calcium.
NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Related Articles NMR-derived three-dimensional solution structure of protein S complexed with calcium.
Structure. 1994 Feb 15;2(2):107-22
Authors: Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M
BACKGROUND: Protein S is a developmentally-regulated Ca(2+)-binding protein of the soil bacterium Myxococcus xanthus. It functions by forming protective, multilayer spore surface assemblies which may additionally act as a cell-cell adhesive. Protein S is...
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08-22-2010 03:33 AM
[NMR paper] Triple-resonance multidimensional NMR study of calmodulin complexed with the binding
Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Related Articles Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Biochemistry. 1991 Jun 4;30(22):5498-504
Authors: Ikura M, Kay LE, Krinks M, Bax A
Heteronuclear 3D and 4D NMR experiments have been...
NMR Structure of Calmodulin Complexed to an N-TerminallyAcetylated ?-Synuclein Peptide
Linear Mode
