Biomolecular NMR experts in Germany have discovered how the U2AF protein facilitates the process of splicing used by cells to make the correct template for RNA transcription and the subsequent expression of proteins.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
NMR solution structure of human VRK1 reveals the C-terminal tail essential for structural stability and autocatalytic activity.
J Biol Chem. 2011 May 3;
Authors: Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS
Vaccinia-related kinase 1 (VRK1) is one of the mitotic kinases which play important roles in cell cycle, nuclear condensation and transcription regulation. Kinase...
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[NMR paper] Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 a
Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 as explained by (1)H, (15)N and (13)C NMR chemical shifts and secondary structure analysis.
Related Articles Mechanisms for the enhanced thermal stability of a mutant of transcription factor 1 as explained by (1)H, (15)N and (13)C NMR chemical shifts and secondary structure analysis.
Biochim Biophys Acta. 2000 Mar 16;1478(1):113-24
Authors: Vu HM, Liu W, Grove A, Geiduschek EP, Kearns DR
A variant of the bacteriophage SPO1-encoded transcription factor 1 (TF1)...
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[NMR paper] New perceptions of transcription factor properties from NMR.
New perceptions of transcription factor properties from NMR.
Related Articles New perceptions of transcription factor properties from NMR.
Biochem Cell Biol. 1998;76(2-3):368-78
Authors: Bagby S, Arrowsmith CH, Ikura M
The complementarity of NMR and X-ray crystallography for biomacromolecular studies has been particularly evident in analysis of transcription factor structures and interactions. While X-ray crystallography can be used to tackle relatively complicated structural problems including multicomponent (three and higher) complexes, NMR...
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[NMR paper] The Aspergillus nidulans transcription factor AlcR forms a stable complex with its ha
The Aspergillus nidulans transcription factor AlcR forms a stable complex with its half-site DNA: a NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The Aspergillus nidulans transcription factor AlcR forms a stable complex with its half-site DNA: a NMR study.
FEBS Lett. 1997 May 19;408(2):235-40
Authors: Cerdan R, Collin D, Lenouvel F, Felenbok B, Guittet E
The Aspergillus nidulans transcription factor AlcR is shown by NMR and gel retardation assay to form a...
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[NMR paper] The Aspergillus nidulans transcription factor AlcR forms a stable complex with its ha
The Aspergillus nidulans transcription factor AlcR forms a stable complex with its half-site DNA: a NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The Aspergillus nidulans transcription factor AlcR forms a stable complex with its half-site DNA: a NMR study.
FEBS Lett. 1997 May 19;408(2):235-40
Authors: Cerdan R, Collin D, Lenouvel F, Felenbok B, Guittet E
The Aspergillus nidulans transcription factor AlcR is shown by NMR and gel retardation assay to form a...
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[NMR paper] The dimerization stability of the HLH-LZ transcription protein family is modulated by
The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers: a CD and NMR study of TFEB and c-Myc.
Related Articles The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers: a CD and NMR study of TFEB and c-Myc.
Biochemistry. 1994 Sep 20;33(37):11296-306
Authors: Muhle-Goll C, Gibson T, Schuck P, Schubert D, Nalis D, Nilges M, Pastore A
In the HLH-LZ protein family, the helix-loop-helix DNA-binding dimerization domain is followed in the sequence by a...
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[NMR paper] A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by sel
A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by selective 2H-labeling. Complete assignment and structural analysis of the aromatic resonances for a 22-kDa homodimer.
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 A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by selective 2H-labeling. Complete assignment and structural analysis of the aromatic resonances for a 22-kDa homodimer.
Eur J...
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Solid-State NMR Reveals Structural and Dynamical Properties of a Membrane Protein
http://pubs.acs.org/cgi-bin/abstract.cgi/jacsat/2007/129/i21/abs/ja069028m.html
Solid-State NMR Reveals Structural and Dynamical Properties of a Membrane-Anchored Electron-Carrier Protein, Cytochrome b<sub>5</sub>
<aui auinm="Durr, U. H. N."> <aui auinm="Yamamoto, K."> <aui auinm="Im, S.-C."> <aui auinm="Waskell, L."> <aui auinm="Ramamoorthy, A."> <aug><aul></aul></aug></aui></aui></aui></aui></aui> <au>Ulrich H. N. Dürr,</au> <au>Kazutoshi Yamamoto,</au><au>Sang-Choul Im,</au><au>Lucy Waskell,and </au><au>Ayyalusamy Ramamoorthy*</au>
*ramamoor@umich.edu
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