Solution structure of the human Tax-interacting protein-1
Content Type Journal Article
Pages 329-334
DOI 10.1007/s10858-009-9361-8
Authors
Michael A. Durney, Harvard Medical School Molecular Medicine Laboratory and Macromolecular Crystallography Unit, Department of Medicine Boston MA 02215 USA
Gabriel Birrane, Harvard Medical School Molecular Medicine Laboratory and Macromolecular Crystallography Unit, Department of Medicine Boston MA 02215 USA
Clemens Anklin, Bruker BioSpin Corporation Billerica MA USA
Aditi Soni, Harvard Medical School Molecular Medicine Laboratory and Macromolecular Crystallography Unit, Department of Medicine Boston MA 02215 USA
John A. A. Ladias, Harvard Medical School Molecular Medicine Laboratory and Macromolecular Crystallography Unit, Department of Medicine Boston MA 02215 USA
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
J Struct Funct Genomics. 2011 Jul 23;
Authors: Eletsky A, Ruyechan WT, Xiao R, Acton TB, Montelione GT, Szyperski T
The solution NMR structure of protein MED25(391-543), comprising the activator interacting domain (ACID) of subunit 25 of the human mediator, is presented along with the measurement of...
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07-26-2011 09:30 PM
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
Solution NMR structure and dynamics of human apo-S100A1 protein.
J Struct Biol. 2011 Feb 2;
Authors: Nowakowski M, Jaremko L, Jaremko M, Zhukov I, Belczyk A, Bierzy?ski A, Ejchart A
S100A1 belongs to the EF-hand superfamily of calcium binding proteins. It is a representative of the S100 protein family based on amino acid sequence, three-dimensional structure, and biological function as a calcium signal transmitter. It is a homodimer of noncovalently bound subunits. S100A1, like most...
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[NMR paper] Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a muta
Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.
Related Articles Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.
Proteins. 2005 May 1;59(2):347-55
Authors: le Maire A, Weber T, Saunier S, Broutin I, Antignac C, Ducruix A, Dardel F
Human nephrocystin is a protein associated with juvenile NPH, an autosomal recessive, inherited kidney disease responsible for chronic renal failure in children. It...
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11-25-2010 08:21 PM
[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these...
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[NMR paper] NMR solution structure of type II human cellular retinoic acid binding protein: impli
NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Related Articles NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Biochemistry. 1998 Sep 15;37(37):12727-36
Authors: Wang L, Li Y, Abildgaard F, Markley JL, Yan H
The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances...
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[NMR paper] Structure of recombinant human parathyroid hormone in solution using multidimensional
Structure of recombinant human parathyroid hormone in solution using multidimensional NMR spectroscopy.
Related Articles Structure of recombinant human parathyroid hormone in solution using multidimensional NMR spectroscopy.
Biol Chem Hoppe Seyler. 1996 Mar;377(3):175-86
Authors: Gronwald W, Schomburg D, Harder MP, Mayer H, Paulsen J, Wingender E, Wray V
The solution structure of human parathyroid hormone, in the form of recombinant prolyl-hPTH(1-84), has been investigated by multidimensional NMR spectroscopy under conditions (aqueous...
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[NMR paper] Characterization of the three-dimensional solution structure of human profilin: 1H, 1
Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern.
Related Articles Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern.
Biochemistry. 1993 Dec 21;32(50):13818-29
Authors: Metzler WJ, Constantine KL, Friedrichs MS, Bell AJ, Ernst EG, Lavoie TB, Mueller L
Human profilin is a 15-kDa protein that plays a major role in the signaling pathway leading to cytoskeletal...
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Solution structure of the RBD1,2 domains from human nucleolin
Solution structure of the RBD1,2 domains from human nucleolin
Content Type Journal Article
DOI 10.1007/s10858-010-9412-1
Authors
Sengodagounder Arumugam, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA
M. Clarke Miller, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA
James Maliekal, University of Louisville JG Brown Cancer Center 505 South Hancock St. Louisville KY 40202 USA