[NMR paper] Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network.
Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network.
Related ArticlesSolution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network.
J Struct Funct Genomics. 2014 Jun 19;
Authors: Xu X, Pulavarti SV, Eletsky A, Huang YJ, Acton TB, Xiao R, Everett JK, Montelione GT, Szyperski T
Abstract
High-quality solution NMR structures of three homeodomains from human proteins ALX4, ZHX1 and CASP8AP2 were solved. These domains were chosen as targets of a biomedical theme project pursued by the Northeast Structural Genomics Consortium. This project focuses on increasing the structural coverage of human proteins associated with cancer.
PMID: 24941917 [PubMed - as supplied by publisher]
[NMR paper] NMR Structural Studies of Human Cellular Prion Proteins.
NMR Structural Studies of Human Cellular Prion Proteins.
Related Articles NMR Structural Studies of Human Cellular Prion Proteins.
Curr Top Med Chem. 2013 Sep 23;
Authors: Biljan I, Ilc G, Giachin G, Legname G, Plavec J
Abstract
Prion diseases or transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders associated with the conformational conversion of the cellular prion protein, PrPC, into a pathological form known as prion or PrPSc. They can be classified into sporadic, inherited and infectious forms....
[NMR paper] Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Mapping Functional Interaction Sites of Human Prune C-Terminal Domain by NMR Spectroscopy in Human Cell Lysates.
Chemistry. 2013 Aug 12;
Authors: Diana D, Smaldone G, De Antonellis P, Pirone L, Carotenuto M, Alonzi A, Di Gaetano S, Zollo M, Pedone EM, Fattorusso R
Abstract
Get well prune: The C-terminal third domain of h-prune is largely unfolded and involved in relevant protein-protein interactions, particularly with...
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Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy
Fabio Arnesano, Lucia Banci, Ivano Bertini, Isabella C. Felli, Maurizio Losacco and Giovanni Natile
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207346p/aop/images/medium/ja-2011-07346p_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207346p
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9nWkAzWuq20
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10-24-2011 11:06 PM
[NMR paper] NMR solution structure of Mob1, a mitotic exit network protein and its interaction wi
NMR solution structure of Mob1, a mitotic exit network protein and its interaction with an NDR kinase peptide.
Related Articles NMR solution structure of Mob1, a mitotic exit network protein and its interaction with an NDR kinase peptide.
J Mol Biol. 2004 Mar 12;337(1):167-82
Authors: Ponchon L, Dumas C, Kajava AV, Fesquet D, Padilla A
Proteins of the Mob1/phocein family are found in all eukaryotic cells. In yeast, they are activating subunits of Dbf2-related protein kinases involved in cell cycle control. Despite the wide occurrence of these...
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11-24-2010 09:25 PM
[NMR paper] Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine
Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy.
Related Articles Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy.
Eur J Biochem. 1998 Oct 1;257(1):69-77
Authors: Clish CB, Peyton DH, Barklis E
The capsid domain of retroviral Gag proteins possesses a single highly conserved...
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[NMR paper] Solution structures of human transforming growth factor alpha derived from 1H NMR dat
Solution structures of human transforming growth factor alpha derived from 1H NMR data.
Related Articles Solution structures of human transforming growth factor alpha derived from 1H NMR data.
Biochemistry. 1990 Aug 28;29(34):7805-13
Authors: Kline TP, Brown FK, Brown SC, Jeffs PW, Kopple KD, Mueller L
The 600-MHz 1H NMR spectrum of the des-Val-Val mutant of human transforming growth factor alpha (TGF-alpha) was reassigned at pH = 6.3. The conformation space of des-Val-Val TGF-alpha was explored by distance geometry embedding followed by...
Solution NMR structures of homeodomains from human proteins ALX4, ZHX1, and CASP8AP2 contribute to the structural coverage of the Human Cancer Protein Interaction Network.
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