[ASAP] A Model for the Solution Structure of Human Fe(II)-Bound Acireductone Dioxygenase and Interactions with the Regulatory Domain of Matrix Metalloproteinase I (MMP-I)
[ASAP] A Model for the Solution Structure of Human Fe(II)-Bound Acireductone Dioxygenase and Interactions with the Regulatory Domain of Matrix Metalloproteinase I (MMP-I)
[ASAP] Glycosylation Fosters Interactions between Model Sea Urchin Spicule Matrix Proteins. Implications for Embryonic Spiculogenesis and Biomineralization
Glycosylation Fosters Interactions between Model Sea Urchin Spicule Matrix Proteins. Implications for Embryonic Spiculogenesis and Biomineralization
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00207/20180517/images/medium/bi-2018-00207u_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00207
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nmrlearner
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05-18-2018 04:15 AM
[NMR paper] Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR.
Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR.
Related Articles Phosphorylation of the regulatory domain of human tyrosine hydroxylase 1 monitored using non-uniformly sampled NMR.
Biophys Chem. 2017 Jan 27;223:25-29
Authors: Louša P, Nedozrálová H, Župa E, Nová?ek J, Hritz J
Abstract
Human tyrosine hydroxylase 1 (hTH1) activity is regulated by phosphorylation of its regulatory domain (RD-hTH1) and by an interaction with the 14-3-3 protein. The RD-hTH1 is...
[NMR paper] Solution NMR Structure and Histone Binding of the PHD Domain of Human MLL5.
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PLoS One. 2013;8(10):e77020
Authors: Lemak A, Yee A, Wu H, Yap D, Zeng H, Dombrovski L, Houliston S, Aparicio S, Arrowsmith CH
Abstract
Mixed Lineage Leukemia 5 (MLL5) is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. In addition to its catalytic domain, MLL5 contains a PHD finger domain, a protein module that...
nmrlearner
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10-17-2013 04:57 PM
Discovered a new regulatory mechanism of c-Src, the human protein bound to ... - HealthCanal.com
Discovered a new regulatory mechanism of c-Src, the human protein bound to ... - HealthCanal.com
<img alt="" height="1" width="1" />
Discovered a new regulatory mechanism of c-Src, the human protein bound to ...
HealthCanal.com
... leader of the Biomolecular Nuclear Magnetic Resonance (NMR) Research Group, affiliated with the Department of Organic Chemistry of the UB, â??the discovery of a new regulatory mechanism in such a relevant and extensively studied protein proves the ...
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nmrlearner
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02-20-2013 05:54 AM
[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.
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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...
nmrlearner
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11-24-2010 09:51 PM
[NMR paper] NMR-based modification of matrix metalloproteinase inhibitors with improved bioavaila
NMR-based modification of matrix metalloproteinase inhibitors with improved bioavailability.
Related Articles NMR-based modification of matrix metalloproteinase inhibitors with improved bioavailability.
J Med Chem. 2002 Dec 19;45(26):5628-39
Authors: Hajduk PJ, Shuker SB, Nettesheim DG, Craig R, Augeri DJ, Betebenner D, Albert DH, Guo Y, Meadows RP, Xu L, Michaelides M, Davidsen SK, Fesik SW
The NMR-based discovery of biaryl hydroxamate inhibitors of the matrix metalloproteinase stromelysin (MMP-3) has been previously described (Hajduk et al....
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[ASAP] A Model for the Solution Structure of Human Fe(II)-Bound Acireductone Dioxygenase and Interactions with the Regulatory Domain of Matrix Metalloproteinase I (MMP-I)
Linear Mode
