Maag D - Search Results

1

Inositol polyphosphate multikinase is a physiologic PI3-kinase that activates Akt/PKB.

Maag D, Maxwell MJ, Hardesty DA, Boucher KL, Choudhari N, Hanno AG, Ma JF, Snowman AS, Pietropaoli JW, Xu R, Storm PB, Saiardi A, Snyder SH, Resnick AC. Maag D, et al. Proc Natl Acad Sci U S A. 2011 Jan 25;108(4):1391-6. doi: 10.1073/pnas.1017831108. Epub 2011 Jan 10. Proc Natl Acad Sci U S A. 2011. PMID: 21220345 Free PMC article.

2

Amino acid signaling to mTOR mediated by inositol polyphosphate multikinase.

Kim S, Kim SF, Maag D, Maxwell MJ, Resnick AC, Juluri KR, Chakraborty A, Koldobskiy MA, Cha SH, Barrow R, Snowman AM, Snyder SH. Kim S, et al. Among authors: maag d. Cell Metab. 2011 Feb 2;13(2):215-21. doi: 10.1016/j.cmet.2011.01.007. Cell Metab. 2011. PMID: 21284988 Free PMC article.

3

Glutamatergic regulation of serine racemase via reversal of PIP2 inhibition.

Mustafa AK, van Rossum DB, Patterson RL, Maag D, Ehmsen JT, Gazi SK, Chakraborty A, Barrow RK, Amzel LM, Snyder SH. Mustafa AK, et al. Among authors: maag d. Proc Natl Acad Sci U S A. 2009 Feb 24;106(8):2921-6. doi: 10.1073/pnas.0813105106. Epub 2009 Feb 4. Proc Natl Acad Sci U S A. 2009. PMID: 19193859 Free PMC article.

4

Inositol pyrophosphates inhibit Akt signaling, thereby regulating insulin sensitivity and weight gain.

Chakraborty A, Koldobskiy MA, Bello NT, Maxwell M, Potter JJ, Juluri KR, Maag D, Kim S, Huang AS, Dailey MJ, Saleh M, Snowman AM, Moran TH, Mezey E, Snyder SH. Chakraborty A, et al. Among authors: maag d. Cell. 2010 Dec 10;143(6):897-910. doi: 10.1016/j.cell.2010.11.032. Cell. 2010. PMID: 21145457 Free PMC article.

5

Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1.

Kim AY, Tang Z, Liu Q, Patel KN, Maag D, Geng Y, Dong X. Kim AY, et al. Among authors: maag d. Cell. 2008 May 2;133(3):475-85. doi: 10.1016/j.cell.2008.02.053. Cell. 2008. PMID: 18455988 Free PMC article.

6

A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon.

Maag D, Fekete CA, Gryczynski Z, Lorsch JR. Maag D, et al. Mol Cell. 2005 Jan 21;17(2):265-75. doi: 10.1016/j.molcel.2004.11.051. Mol Cell. 2005. PMID: 15664195 Free article.

7

Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation.

Algire MA, Maag D, Lorsch JR. Algire MA, et al. Among authors: maag d. Mol Cell. 2005 Oct 28;20(2):251-62. doi: 10.1016/j.molcel.2005.09.008. Mol Cell. 2005. PMID: 16246727 Free article.

8

Uncoupling of initiation factor eIF5B/IF2 GTPase and translational activities by mutations that lower ribosome affinity.

Shin BS, Maag D, Roll-Mecak A, Arefin MS, Burley SK, Lorsch JR, Dever TE. Shin BS, et al. Among authors: maag d. Cell. 2002 Dec 27;111(7):1015-25. doi: 10.1016/s0092-8674(02)01171-6. Cell. 2002. PMID: 12507428 Free article.

9

Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit.

Maag D, Lorsch JR. Maag D, et al. J Mol Biol. 2003 Jul 25;330(5):917-24. doi: 10.1016/s0022-2836(03)00665-x. J Mol Biol. 2003. PMID: 12860115

10

Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection.

Maag D, Algire MA, Lorsch JR. Maag D, et al. J Mol Biol. 2006 Feb 24;356(3):724-37. doi: 10.1016/j.jmb.2005.11.083. Epub 2005 Dec 15. J Mol Biol. 2006. PMID: 16380131

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