Grüber G - Search Results

1

Structural insight and flexible features of NS5 proteins from all four serotypes of Dengue virus in solution.

Saw WG, Tria G, Grüber A, Subramanian Manimekalai MS, Zhao Y, Chandramohan A, Srinivasan Anand G, Matsui T, Weiss TM, Vasudevan SG, Grüber G. Saw WG, et al. Among authors: gruber g, gruber a. Acta Crystallogr D Biol Crystallogr. 2015 Nov;71(Pt 11):2309-27. doi: 10.1107/S1399004715017721. Epub 2015 Oct 31. Acta Crystallogr D Biol Crystallogr. 2015. PMID: 26527147 Free PMC article.

2

Crystal structure of the NS3 protease-helicase from dengue virus.

Luo D, Xu T, Hunke C, Grüber G, Vasudevan SG, Lescar J. Luo D, et al. Among authors: gruber g. J Virol. 2008 Jan;82(1):173-83. doi: 10.1128/JVI.01788-07. Epub 2007 Oct 17. J Virol. 2008. PMID: 17942558 Free PMC article.

3

Structure of the nucleotide-binding subunit B of the energy producer A1A0 ATP synthase in complex with adenosine diphosphate.

Kumar A, Manimekalai MS, Grüber G. Kumar A, et al. Among authors: gruber g. Acta Crystallogr D Biol Crystallogr. 2008 Nov;64(Pt 11):1110-5. doi: 10.1107/S090744490802790X. Epub 2008 Oct 18. Acta Crystallogr D Biol Crystallogr. 2008. PMID: 19020348

4

Structural determination of functional units of the nucleotide binding domain (NBD94) of the reticulocyte binding protein Py235 of Plasmodium yoelii.

Grüber A, Manimekalai MS, Balakrishna AM, Hunke C, Jeyakanthan J, Preiser PR, Grüber G. Grüber A, et al. Among authors: gruber g. PLoS One. 2010 Feb 10;5(2):e9146. doi: 10.1371/journal.pone.0009146. PLoS One. 2010. PMID: 20161776 Free PMC article.

5

Crystallographic studies of the coupling segment NBD94(674-781) of the nucleotide-binding domain of the Plasmodium yoelii reticulocyte-binding protein Py235.

Grüber A, Manimekalai MS, Preiser PR, Grüber G. Grüber A, et al. Among authors: gruber g. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1631-4. doi: 10.1107/S1744309110040996. Epub 2010 Nov 26. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010. PMID: 21139212 Free PMC article.

6

NMR solution structure of NBD94(483-502) of the nucleotide-binding domain of the Plasmodium yoelii reticulocyte-binding protein Py235.

Basak S, Gayen S, Ramalingam JK, Grüber A, Preiser PR, Grüber G. Basak S, et al. Among authors: gruber g, gruber a. FEMS Microbiol Lett. 2011 May;318(2):152-8. doi: 10.1111/j.1574-6968.2011.02253.x. Epub 2011 Mar 18. FEMS Microbiol Lett. 2011. PMID: 21366672

7

Structural characterization of the erythrocyte binding domain of the reticulocyte binding protein homologue family of Plasmodium yoelii.

Grüber A, Gunalan K, Ramalingam JK, Manimekalai MS, Grüber G, Preiser PR. Grüber A, et al. Among authors: gruber g. Infect Immun. 2011 Jul;79(7):2880-8. doi: 10.1128/IAI.01326-10. Epub 2011 Apr 11. Infect Immun. 2011. PMID: 21482683 Free PMC article.

8

Solution structure of subunit a, a₁₀₄₋₃₆₃, of the Saccharomyces cerevisiae V-ATPase and the importance of its C-terminus in structure formation.

Dip PV, Saw WG, Roessle M, Marshansky V, Grüber G. Dip PV, et al. Among authors: gruber g. J Bioenerg Biomembr. 2012 Jun;44(3):341-50. doi: 10.1007/s10863-012-9442-3. Epub 2012 May 5. J Bioenerg Biomembr. 2012. PMID: 22562380

9

Structural architecture and interplay of the nucleotide- and erythrocyte binding domain of the reticulocyte binding protein Py235 from Plasmodium yoelii.

Grüber A, Manimekalai MS, Preiser PR, Grüber G. Grüber A, et al. Among authors: gruber g. Int J Parasitol. 2012 Nov;42(12):1083-9. doi: 10.1016/j.ijpara.2012.07.004. Epub 2012 Aug 3. Int J Parasitol. 2012. PMID: 22878128 Review.

10

The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation.

Zhang Q, Hunke C, Yau YH, Seow V, Lee S, Tanner LB, Guan XL, Wenk MR, Fibriansah G, Chew PL, Kukkaro P, Biukovic G, Shi PY, Shochat SG, Grüber G, Lok SM. Zhang Q, et al. Among authors: gruber g. J Biol Chem. 2012 Nov 23;287(48):40525-34. doi: 10.1074/jbc.M112.384446. Epub 2012 Oct 3. J Biol Chem. 2012. PMID: 23035113 Free PMC article.

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