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Items: 4

1.

Interplay between negative and positive design elements in Gα helical domains of G proteins determines interaction specificity towards RGS2.

Kasom M, Gharra S, Sadiya I, Avital-Shacham M, Kosloff M.

Biochem J. 2018 Jun 20. pii: BCJ20180285. doi: 10.1042/BCJ20180285. [Epub ahead of print]

PMID:
29925530
2.

"Disruptor" residues in the regulator of G protein signaling (RGS) R12 subfamily attenuate the inactivation of Gα subunits.

Asli A, Sadiya I, Avital-Shacham M, Kosloff M.

Sci Signal. 2018 Jun 12;11(534). pii: eaan3677. doi: 10.1126/scisignal.aan3677.

PMID:
29895615
3.

NTPDASE4 gene products cooperate with the adenovirus E4orf4 protein through PP2A-dependent and -independent mechanisms and contribute to induction of cell death.

Avital-Shacham M, Sharf R, Kleinberger T.

J Virol. 2014 Jun;88(11):6318-28. doi: 10.1128/JVI.00381-14. Epub 2014 Mar 26.

4.

Structure- and modeling-based identification of the adenovirus E4orf4 binding site in the protein phosphatase 2A B55α subunit.

Horowitz B, Sharf R, Avital-Shacham M, Pechkovsky A, Kleinberger T.

J Biol Chem. 2013 May 10;288(19):13718-27. doi: 10.1074/jbc.M112.343756. Epub 2013 Mar 25.

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