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Items: 6

1.

Phase changes in neurotransmission.

Boczek EE, Alberti S.

Science. 2018 Aug 10;361(6402):548-549. doi: 10.1126/science.aau5477. No abstract available.

PMID:
30093586
2.

One domain fits all: Using disordered regions to sequester misfolded proteins.

Boczek EE, Alberti S.

J Cell Biol. 2018 Apr 2;217(4):1173-1175. doi: 10.1083/jcb.201803015. Epub 2018 Mar 9.

PMID:
29523584
3.

Features of the Chaperone Cellular Network Revealed through Systematic Interaction Mapping.

Rizzolo K, Huen J, Kumar A, Phanse S, Vlasblom J, Kakihara Y, Zeineddine HA, Minic Z, Snider J, Wang W, Pons C, Seraphim TV, Boczek EE, Alberti S, Costanzo M, Myers CL, Stagljar I, Boone C, Babu M, Houry WA.

Cell Rep. 2017 Sep 12;20(11):2735-2748. doi: 10.1016/j.celrep.2017.08.074.

4.

An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.

Mateju D, Franzmann TM, Patel A, Kopach A, Boczek EE, Maharana S, Lee HO, Carra S, Hyman AA, Alberti S.

EMBO J. 2017 Jun 14;36(12):1669-1687. doi: 10.15252/embj.201695957. Epub 2017 Apr 4.

5.

Hsp90 dependence of a kinase is determined by its conformational landscape.

Luo Q, Boczek EE, Wang Q, Buchner J, Kaila VR.

Sci Rep. 2017 Mar 14;7:43996. doi: 10.1038/srep43996.

6.

Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90.

Boczek EE, Reefschläger LG, Dehling M, Struller TJ, Häusler E, Seidl A, Kaila VR, Buchner J.

Proc Natl Acad Sci U S A. 2015 Jun 23;112(25):E3189-98. doi: 10.1073/pnas.1424342112. Epub 2015 Jun 8.

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