Literature DB >> 25004925

Chaperoning parasitism: the importance of molecular chaperones in pathogen virulence.

Utpal Tatu1, Len Neckers2.   

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Year:  2014        PMID： 25004925      PMCID： PMC7667492          DOI： 10.1017/S0031182014000778

Source DB:  PubMed          Journal:  Parasitology        ISSN： 0031-1820            Impact factor:   3.234


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  32 in total

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4.  The charged linker region is an important regulator of Hsp90 function.

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5.  Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.

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6.  The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis.

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7.  Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.

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8.  Mice lacking HSP90beta fail to develop a placental labyrinth.

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10.  The molecular chaperone Hsp90α is required for meiotic progression of spermatocytes beyond pachytene in the mouse.

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2.  Identification and characterization of the antiplasmodial activity of Hsp90 inhibitors.

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Review 3.  Hsp90 in Human Diseases: Molecular Mechanisms to Therapeutic Approaches.

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