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Giorgio Colombo

Researcher at University of Pavia

Publications -  87
Citations -  4205

Giorgio Colombo is an academic researcher from University of Pavia. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 32, co-authored 67 publications receiving 3750 citations. Previous affiliations of Giorgio Colombo include Pennsylvania State University & University of Massachusetts Medical School.

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Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: A molecular dynamics study

Danilo Roccatano, +3 more
- 17 Sep 2002 - 
TL;DR: Two molecular dynamics simulation techniques have been used to investigate the effect of 2,2,2-trifluoroethanol as a cosolvent on the stability of three different secondary structure-forming peptides, suggesting that the stabilizing effect of TFE is induced by the preferential aggregation of T FE molecules around the peptides.
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Rational design of shepherdin, a novel anticancer agent

Janet Plescia, +12 more
- 01 May 2005 - 
TL;DR: Systemic administration of shepherdin in vivo is well tolerated, and inhibits human tumor growth in mice without toxicity, suggesting that shepherdin could provide a potent and selective anticancer agent in humans.
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Combinatorial drug design targeting multiple cancer signaling networks controlled by mitochondrial Hsp90

Byoung Heon Kang, +8 more
- 02 Mar 2009 - 
TL;DR: Gamitrinibs were shown to accumulate in the mitochondria of human tumor cell lines and to inhibit Hsp90 activity by acting as ATPase antagonists, and exhibited a "mitochondriotoxic" mechanism of action.
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Structure-activity relationships of linear and cyclic peptides containing the NGR tumor-homing motif.

Giorgio Colombo, +7 more
- 06 Dec 2002 - 
TL;DR: Results suggest that the NGR motif has a strong propensity to form β-turn in linear peptides and may explain the finding that GNGRG peptide can target TNF to tumors, albeit to a lower extent than CNGRC.
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Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function.

Mehdi Mollapour, +18 more
- 12 Feb 2010 - 
TL;DR: Hsp90 chaperoning of distinct client proteins is differentially regulated by specific posttranslational modification of a unique subcellular pool of the chaperone, and they provide a strategy to increase the cellular potency of Hsp90 inhibitors.