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The Journal of Biological Chemistry|May 12, 2006
A structural determinant of human cytomegalovirus US2 dictates the down-regulation of class I major histocompatibility moleculesKristina Oresic, Vanessa Noriega, Laura Andrews, et al.
The Journal of Biological Chemistry|January 16, 2002
US2, a human cytomegalovirus-encoded type I membrane protein, contains a non-cleavable amino-terminal signal peptideBenjamin E Gewurz, Hidde L Ploegh, Domenico Tortorella
Immunologic Research|March 29, 2012
Diverse immune evasion strategies by human cytomegalovirusVanessa Noriega, Veronika Redmann, Thomas Gardner, et al.
The EMBO Journal|February 28, 2002
Visualization of the ER-to-cytosol dislocation reaction of a type I membrane proteinEdda Fiebiger, Craig Story, Hidde L Ploegh, et al.
Langmuir : the ACS Journal of Surfaces and Colloids|March 30, 2016
Combating Frosting with Joule-Heated Liquid-Infused Superhydrophobic CoatingsMohamed Elsharkawy, Domenico Tortorella, Shreyas Kapatral, et al.
Journal of Virology|October 22, 2002
The human cytomegalovirus US10 gene product delays trafficking of major histocompatibility complex class I moleculesMargo H Furman, Neelendu Dey, Domenico Tortorella, et al.
The Journal of Biological Chemistry|December 17, 2002
Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocationBoaz Tirosh, Margo H Furman, Domenico Tortorella, et al.
The Journal of Biological Chemistry|July 2, 2003
Ubiquitinylation of the cytosolic domain of a type I membrane protein is not required to initiate its dislocation from the endoplasmic reticulumMargo H Furman, Joana Loureiro, Hidde L Ploegh, et al.
The EMBO Journal|January 30, 2004
A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromisedDaniël Blom, Christian Hirsch, Patrick Stern, et al.
Scientific Reports|March 31, 2016
Human cytomegalovirus gH stability and trafficking are regulated by ER-associated degradation and transmembrane architectureThomas J Gardner, Rosmel E Hernandez, Vanessa M Noriega, et al.
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