Christopher Nicchitta

Endoplasmic reticulum-bound ribosomes reside in stable association with the translocon following termination of protein synthesis.

Cutting edge: CD91-independent cross-presentation of GRP94(gp96)-associated peptides.

GRP94-associated enzymatic activities. Resolution by chromatographic fractionation.

A platform for compartmentalized protein synthesis: protein translation and translocation in the ER.

GRP94 (gp96) and GRP94 N-terminal geldanamycin binding domain elicit tissue nonrestricted tumor suppression.

ISO: a critical evaluation of the role of peptides in heat shock/chaperone protein-mediated tumor rejection.

Re-evaluating the role of heat-shock protein-peptide interactions in tumour immunity.

GRP94/gp96 elicits ERK activation in murine macrophages. A role for endotoxin contamination in NF-kappa B activation and nitric oxide production.

Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes.

Come forth CD1d: Hsp110 in the regulation of intestinal epithelial CD1d expression.

Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.

Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells.

Glucose-regulated protein 94/glycoprotein 96 elicits bystander activation of CD4+ T cell Th1 cytokine production in vivo.

Adenosine nucleotides and the regulation of GRP94-client protein interactions.

The messenger and the message: gp96 (GRP94)-peptide interactions in cellular immunity.

Catheter-mediated subselective intracoronary gene delivery to the rabbit heart: introduction of a novel method.

Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation.

HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor.

Stable ribosome binding to the endoplasmic reticulum enables compartment-specific regulation of mRNA translation.

Enhancement of cancer radiation therapy by use of adenovirus-mediated secretable glucose-regulated protein 94/gp96 expression.

Pathways for compartmentalizing protein synthesis in eukaryotic cells: the template-partitioning model.

mRNA translation is compartmentalized to the endoplasmic reticulum following physiological inhibition of cap-dependent translation.

Synthesis of Hsp90 dimerization modulators.

Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94.

Interaction of TLR2 and TLR4 ligands with the N-terminal domain of Gp96 amplifies innate and adaptive immune responses.

The DRiP hypothesis decennial: support, controversy, refinement and extension.

In vitro and tissue culture methods for analysis of translation initiation on the endoplasmic reticulum.

Divergent regulation of protein synthesis in the cytosol and endoplasmic reticulum compartments of mammalian cells.

Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum.

Analysis of mRNA partitioning between the cytosol and endoplasmic reticulum compartments of mammalian cells.

Redundancy renders the glycoprotein 96 receptor scavenger receptor A dispensable for cross priming in vivo.

The exception that reinforces the rule: crosspriming by cytosolic peptides that escape degradation.

Cell biology: How to combat stress.

Heat shock protein 96 is elevated in rheumatoid arthritis and activates macrophages primarily via TLR2 signaling.

Efficient cross-priming of antiviral CD8+ T cells by antigen donor cells is GRP94 independent.

Glioblastoma proto-oncogene SEC61gamma is required for tumor cell survival and response to endoplasmic reticulum stress.

Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control.

Re-examination of CD91 function in GRP94 (glycoprotein 96) surface binding, uptake, and peptide cross-presentation.

Analyzing mRNA localization to the endoplasmic reticulum via cell fractionation.

Out with the old, in with the new? Comparing methods for measuring protein degradation.

Polysome profiling of the malaria parasite Plasmodium falciparum.

Hierarchical regulation of mRNA partitioning between the cytoplasm and the endoplasmic reticulum of mammalian cells.

Primary role for endoplasmic reticulum-bound ribosomes in cellular translation identified by ribosome profiling.

The enduring enigma of nuclear translation.

Development of a Grp94 inhibitor.

Glycoprotein 96 perpetuates the persistent inflammation of rheumatoid arthritis.

Translocation of sickle cell erythrocyte microRNAs into Plasmodium falciparum inhibits parasite translation and contributes to malaria resistance.

Rare codons regulate KRas oncogenesis.

Premature translational termination products are rapidly degraded substrates for MHC class I presentation.

Induction of the unfolded protein response drives enhanced metabolism and chemoresistance in glioma cells.

Multifunctional roles for the protein translocation machinery in RNA anchoring to the endoplasmic reticulum.

De novo translation initiation on membrane-bound ribosomes as a mechanism for localization of cytosolic protein mRNAs to the endoplasmic reticulum.

The unfolded protein response triggers selective mRNA release from the endoplasmic reticulum.

A novel ribosomopathy caused by dysfunction of RPL10 disrupts neurodevelopment and causes X-linked microcephaly in humans.

Diversity and selectivity in mRNA translation on the endoplasmic reticulum.

LOCAL TRANSLATION. Comment on "Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling".

Simple and inexpensive ribosome profiling analysis of mRNA translation.