Richard A. Cerione

ORCID: 0000-0003-4512-5897
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About
Contact & Profiles
Research Areas
  • Protein Kinase Regulation and GTPase Signaling
  • Receptor Mechanisms and Signaling
  • Cancer, Hypoxia, and Metabolism
  • Cellular transport and secretion
  • Extracellular vesicles in disease
  • Blood properties and coagulation
  • Amino Acid Enzymes and Metabolism
  • PI3K/AKT/mTOR signaling in cancer
  • Chemical Reactions and Isotopes
  • Cellular Mechanics and Interactions
  • Erythrocyte Function and Pathophysiology
  • Enzyme Structure and Function
  • MicroRNA in disease regulation
  • Cell Adhesion Molecules Research
  • Biochemical and Molecular Research
  • HER2/EGFR in Cancer Research
  • Lung Cancer Treatments and Mutations
  • RNA modifications and cancer
  • RNA Research and Splicing
  • Neuroscience and Neuropharmacology Research
  • Metabolism, Diabetes, and Cancer
  • Cancer Research and Treatments
  • Ubiquitin and proteasome pathways
  • Phosphodiesterase function and regulation
  • Microtubule and mitosis dynamics

Cornell University
2016-2025

New York State College of Veterinary Medicine
1986-2023

Ithaca College
1998-2023

Cornell High Energy Synchrotron Source
2019

Institute of Molecular Medicine
1999-2016

Laboratory of Molecular Genetics
2016

Milbank Memorial Fund
2010-2011

Institut Langevin
2010

Arkema (France)
2010

Park University
2008

Protein kinases share a number of highly conserved or invariant amino acid residues in their catalytic domains, suggesting that these are necessary for kinase activity. In p180erbB3, receptor tyrosine belonging to the epidermal growth factor (EGF) subfamily, three altered, this protein might have an impaired To test hypothesis, we expressed human EGF and bovine p180erbB3 insect cells via baculovirus infection compared autophosphorylation substrate phosphorylation activities. We found that,...

10.1073/pnas.91.17.8132 article EN Proceedings of the National Academy of Sciences 1994-08-16

The heregulin/neu differentiation factor gene products were purified and cloned based on their ability to stimulate the phosphorylation of a 185-kDa protein in human breast carcinoma cell lines known express erbB2. However, not all cells that erbB2 respond heregulin, indicating other components besides may be required for heregulin binding. Cells are transfected with closely related receptor, erbB3, display single class lower affinity binding sites than has been previously observed lines....

10.1016/s0021-9258(17)36676-0 article EN cc-by Journal of Biological Chemistry 1994-05-01

The PAK family of protein kinases has been suggested as a potential target the Cdc42 and Rac GTPases based on studies in vitro. We show that PAK-3 is activated by vivo. Both, (GTPase-defective) constitutively active mutant stimulated activity Jun kinase 1 (JNK1) transfected cells. Activated also related p38 mitogen-activated but was less effective activator ERK2. effect JNK similar to potent inflammatory cytokine interleukin-1 (IL-1). observation dominant-negative inhibited IL-1 activation...

10.1074/jbc.270.47.27995 article EN cc-by Journal of Biological Chemistry 1995-11-01

Tumor progression involves the ability of cancer cells to communicate with each other and neighboring normal in their microenvironment. Microvesicles (MV) derived from human have received a good deal attention because participate horizontal transfer signaling proteins between contribute invasive activity. Here we show that MV may play another important role oncogenesis. In particular, demonstrate shed by two different cells, MDAMB231 breast carcinoma U87 glioma are capable conferring onto...

10.1073/pnas.1017667108 article EN Proceedings of the National Academy of Sciences 2011-02-28

We have isolated a novel member of the mammalian PAK (p21 activated kinase) and yeast Ste20 serine/threonine kinase family from mouse fibroblast cDNA library, designated mPAK-3. Expression mPAK-3 in Saccharomyces cerevisiae partially restores mating function ste20 null cells. Like other PAKs, contains putative Cdc42Hs/Rac binding sequence when transiently expressed COS cells, full-length binds (GTPγS (guanosine 5′-3-O-(thiotriphosphate)-bound) glutathione S-transferase (GST)-Cdc42Hs GST-Rac1...

10.1074/jbc.270.39.22731 article EN cc-by Journal of Biological Chemistry 1995-09-01

The Ras-like GTPase Cdc42 is essential for cell polarity and bud site assembly in Saccharomyces cerevisiae by regulating cycle-dependent reorganization of cortical cytoskeletal elements. However, its role mammalian cells unknown. To identify potential effectors Cdc42Hs, we incubated lysates from NIH 3T3 fibroblasts or PC12 with immobilized glutathione S-transferase (GST)-Cdc42Hs fusion proteins bound to different guanine nucleotides observed a specific association between the 85-kDa subunit...

10.1016/s0021-9258(17)32226-3 article EN cc-by Journal of Biological Chemistry 1994-07-01

Abstract Non-classical secretory vesicles, collectively referred to as extracellular vesicles (EVs), have been implicated in different aspects of cancer cell survival and metastasis. Here, we describe how a specific class EVs, called microvesicles (MVs), activates VEGF receptors tumour angiogenesis through unique 90 kDa form (VEGF 90K ). We show that is generated by the crosslinking 165 , catalysed enzyme tissue transglutaminase, associates with MVs its interaction chaperone Hsp90. further...

10.1038/ncomms14450 article EN cc-by Nature Communications 2017-02-16

Abstract Communication between the inner cell mass (ICM) and trophoblast layer of blastocyst is known to occur, but its functional consequences on early developmental events unclear. Here we demonstrate that embryonic stem (ES) cells derived from ICM generate shed microvesicles (MVs), a major class extracellular vesicles (EVs), which influence behaviour during implantation process. The MV cargo proteins laminin fibronectin interact with integrins along surfaces trophoblasts, triggering...

10.1038/ncomms11958 article EN cc-by Nature Communications 2016-06-15

ErbB3 is a member of the epidermal growth factor (EGF) receptor subfamily tyrosine kinases and believed to be for an unknown ligand. We have tested possibility that heregulin, possessing EGF-like domain, ligand ErbB3. found iodinated recombinant domain heregulin-beta 1 (125I-rHRG beta 1(177-244) bound specifically insect cell-expressed bovine with dissociation constant 0.85 nM. Moreover, 125I-rHRG NIH3T3 fibroblasts stably transfected erbB3 60 pM, but did not bind parental cells. could...

10.1016/s0021-9258(17)36789-3 article EN cc-by Journal of Biological Chemistry 1994-05-01
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