Physician
Family Medicine
Dr. Bruce M. Mayer, MD
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Dr. Bruce M. Mayer is an expert in the field of Family Medicine. He over the years received 1 awards: "Meaningful Use Stage 1 Certification". Bruce M. Mayer is also a published physician. He has 85 paper published. The most recent paper is: Mechanism of activation of Pak1 kinase by membrane localization. He accepts Medicare payments and is listed with Medicare.gov.
Publications
- Phosphorylation of Dok1 by Abl family kinases inhibits CrkI transforming activity.
- Paxillin Kinase Linker (PKL) regulates Vav2 signaling during cell spreading and migration.
- There is More Than One Way to Model an Elephant. Experiment-Driven Modeling of the Actin Cytoskeleton.
- Tony Pawson and the germination and flowering of cell signaling: an appreciation.
- Signalling through SH2 and SH3 domains.
- Characterization of p47gag-crk, a novel oncogene product with sequence similarity to a putative modulatory domain of protein-tyrosine kinases and phospholipase C.
- Genetic analysis of p60v-src domains involved in the induction of different cell transformation parameters.
- Identification of a ten-amino acid proline-rich SH3 binding site.
- The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
- A novel oncogene, v-ryk, encoding a truncated receptor tyrosine kinase is transduced into the RPL30 virus without loss of viral sequences.
- A novel viral oncogene with structural similarity to phospholipase C.
- Concentration-dependent positive and negative regulation of a MAP kinase by a MAP kinase kinase.
- p21CIP1 and Cdc25A: competition between an inhibitor and an activator of cyclin-dependent kinases.
- Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating transcription factor c-Jun.
- The product of the cellular crk gene consists primarily of SH2 and SH3 regions.
- Cell transformation by an oncogene that regulates protein kinases.
- Protein-protein interactions in signaling cascades.
- Endocytosis: EH domains lend a hand.
- Association of the v-crk oncogene product with phosphotyrosine-containing proteins and protein kinase activity.
- SH3-Domain binding function of HIV-1 Nef is required for association with a PAK-related kinase.
- Crk is required for apoptosis in Xenopus egg extracts.
- The noncatalytic src homology region 2 segment of abl tyrosine kinase binds to tyrosine-phosphorylated cellular proteins with high affinity.
- Functions of SH2 and SH3 domains.
- The p35/Cdk5 kinase is a neuron-specific Rac effector that inhibits Pak1 activity.
- c-Src signaling induced by the adapters Sin and Cas is mediated by Rap1 GTPase.
- Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.
- Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins.
- Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.
- Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase.
- NS5A, a nonstructural protein of hepatitis C virus, binds growth factor receptor-bound protein 2 adaptor protein in a Src homology 3 domain/ligand-dependent manner and...
- Signal transduction: clamping down on Src activity.
- Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactio...
- Mutagenic analysis of the v-crk oncogene: requirement for SH2 and SH3 domains and correlation between increased cellular phosphotyrosine and transformation.
- Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides.
- Direct analysis of the binding of the abl Src homology 2 domain to the activated epidermal growth factor receptor.
- Mechanism of activation of Pak1 kinase by membrane localization.
- SH3 domains. Minding your p''s and q''s.
- Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins.
- Identification of domains of the v-crk oncogene product sufficient for association with phosphotyrosine-containing proteins.
- Dominant-negative mutants of the SH2/SH3 adapters Nck and Grb2 inhibit MAP kinase activation and mesoderm-specific gene induction by eFGF in Xenopus.
- The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck.
- Phosphorylation of c-Crk II on the negative regulatory Tyr222 mediates nerve growth factor-induced cell spreading and morphogenesis.
- Growth inhibition by Abl requires an interplay of its SH2 and tyrosine kinase domains.
- Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck.
- Expression of mutated Nck SH2/SH3 adaptor respecifies mesodermal cell fate in Xenopus laevis development.
- Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases.
- SH3 domains: complexity in moderation.
- Proteins that bind the Src homology 3 domain of CrkI have distinct roles in Crk transformation.
- Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway.
- Activation of the Abl tyrosine kinase in vivo by Src homology 3 domains from the Src homology 2/Src homology 3 adaptor Nck.
- Engineering temperature-sensitive SH3 domains.
- Requirement of Nck adaptors for actin dynamics and cell migration stimulated by platelet-derived growth factor B.
- Requirement for C3G-dependent Rap1 activation for cell adhesion and embryogenesis.
- Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch.
- Abl family kinases and Cbl cooperate with the Nck adaptor to modulate Xenopus development.
- Profiling the global tyrosine phosphorylation state by Src homology 2 domain binding.
- Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor.
- Cdc42 is required for PIP(2)-induced actin polymerization and early development but not for cell viability.
- Oncogenic Src requires a wild-type counterpart to regulate invadopodia maturation.
- Characterizing tyrosine phosphorylation signaling in lung cancer using SH2 profiling.
- A FRET-based probe for epidermal growth factor receptor bound non-covalently to a pair of synthetic amphipathic helixes.
- The SH2 domain: versatile signaling module and pharmaceutical target.
- Abi1/Hssh3bp1 pY213 links Abl kinase signaling to p85 regulatory subunit of PI-3 kinase in regulation of macropinocytosis in LNCaP cells.
- Tyrosine residues at the carboxyl terminus of Vav1 play an important role in regulation of its biological activity.
- A reciprocal interdependence between Nck and PI(4,5)P(2) promotes localized N-WASp-mediated actin polymerization in living cells.
- Distinct roles for Crk adaptor isoforms in actin reorganization induced by extracellular signals.
- Molecular machines or pleiomorphic ensembles: signaling complexes revisited.
- Regulation of process retraction and cell migration by EphA3 is mediated by the adaptor protein Nck1.
- Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion.
- Detection of protein-protein interactions by far-western blotting.
- Profiling the tyrosine phosphorylation state using SH2 domains.
- Phosphorylation of p130Cas initiates Rac activation and membrane ruffling.
- A crucial role in cell spreading for the interaction of Abl PxxP motifs with Crk and Nck adaptors.
- The pathogen protein EspF(U) hijacks actin polymerization using mimicry and multivalency.
- Clues to the evolution of complex signaling machinery.
- High-throughput phosphotyrosine profiling using SH2 domains.
- Quantitative multiplexed profiling of cellular signaling networks using phosphotyrosine-specific DNA-tagged SH2 domains.
- Inducible clustering of membrane-targeted SH3 domains of the adaptor protein Nck triggers localized actin polymerization.
- Functional interaction trap: a strategy for validating the functional consequences of tyrosine phosphorylation of specific substrates in vivo.
- Profiling the global tyrosine phosphorylation state.
- A single-chain antibody/epitope system for functional analysis of protein-protein interactions.
- Normalization of nomenclature for peptide motifs as ligands of modular protein domains.
- Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1.
- Abl: mechanisms of regulation and activation.
Schools
Universidad Autonoma De Guadalajara Facultad De Medicina
Suny Downstate Med Center
SUNY Stony Brook
University Of Minnesota
University of Washington
Res Med College Wisc
Doctors Specialties
- Family Medicine
Accepted Insurances
- Aetna
- Pathway X Tier Hosp HealthKeepers DirectAccess VA
- HealthKeepers HMO
- KeyCare PPO
- Assurant Health
- Cigna HMO
- Cigna PPO
- Great West Healthcare-Cigna PPO
- Open Access Plus
- Commercial Insurance Company
- Southern Health PPO
- Coventry Health Care of Virginia HMO
- Emblem Health
- First Health (Coventry Health Care) PPO
- Golden Rule
- Harvard Pilgrim Health Care PPO
- Humana
- Medical Mutual of Ohio
- Medicare MCR
- Optima Health
- UniCare
- Choice Plus POS
- Navigate HMO
- Navigate POS
- Options PPO
- United Healthcare
- Universal American
Awards
- Meaningful Use Stage 1 Certification
Education
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SUNY Stony Brook University Hospital & Medical Center -
Universidad Autonoma de Guadalajara
Drug Facts
| NPI NUMBER | 1104806173 | |
| NPPES Provider LastName | MAYER | |
| NPPES Provider FirstName | BRUCE | |
| NPPES Provider ZIPCode | 231887114 | |
| NPPES Provider State | VA | |
| Specialty Description | Family Practice | |
| Total Claim Count | 6122.0 | |
| Distinct Opioid Count | 7.0 | |
| Opioid Claim Count | 394.0 | |
| Percent Opioid Claims | 6.44 |
Helpful Reviews
Medicare Facts
| National Provider Identifier [NPI] | 1104806173 |
| Last Name Of The Provider | MAYER |
| First Name Of The Provider | BRUCE |
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