Professor, Cell and Molecular Biology, Northwestern University, The Feinberg School of Medicine
Emergency Medicine
Dr. Vladimir L. Gelfand, MD
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Doctor Vladimir L. Gelfand, MD works in the field of Emergency Medicine. He attended St Louis University School of Medicine. Vladimir Gelfand is also published. He has 101 publications published. The lastest publication: "Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores.' Vladimir Gelfand accepts Medicare payments and is registered with Medicare.gov.
Publications
- Intermediate filament dynamics: What we can see now and why it matters.
- Abnormal intermediate filament organization alters mitochondrial motility in giant axonal neuropathy fibroblasts.
- Mitochondrial membrane potential is regulated by vimentin intermediate filaments.
- Kinesin-1-powered microtubule sliding initiates axonal regeneration in Drosophila cultured neurons.
- Microtubule-dependent transport and dynamics of vimentin intermediate filaments.
- Pavarotti/MKLP1 regulates microtubule sliding and neurite outgrowth in Drosophila neurons.
- Breaking Up Isn't Easy: Myosin V and Its Cargoes Need Dma1 Ubiquitin Ligase's Help.
- Microtubule-dependent transport of vimentin filament precursors is regulated by actin and by the concerted action of Rho- and p21-activated kinases.
- Protein kinase Darkener of apricot and its substrate EF1γ regulate organelle transport along microtubules.
- Initial Neurite Outgrowth in Drosophila Neurons Is Driven by Kinesin-Powered Microtubule Sliding.
- The journey of the organelle: teamwork and regulation in intracellular transport.
- The Microtubule-Binding Protein Ensconsin Is an Essential Cofactor of Kinesin-1.
- Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores.
- Organelle transport along microtubules in Xenopus melanophores: evidence for cooperation between multiple motors.
- Bidirectional intracellular transport: utility and mechanism.
- Vimentin intermediate filaments modulate the motility of mitochondria.
- Cytoplasmic microtubule sliding: An unconventional function of conventional kinesin.
- Statistics of active transport in Xenopus melanophores cells.
- Intracellular transport: ER and mitochondria meet and greet along designated tracks.
- Kinesin-1 heavy chain mediates microtubule sliding to drive changes in cell shape.
- Microtubule-mediated transport of the tumor-suppressor protein Merlin and its mutants.
- Opposite-polarity motors activate one another to trigger cargo transport in live cells.
- Myosin-Va restrains the trafficking of Na+/K+-ATPase-containing vesicles in alveolar epithelial cells.
- Role of kinesin light chain-2 of kinesin-1 in the traffic of Na,K-ATPase-containing vesicles in alveolar epithelial cells.
- The dynamic properties of intermediate filaments during organelle transport.
- Alpha-E-catenin binds to dynamitin and regulates dynactin-mediated intracellular traffic.
- The role of microtubule movement in bidirectional organelle transport.
- Motor-cargo release: CaMKII as a traffic cop.
- Rab32 regulates melanosome transport in Xenopus melanophores by protein kinase a recruitment.
- Tracking melanosomes inside a cell to study molecular motors and their interaction.
- Microtubule binding by dynactin is required for microtubule organization but not cargo transport.
- Paradigm lost: milton connects kinesin heavy chain to miro on mitochondria.
- Regulation of mitochondria distribution by RhoA and formins.
- Melanosomes transported by myosin-V in Xenopus melanophores perform slow 35 nm steps.
- Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement?
- Regulation of bidirectional melanosome transport by organelle bound MAP kinase.
- Transport of Drosophila fragile X mental retardation protein-containing ribonucleoprotein granules by kinesin-1 and cytoplasmic dynein.
- Pigment cells: a model for the study of organelle transport.
- Differential regulation of dynein-driven melanosome movement.
- Dynactin is required for bidirectional organelle transport.
- Improved sensitivity for phosphopeptide mapping using capillary column HPLC and microionspray mass spectrometry: comparative phosphorylation site mapping from gel-deri...
- Interactions and regulation of molecular motors in Xenopus melanophores.
- Motor-cargo interactions: the key to transport specificity.
- Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II.
- Of yeast, mice, and men. Rab proteins and organelle transport.
- Regulation of molecular motor proteins.
- A dominant negative approach for functional studies of the kinesin II complex.
- Purification of kinesin from the brain.
- Postsynaptic scaffolds of excitatory and inhibitory synapses in hippocampal neurons: maintenance of core components independent of actin filaments and microtubules.
- Membrane trafficking, organelle transport, and the cytoskeleton.
- Molecular mechanisms of pigment transport in melanophores.
- Regulation of melanosome movement in the cell cycle by reversible association with myosin V.
- In vitro motility assay for melanophore pigment organelles.
- Regulation of organelle movement in melanophores by protein kinase A (PKA), protein kinase C (PKC), and protein phosphatase 2A (PP2A).
- Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors.
- Myosin cooperates with microtubule motors during organelle transport in melanophores.
- Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro.
- Microtubule-dependent control of cell shape and pseudopodial activity is inhibited by the antibody to kinesin motor domain.
- Kinesin-like molecules involved in spindle formation.
- Microtubule dynamics in fish melanophores.
- Structural and biochemical properties of kinesin heavy chain associated with rat brain mitochondria.
- Antibodies to the kinesin motor domain and CENP-E inhibit microtubule depolymerization-dependent motion of chromosomes in vitro.
- Comparison of mitostatic effect, cell uptake and tubulin-binding activity on colchicine and colcemid.
- High molecular weight protein MAP 2 promoting microtubule assembly in vitro is associated with microtubules in cells.
- G-actin-tubulin interaction.
- Microtubule-associated protein MAP1 promotes microtubule assembly in vitro.
- Purification of high-Mr microtubule proteins MAP1 and MAP2.
- Multinucleation of transformed cells normalizes their spreading on the substratum and their cytoskeleton structure.
- Effects of small doses of cytochalasins on fibroblasts: preferential changes of active edges and focal contacts.
- ATP-dependent regulation of cytoplasmic microtubule disassembly.
- Destruction of microfilament bundles in mouse embryo fibroblasts treated with inhibitors of energy metabolism.
- MAP2 competes with MAP1 for binding to microtubules.
- Cytoskeleton of mouse embryo fibroblasts. Electron microscopy of platinum replicas.
- Phalloidin and tropomyosin do not prevent actin filament shortening by the 90 kD protein-actin complex from brain.
- Role of ATP in the regulation of stability of cytoskeletal structures.
- Visualization of cellular focal contacts using a monoclonal antibody to 80 kD serum protein adsorbed on the substratum.
- Multinucleation-induced improvement of the spreading of transformed cells on the substratum.
- Polarization of cytoplasmic fragments microsurgically detached from mouse fibroblasts.
- Identification of a 100 kD protein associated with microtubules, intermediate filaments and coated vesicles in cultured cells.
- 18 kDa microtubule-associated protein: identification as a new light chain (LC-3) of microtubule-associated protein 1 (MAP-1).
- The movement of melanosomes in melanophore fragments obtained by laser microbeam irradiation.
- Identification of a 34-kD polypeptide as a light chain of microtubule-associated protein-1 (MAP-1) and its association with a MAP-1 peptide that binds to microtubules.
- Vimentin intermediate filaments in fish melanophores.
- Immunofluorescent localization of protein synthesis components in mouse embryo fibroblasts.
- The quaternary structure of bovine brain kinesin.
- Bovine brain kinesin is a microtubule-activated ATPase.
- Organization of stress fibers in cultured fibroblasts after extraction of actin with bovine brain gelsolin-like protein.
- Direct visualization of bipolar myosin filaments in stress fibers of cultured fibroblasts.
- Cytoplasmic microtubular motors.
- Isolation of a 45-kDa fragment from the kinesin heavy chain with enhanced ATPase and microtubule-binding activities.
- Stimulation of actin synthesis in phalloidin-treated cells. Evidence for autoregulatory control.
- Microtubule-associated proteins and microtubule-based translocators have different binding sites on tubulin molecule.
- Effect of MAP 1, MAP 2, and tau-proteins on structural parameters of tubulin assemblies.
- MAP2-mediated binding of chromaffin granules to microtubules.
- Some of eukaryotic elongation factor 2 is colocalized with actin microfilament bundles in mouse embryo fibroblasts.
- Coalignment of vimentin intermediate filaments with microtubules depends on kinesin.
- Kinesin is responsible for centrifugal movement of pigment granules in melanophores.
- Microtubule dynamics: mechanism, regulation, and function.
- HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein.
- Cell biology. Every motion has its motor.
Schools
Saint Petersburg SanitarnoGigienceskij Medical Institute
St Louis University Hospital
Doctors Specialties
- Emergency Medicine
Accepted Insurances
Education
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St Louis University School of Medicine
Drug Facts
| NPI NUMBER | 1346303641 | |
| NPPES Provider LastName | GELFAND | |
| NPPES Provider FirstName | VLADIMIR | |
| NPPES Provider ZIPCode | 630174979 | |
| NPPES Provider State | MO | |
| Specialty Description | Internal Medicine | |
| Total Claim Count | 16091.0 | |
| Distinct Opioid Count | 5.0 | |
| Opioid Claim Count | 360.0 | |
| Percent Opioid Claims | 2.24 |
Helpful Reviews
Medicare Facts
| National Provider Identifier [NPI] | 1346303641 |
| Last Name Of The Provider | GELFAND |
| First Name Of The Provider | VLADIMIR |
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