Physician

Family Medicine

Smita Patel works in the field of Family Medicine. She researched medicine at Saba University School of Medicine. Smita S. Patel is a published doctor. She published 95 publications, including: 'Bacteriophage T7 DNA helicase binds dTTP, forms hexamers, and binds DNA in the absence of Mg2+. The presence of dTTP is sufficient for hexamer formation and DNA binding.'

Publications

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• Homologous DNA strand exchange activity of the human mitochondrial DNA helicase TWINKLE.
• Interactions of the yeast mitochondrial RNA polymerase with the +1 and +2 promoter bases dictate transcription initiation efficiency.
• Evidence That Bank Vole PrP Is a Universal Acceptor for Prions.
• Helicase and Polymerase Move Together Close to the Fork Junction and Copy DNA in One-Nucleotide Steps.
• Single-Molecule Fluorescence Reveals the Unwinding Stepping Mechanism of Replicative Helicase.
• Histone chaperone FACT action during transcription through chromatin by RNA polymerase II.
• Yeast Pif1 Helicase Exhibits a One Base Pair Stepping Mechanism for Unwinding Duplex DNA.
• Switching from single-stranded to double-stranded DNA limits the unwinding processivity of ring-shaped T7 DNA helicase.
• ATP-induced helicase slippage reveals highly coordinated subunits.
• Structural basis of RNA recognition and activation by innate immune receptor RIG-I.
• Opening-closing dynamics of the mitochondrial transcription pre-initiation complex.
• Transcription factor-dependent DNA bending governs promoter recognition by the mitochondrial RNA polymerase.
• Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase.
• Direct measurements of torque during holliday junction migration.
• The N-terminal Domain of the Yeast Mitochondrial RNA Polymerase Regulates Multiple Steps of Transcription.
• The A257T linker region mutant of T7 helicase-primase protein is defective in DNA loading and rescued by T7 DNA polymerase.
• Fluorescence-based assay to measure the real-time kinetics of nucleotide incorporation during transcription elongation.
• One motor driving two translocases.
• The protease domain increases the translocation stepping efficiency of the hepatitis C virus NS3-4A helicase.
• Mitochondrial transcription factor Mtf1 traps the unwound non-template strand to facilitate open complex formation.
• Experimental and computational analysis of DNA unwinding and polymerization kinetics.
• Real-time observation of the transition from transcription initiation to elongation of the RNA polymerase.
• Coordinating DNA replication by means of priming loop and differential synthesis rate.
• Structural biology: Steps in the right direction.
• Fluorescent lifetime trajectories of a single fluorophore reveal reaction intermediates during transcription initiation.
• Fluorescence mapping of the open complex of yeast mitochondrial RNA polymerase.
• Model-based global analysis of heterogeneous experimental data using gfit.
• Branch migration enzyme as a Brownian ratchet.
• Coupling of DNA unwinding to nucleotide hydrolysis in a ring-shaped helicase.
• Mechanistic and kinetic analysis of the DcpS scavenger decapping enzyme.
• Transcription initiation in a single-subunit RNA polymerase proceeds through DNA scrunching and rotation of the N-terminal subdomains.
• Single strand binding proteins increase the processivity of DNA unwinding by the hepatitis C virus helicase.
• Interaction of CheY with the C-terminal peptide of CheZ.
• Kinetic pathway of pyrophosphorolysis by a retrotransposon reverse transcriptase.
• The transition to an elongation complex by T7 RNA polymerase is a multistep process.
• Nucleic acid unwinding by hepatitis C virus and bacteriophage t7 helicases is sensitive to base pair stability.
• Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase.
• Participation of the fingers subdomain of Escherichia coli DNA polymerase I in the strand displacement synthesis of DNA.
• The role of the C-terminal domain of protein tyrosine phosphatase-1B in phosphatase activity and substrate binding.
• Transient state kinetics of transcription elongation by T7 RNA polymerase.
• Mechanisms of a ring shaped helicase.
• Sequential release of promoter contacts during transcription initiation to elongation transition.
• Mechanisms of helicases.
• Mechanochemistry of transcription termination factor Rho.
• T7 RNA polymerase-induced bending of promoter DNA is coupled to DNA opening.
• Rapid binding of T7 RNA polymerase is followed by simultaneous bending and opening of the promoter DNA.
• Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains.
• Extended upstream A-T sequence increases T7 promoter strength.
• Mechanochemistry of t7 DNA helicase.
• DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase.
• A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase.
• The functional interaction of the hepatitis C virus helicase molecules is responsible for unwinding processivity.
• The DNA-unwinding mechanism of the ring helicase of bacteriophage T7.
• Nucleotide binding induces conformational changes in Escherichia coli transcription termination factor Rho.
• T7 lysozyme represses T7 RNA polymerase transcription by destabilizing the open complex during initiation.
• Kinetics of transcription initiation at lacP1. Multiple roles of cyclic AMP receptor protein.
• ATP binding modulates the nucleic acid affinity of hepatitis C virus helicase.
• Fluorescence methods for studying the kinetics and thermodynamics of transcription initiation.
• The energetics of consensus promoter opening by T7 RNA polymerase.
• Kinetic pathway of dTTP hydrolysis by hexameric T7 helicase-primase in the absence of DNA.
• The +2 NTP binding drives open complex formation in T7 RNA polymerase.
• T7 DNA helicase: a molecular motor that processively and unidirectionally translocates along single-stranded DNA.
• Helicase from hepatitis C virus, energetics of DNA binding.
• Kinetic and thermodynamic basis of promoter strength: multiple steps of transcription initiation by T7 RNA polymerase are modulated by the promoter sequence.
• The intercalating beta-hairpin of T7 RNA polymerase plays a role in promoter DNA melting and in stabilizing the melted DNA for efficient RNA synthesis.
• The primase active site is on the outside of the hexameric bacteriophage T7 gene 4 helicase-primase ring.
• Peculiar 2-aminopurine fluorescence monitors the dynamics of open complex formation by bacteriophage T7 RNA polymerase.
• The kinetic pathway of RNA binding to the Escherichia coli transcription termination factor Rho.
• A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein.
• DNA binding in the central channel of bacteriophage T7 helicase-primase is a multistep process. Nucleotide hydrolysis is not required.
• Structure and function of hexameric helicases.
• The mechanism of ATP hydrolysis at the noncatalytic sites of the transcription termination factor Rho.
• The helicase from hepatitis C virus is active as an oligomer.
• Transcription termination factor Rho contains three noncatalytic nucleotide binding sites.
• Bacteriophage T7 DNA helicase binds dTTP, forms hexamers, and binds DNA in the absence of Mg2+. The presence of dTTP is sufficient for hexamer formation and DNA binding.
• Increased DNA unwinding efficiency of bacteriophage T7 DNA helicase mutant protein 4A'/E348K.
• Asymmetric interactions of hexameric bacteriophage T7 DNA helicase with the 5'- and 3'-tails of the forked DNA substrate.
• Kinetic mechanism of GTP binding and RNA synthesis during transcription initiation by bacteriophage T7 RNA polymerase.
• Inhibition of T7 RNA polymerase: transcription initiation and transition from initiation to elongation are inhibited by T7 lysozyme via a ternary complex with RNA poly...
• DNA polymerase beta: multiple conformational changes in the mechanism of catalysis.
• High-speed, random-access fluorescence microscopy: I. High-resolution optical recording with voltage-sensitive dyes and ion indicators.
• The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase.
• Kinetic mechanism of transcription initiation by bacteriophage T7 RNA polymerase.
• Equilibrium and stopped-flow kinetic studies of interaction between T7 RNA polymerase and its promoters measured by protein and 2-aminopurine fluorescence changes.
• Selection, identification, and genetic analysis of random mutants in the cloned primase/helicase gene of bacteriophage T7.
• Biochemical analysis of mutant T7 primase/helicase proteins defective in DNA binding, nucleotide hydrolysis, and the coupling of hydrolysis with DNA unwinding.
• DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase.
• Cooperative interactions of nucleotide ligands are linked to oligomerization and DNA binding in bacteriophage T7 gene 4 helicases.
• Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases.
• Nucleotide binding studies of bacteriophage T7 DNA helicase-primase protein.
• Involvement of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing. A new method for purifying the protein and characterization of physical and enzymatic ...
• Error-prone replication of repeated DNA sequences by T7 DNA polymerase in the absence of its processivity subunit.
• The K318A mutant of bacteriophage T7 DNA primase-helicase protein is deficient in helicase but not primase activity and inhibits primase-helicase protein wild-type act...
• Relaxed Rotational and Scrunching Changes in P266L Mutant of T7 RNA Polymerase Reduce Short Abortive RNAs while Delaying Transition into Elongation.

Schools

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• Saba University School Of Med

• Ochsner Clin Found

• Ochsner Foundation Hospital

Doctors Specialties

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• Family Medicine

Accepted Insurances

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Education

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• Ochsner Clinic Foundation
• Saba University School of Medicine

Hospital

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• Ochsner Medical Center - North Shore

Drug Facts

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NPI NUMBER		1043203615
NPPES Provider LastName		PATEL
NPPES Provider FirstName		SMITA
NPPES Provider ZIPCode		70433
NPPES Provider State		LA
Specialty Description		Family Practice
Total Claim Count		360.0
Distinct Opioid Count		1.0
Opioid Claim Count		11.0
Percent Opioid Claims		3.06

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Medicare Facts

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National Provider Identifier [NPI]	1043203615
Last Name Of The Provider	PATEL
First Name Of The Provider	SMITA
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