Professor, Medicine-Massachusetts General Hospital, Harvard Medical School
Infectious Disease
Dr. Marcia B. Goldberg, MD
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Marcia Goldberg is an expert in the field of Infectious Disease. She studied medicine at Harvard Medical School. Harvard Medical School is a top medical college. Harvard Medical School is ranked 1/12 in Research/PrimaryCare. She received awards:"Elected Member". Marcia Goldberg is a published physician as well. She has 64 publications published. The latest was: Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence. She accepts Medicare payments and is listed with Medicare.gov.
Publications
- Biogenesis of YidC cytoplasmic membrane substrates is required for positioning of autotransporter IcsA at future poles.
- Identification of YidC residues that define interactions with the Sec apparatus.
- Bacterial subversion of host innate immune pathways.
- Unbalanced Charge Distribution as a Determinant for Dependence of a Subset of Escherichia coli Membrane Proteins on the Membrane Insertase YidC.
- Antigen-Specific CD8+ T Cells Fail To Respond to Shigella flexneri.
- Microbiology. Establishing the secretion hierarchy.
- Caging targets for destruction.
- Bacterial exploitation of host cell signaling.
- Requirement for formin-induced actin polymerization during spread of Shigella flexneri.
- A genome-scale proteomic screen identifies a role for DnaK in chaperoning of polar autotransporters in Shigella.
- Enterohemorrhagic Escherichia coli raises the I-BAR.
- Putting enterohemorrhagic E. coli on a pedestal.
- Contribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri.
- Structural and functional studies indicate that Shigella VirA is not a protease and does not directly destabilize microtubules.
- Differential regulation by magnesium of the two MsbB paralogs of Shigella flexneri.
- Bacterial actin assembly requires toca-1 to relieve N-wasp autoinhibition.
- Requirement for YaeT in the outer membrane assembly of autotransporter proteins.
- Polar positional information in Escherichia coli spherical cells.
- Polar localization of the autotransporter family of large bacterial virulence proteins.
- Presence of multiple sites containing polar material in spherical Escherichia coli cells that lack MreB.
- Modulation of an outer membrane protease contributes to the virulence defect of Shigella flexneri strains carrying a mutation in the virK locus.
- Alpha C protein of group B Streptococcus binds host cell surface glycosaminoglycan and enters cells by an actin-dependent mechanism.
- Regulation of IcsP, the outer membrane protease of the Shigella actin tail assembly protein IcsA, by virulence plasmid regulators VirF and VirB.
- Evidence for polar positional information independent of cell division and nucleoid occlusion.
- Quantification of Shigella IcsA required for bacterial actin polymerization.
- Branching sites and morphological abnormalities behave as ectopic poles in shape-defective Escherichia coli.
- Recent advances on the development of bacterial poles.
- IcsA, a polarly localized autotransporter with an atypical signal peptide, uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially distri...
- Genetic reporter system for positioning of proteins at the bacterial pole.
- Anaerobic environment of the intestine primes pathogenic Shigella for infection.
- Bacteriophage infection is targeted to cellular poles.
- Shigella interactions with the actin cytoskeleton in the absence of Ena/VASP family proteins.
- Functional analysis of a rickettsial OmpA homology domain of Shigella flexneri icsA.
- Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA.
- Shigella actin-based motility in the absence of vinculin.
- Regulation of surface presentation of IcsA, a Shigella protein essential to intracellular movement and spread, is growth phase dependent.
- Disruption of IcsP, the major Shigella protease that cleaves IcsA, accelerates actin-based motility.
- Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement.
- Cleavage of the Shigella surface protein IcsA (VirG): intention or accident?
- An essential role for gamma interferon in innate resistance to Shigella flexneri infection.
- Impact of either elevated or decreased levels of cytochrome bd expression on Shigella flexneri virulence.
- Adaptive immune response to Shigella flexneri 2a cydC in immunocompetent mice and mice lacking immunoglobulin A.
- Thymic independence of adaptive immunity to the intracellular pathogen Shigella flexneri serotype 2a.
- Clearance of Shigella flexneri infection occurs through a nitric oxide-independent mechanism.
- N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility.
- The unipolar Shigella surface protein IcsA is targeted directly to the bacterial old pole: IcsP cleavage of IcsA occurs over the entire bacterial surface.
- Characterization of a Vibrio cholerae virulence factor homologous to the family of TonB-dependent proteins.
- Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio.
- Avirulence of rough mutants of Shigella flexneri: requirement of O antigen for correct unipolar localization of IcsA in the bacterial outer membrane.
- Effect of O side-chain length and composition on the virulence of Shigella flexneri 2a.
- Shigella flexneri surface protein IcsA is sufficient to direct actin-based motility.
- Shigella subversion of the cellular cytoskeleton: a strategy for epithelial colonization.
- Transcriptional regulation by iron of a Vibrio cholerae virulence gene and homology of the gene to the Escherichia coli fur system.
- Complete DNA sequence and analysis of the large virulence plasmid of Shigella flexneri.
- The making of a gradient: IcsA (VirG) polarity in Shigella flexneri.
- New attenuated derivatives of Vibrio cholerae.
- Positive transcriptional regulation of an iron-regulated virulence gene in Vibrio cholerae.
- A system for production and rapid purification of large amounts of the Shiga toxin/Shiga-like toxin I B subunit.
- Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.
- Identification of an iron-regulated virulence determinant in Vibrio cholerae, using TnphoA mutagenesis.
- Actin-based motility of intracellular microbial pathogens.
- The spectrum of Salmonella infection.
- Host and Bacterial Proteins That Repress Recruitment of LC3 to Shigella Early during Infection.
Schools
Harvard Medical School
Massachusetts General Hospital
Doctors Specialties
- Infectious Disease Medicine
- Infectious Disease
Accepted Insurances
Awards
- Elected Member
Education
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Massachusetts General Hospital -
Harvard Medical School
Hospital
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Massachusetts General Hospital
Helpful Reviews
Medicare Facts
| National Provider Identifier [NPI] | 1700877834 |
| Last Name Of The Provider | GOLDBERG |
| First Name Of The Provider | MARCIA |
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