Assistant Professor, Medicine, University of Connecticut SOM

Physical Medicine/Rehab

Doctor Robert Krug, MD practices Physical Medicine/Rehab. He graduated from Stony Brook University School of Medicine. He over the years received 2 awards: "CMS Meaningful Use Stage 1 Certification" and "Top MD". Robert Krug is a published doctor. He has 85 publications published. The most current publication "RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding ..." He is registered with Medicare and accepts Medicare payments.

Publications

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• Battle between influenza A virus and a newly identified antiviral activity of the PARP-containing ZAPL protein.
• Viral Proteins That Bind Double-Stranded RNA: Countermeasures Against Host Antiviral Responses.
• Cellular DDX21 RNA Helicase Inhibits Influenza A Virus Replication but Is Counteracted by the Viral NS1 Protein.
• (19)F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus.
• Exploring naphthyl-carbohydrazides as inhibitors of influenza A viruses.
• Reciprocal Inhibition between Intracellular Antiviral Signaling and the RNAi Machinery in Mammalian Cells.
• Interferon-induced ISG15 pathway: an ongoing virus-host battle.
• Biochemical and structural evidence in support of a coherent model for the formation of the double-helical influenza A virus ribonucleoprotein.
• Backbone and Ile-δ1, Leu, Val methyl 1H, 13C and 15N NMR chemical shift assignments for human interferon-stimulated gene 15 protein.
• Structural basis for the sequence-specific recognition of human ISG15 by the NS1 protein of influenza B virus.
• Dimer interface of the effector domain of non-structural protein 1 from influenza A virus: an interface with multiple functions.
• The virulence of 1997 H5N1 influenza viruses in the mouse model is increased by correcting a defect in their NS1 proteins.
• Synthesis and evaluation of quinoxaline derivatives as potential influenza NS1A protein inhibitors.
• Influenza A virus strains that circulate in humans differ in the ability of their NS1 proteins to block the activation of IRF3 and interferon-? transcription.
• Structure of the iSH2 domain of human phosphatidylinositol 3-kinase p85β subunit reveals conformational plasticity in the interhelical turn region.
• The ESEV PDZ-binding motif of the avian influenza A virus NS1 protein protects infected cells from apoptosis by directly targeting Scribble.
• Structures of influenza A proteins and insights into antiviral drug targets.
• Species specificity of the NS1 protein of influenza B virus: NS1 binds only human and non-human primate ubiquitin-like ISG15 proteins.
• ISG15 conjugation system targets the viral NS1 protein in influenza A virus-infected cells.
• Emerging antiviral targets for influenza A virus.
• Interferon-induced ISG15 conjugation inhibits influenza A virus gene expression and replication in human cells.
• Influenza a virus polymerase is an integral component of the CPSF30-NS1A protein complex in infected cells.
• Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication.
• Structural basis for suppression of a host antiviral response by influenza A virus.
• The H5N1 influenza virus NS genes selected after 1998 enhance virus replication in mammalian cells.
• Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses.
• A site on the influenza A virus NS1 protein mediates both inhibition of PKR activation and temporal regulation of viral RNA synthesis.
• Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes.
• The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA.
• Retinoic acid inducible gene-I and mda-5 are involved in influenza A virus-induced expression of antiviral cytokines.
• Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA.
• The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2'-5' oligo (A) synthetase/RNase L pathway.
• The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target.
• Virology. Clues to the virulence of H5N1 viruses in humans.
• Herc5, an interferon-induced HECT E3 enzyme, is required for conjugation of ISG15 in human cells.
• Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways.
• Influenza virus virulence and its molecular determinants.
• Properties of the ISG15 E1 enzyme UbE1L.
• The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein.
• Biophysical characterization of the complex between double-stranded RNA and the N-terminal domain of the NS1 protein from influenza A virus: evidence for a novel RNA-b...
• Intracellular warfare between human influenza viruses and human cells: the roles of the viral NS1 protein.
• Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein r...
• Crucial role of CA cleavage sites in the cap-snatching mechanism for initiating viral mRNA synthesis.
• The potential use of influenza virus as an agent for bioterrorism.
• Structural basis for ubiquitin-like ISG 15 protein binding to the NS1 protein of influenza B virus: a protein-protein interaction function that is not shared by the co...
• Human influenza viruses activate an interferon-independent transcription of cellular antiviral genes: outcome with influenza A virus is unique.
• New ways of initiating translation in eukaryotes.
• Efficient translation of mRNAs in influenza A virus-infected cells is independent of the viral 5' untranslated region.
• The 3'-end-processing factor CPSF is required for the splicing of single-intron pre-mRNAs in vivo.
• The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits.
• Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein.
• Selective nuclear export of viral mRNAs in influenza-virus-infected cells.
• Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery.
• RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids.
• RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding ...
• Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs.
• Regulation of a nuclear export signal by an adjacent inhibitory sequence: the effector domain of the influenza virus NS1 protein.
• Chimeras containing influenza NS1 and HIV-1 Rev protein sequences: mechanism of their inhibition of nuclear export of Rev protein-RNA complexes.
• U6atac snRNA, the highly divergent counterpart of U6 snRNA, is the specific target that mediates inhibition of AT-AC splicing by the influenza virus NS1 protein.
• Crystal structure of the unique RNA-binding domain of the influenza virus NS1 protein.
• A novel RNA-binding motif in influenza A virus non-structural protein 1.
• Surprising function of the three influenza viral polymerase proteins: selective protection of viral mRNAs against the cap-snatching reaction catalyzed by the same poly...
• Novel exploitation of a nuclear function by influenza virus: the cellular SF2/ASF splicing factor controls the amount of the essential viral M2 ion channel protein in ...
• The RNA-binding and effector domains of the viral NS1 protein are conserved to different extents among influenza A and B viruses.
• New approach for inhibiting Rev function and HIV-1 production using the influenza virus NS1 protein.
• Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation fa...
• An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure.
• The influenza virus NS1 protein forms multimers in vitro and in vivo.
• The choice of alternative 5' splice sites in influenza virus M1 mRNA is regulated by the viral polymerase complex.
• The influenza virus NS1 protein binds to a specific region in human U6 snRNA and inhibits U6-U2 and U6-U4 snRNA interactions during splicing.
• The influenza virus NS1 protein: a novel inhibitor of pre-mRNA splicing.
• Two functional domains of the influenza virus NS1 protein are required for regulation of nuclear export of mRNA.
• The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A).
• The regulation of export of mRNA from nucleus to cytoplasm.
• Interferon-induced Mx proteins form oligomers and contain a putative leucine zipper.
• Identification of cis-acting intron and exon regions in influenza virus NS1 mRNA that inhibit splicing and cause the formation of aberrantly sedimenting presplicing co...
• Nucleocytoplasmic transport: the influenza virus NS1 protein regulates the transport of spliced NS2 mRNA and its precursor NS1 mRNA.
• Regulation of the extent of splicing of influenza virus NS1 mRNA: role of the rates of splicing and of the nucleocytoplasmic transport of NS1 mRNA.
• Parental influenza virion nucleocapsids are efficiently transported into the nuclei of murine cells expressing the nuclear interferon-induced Mx protein.
• Translational control in influenza virus-infected cells.
• A block in mammalian splicing occurring after formation of large complexes containing U1, U2, U4, U5, and U6 small nuclear ribonucleoproteins.
• Influenza virus regulates protein synthesis during infection by repressing autophosphorylation and activity of the cellular 68,000-Mr protein kinase.
• Influenza virus RNA replication in vitro: synthesis of viral template RNAs and virion RNAs in the absence of an added primer.
• Efficient transcription, not translation, is dependent on adenovirus tripartite leader sequences at late times of infection.

Schools

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• Stony Brook Univ Health Sciences Center School Of Medicine

• Thomas Jefferson University Hospital

Procedures Preformed

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• Joint Drainage
• Myofascial Trigger Point Injection
• Trigger Point Injection

Doctors Specialties

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• Physical Medicine/Rehab

Accepted Insurances

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Awards

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• CMS Meaningful Use Stage 1 Certification
• Top MD

Education

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• Spaulding Rehabilitation Hospital
• Thomas Jefferson University
• Stony Brook University School of Medicine

Hospital

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• Hartford Hospital

Drug Facts

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NPI NUMBER		1215935168
NPPES Provider LastName		KRUG
NPPES Provider FirstName		ROBERT
NPPES Provider ZIPCode		061121513
NPPES Provider State		CT
Specialty Description		Physical Medicine and Rehabilitation
Total Claim Count		327.0
Distinct Opioid Count		1.0
Opioid Claim Count		14.0
Percent Opioid Claims		4.28

Helpful Reviews

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Medicare Facts

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National Provider Identifier [NPI]	1215935168
Last Name Of The Provider	KRUG
First Name Of The Provider	ROBERT
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