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  1. Article: A Hands-on Activity for V(D)J Recombination in an Undergraduate Immunology Class.

    Hallstrom, Kelly N / Knapp, Gwendowlyn S

    Journal of microbiology & biology education

    2022  Volume 24, Issue 1

    Abstract: This learning activity teaches the difficult concept of V(D)J recombination as it occurs in B cells. Following the traditional lecture, this hands-on activity uses pipe cleaners of various colors representing variable, joining, and diversity gene ... ...

    Abstract This learning activity teaches the difficult concept of V(D)J recombination as it occurs in B cells. Following the traditional lecture, this hands-on activity uses pipe cleaners of various colors representing variable, joining, and diversity gene segments and recombination signal sequences. Students are provided with instructions for using the pipe cleaners to assemble specific light and heavy immunoglobulin chains. Students each assemble their own light and heavy chains and compare the products made by classmates. This activity uses materials that are easy and affordable to acquire and provides a tactile approach to reinforcing concepts that students often struggle to visualize and master from lecture and textbook material alone.
    Language English
    Publishing date 2022-12-21
    Publishing country United States
    Document type Journal Article
    ISSN 1935-7877
    ISSN 1935-7877
    DOI 10.1128/jmbe.00145-22
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  2. Article ; Online: A Hands-on Activity for V(D)J Recombination in an Undergraduate Immunology Class

    Kelly N. Hallstrom / Gwendowlyn S. Knapp

    Journal of Microbiology & Biology Education, Vol 24, Iss

    2023  Volume 1

    Abstract: ABSTRACT This learning activity teaches the difficult concept of V(D)J recombination as it occurs in B cells. Following the traditional lecture, this hands-on activity uses pipe cleaners of various colors representing variable, joining, and diversity ... ...

    Abstract ABSTRACT This learning activity teaches the difficult concept of V(D)J recombination as it occurs in B cells. Following the traditional lecture, this hands-on activity uses pipe cleaners of various colors representing variable, joining, and diversity gene segments and recombination signal sequences. Students are provided with instructions for using the pipe cleaners to assemble specific light and heavy immunoglobulin chains. Students each assemble their own light and heavy chains and compare the products made by classmates. This activity uses materials that are easy and affordable to acquire and provides a tactile approach to reinforcing concepts that students often struggle to visualize and master from lecture and textbook material alone.
    Keywords immunology laboratory ; remote learning activities ; tactile learning ; undergraduate immunology ; V(D)J recombination ; Special aspects of education ; LC8-6691 ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2023-04-01T00:00:00Z
    Publisher American Society for Microbiology
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: The type three secreted effector SipC regulates the trafficking of PERP during Salmonella infection.

    Hallstrom, Kelly N / McCormick, Beth A

    Gut microbes

    2016  Volume 7, Issue 2, Page(s) 136–145

    Abstract: Salmonella enterica Typhimurium employs type III secreted effectors to induce cellular invasion and pathogenesis. We previously reported the secreted effector SipA is in part responsible for inducing the apical accumulation of the host membrane protein ... ...

    Abstract Salmonella enterica Typhimurium employs type III secreted effectors to induce cellular invasion and pathogenesis. We previously reported the secreted effector SipA is in part responsible for inducing the apical accumulation of the host membrane protein PERP, a host factor we have shown is key to the inflammatory response induced by Salmonella. We now report that the S. Typhimurium type III secreted effector SipC significantly contributes to PERP redistribution to the apical membrane surface. To our knowledge, this is the first report demonstrating a role for SipC in directing the trafficking of a host membrane protein to the cell surface. In sum, facilitation of PERP trafficking appears to be a result of type III secreted effector-mediated recruitment of vesicles to the apical surface. Our study therefore reveals a new role for SipC, and builds upon previous reports suggesting recruitment of vesicles to the cell surface is important for Salmonella invasion.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Genes, Tumor Suppressor ; Host-Pathogen Interactions ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Protein Transport ; Salmonella Infections/genetics ; Salmonella Infections/metabolism ; Salmonella Infections/microbiology ; Salmonella typhimurium/genetics ; Salmonella typhimurium/metabolism ; Type III Secretion Systems/genetics ; Type III Secretion Systems/metabolism
    Chemical Substances Bacterial Proteins ; Membrane Proteins ; PERP protein, human ; Salmonella invasion protein C ; Type III Secretion Systems
    Language English
    Publishing date 2016
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1949-0984
    ISSN (online) 1949-0984
    DOI 10.1080/19490976.2015.1128626
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  4. Article: A convenient preparation of heteroaryl sulfonamides and sulfonyl fluorides from heteroaryl thiols.

    Wright, Stephen W / Hallstrom, Kelly N

    The Journal of organic chemistry

    2006  Volume 71, Issue 3, Page(s) 1080–1084

    Abstract: Heteroaromatic thiols may be oxidized to the sulfonyl chloride at low temperature (-25 degrees C) by using 3.3 equiv of aqueous sodium hypochlorite. The reaction is rapid, avoids the use of chlorine gas, and succeeds with substrates that have previously ... ...

    Abstract Heteroaromatic thiols may be oxidized to the sulfonyl chloride at low temperature (-25 degrees C) by using 3.3 equiv of aqueous sodium hypochlorite. The reaction is rapid, avoids the use of chlorine gas, and succeeds with substrates that have previously been found to afford little or none of the sulfonamide product with other procedures. The method allows the preparation of the sulfonyl fluorides, which are stable enough to be purified and stored, making them potentially useful monomers in parallel chemistry efforts.
    MeSH term(s) Molecular Structure ; Oxidation-Reduction ; Sulfhydryl Compounds/chemistry ; Sulfinic Acids/chemistry ; Sulfonamides/chemistry
    Chemical Substances Sulfhydryl Compounds ; Sulfinic Acids ; Sulfonamides ; sulfuryl fluoride (64B59K7U6Q)
    Language English
    Publishing date 2006-02-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/jo052164+
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4473: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
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  5. Article: Diversification of NRT2 and the origin of its fungal homolog.

    Slot, Jason C / Hallstrom, Kelly N / Matheny, Patrick B / Hibbett, David S

    Molecular biology and evolution

    2007  Volume 24, Issue 8, Page(s) 1731–1743

    Abstract: We investigated the origin and diversification of the high-affinity nitrate transporter NRT2 in fungi and other eukaryotes using Bayesian and maximum parsimony methods. To assess the higher-level relationships and origins of NRT2 in eukaryotes, we ... ...

    Abstract We investigated the origin and diversification of the high-affinity nitrate transporter NRT2 in fungi and other eukaryotes using Bayesian and maximum parsimony methods. To assess the higher-level relationships and origins of NRT2 in eukaryotes, we analyzed 200 amino acid sequences from the Nitrate/Nitrite Porter (NNP) Family (to which NRT2 belongs), including 55 fungal, 41 viridiplantae (green plants), 11 heterokonts (stramenopiles), and 87 bacterial sequences. To assess evolution of NRT2 within fungi and other eukaryotes, we analyzed 116 amino acid sequences of NRT2 from 58 fungi, 40 viridiplantae (green plants), 1 rhodophyte, and 5 heterokonts, rooted with 12 bacterial sequences. Our results support a single origin of eukaryotic NRT2 from 1 of several clades of mostly proteobacterial NNP transporters. The phylogeny of bacterial NNP transporters does not directly correspond with bacterial taxonomy, apparently due to ancient duplications and/or horizontal gene transfer events. The distribution of NRT2 in the eukaryotes is patchy, but the NRT2 phylogeny nonetheless supports the monophyly of major groups such as viridiplantae, flowering plants, monocots, and eudicots, as well as fungi, ascomycetes, basidiomycetes, and agaric mushrooms. At least 1 secondary origin of eukaryotic NRT2 via horizontal transfer to the fungi is suggested, possibly from a heterokont donor. Our analyses also suggest that there has been a horizontal transfer of nrt2 from a basidiomycete fungus to an ascomycete fungus and reveal a duplication of nrt2 in the ectomycorrhizal mushroom genus, Hebeloma.
    MeSH term(s) Anion Transport Proteins/genetics ; Anion Transport Proteins/metabolism ; Eukaryota/classification ; Eukaryota/genetics ; Eukaryotic Cells/physiology ; Evolution, Molecular ; Fungi/genetics ; Fungi/metabolism ; Gene Expression Regulation, Plant ; Nitrates/metabolism ; Phylogeny ; Sequence Alignment
    Chemical Substances Anion Transport Proteins ; Nitrates ; nitrate transporters
    Language English
    Publishing date 2007-08
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 998579-7
    ISSN 1537-1719 ; 0737-4038
    ISSN (online) 1537-1719
    ISSN 0737-4038
    DOI 10.1093/molbev/msm098
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    Zs.A 2137: Show issues Location:
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  6. Article ; Online: PERP, a host tetraspanning membrane protein, is required for Salmonella-induced inflammation.

    Hallstrom, Kelly N / Srikanth, C V / Agbor, Terence A / Dumont, Christopher M / Peters, Kristen N / Paraoan, Luminita / Casanova, James E / Boll, Erik J / McCormick, Beth A

    Cellular microbiology

    2015  Volume 17, Issue 6, Page(s) 843–859

    Abstract: Salmonella enterica Typhimurium induces intestinal inflammation through the activity of type III secreted effector (T3SE) proteins. Our prior results indicate that the secretion of the T3SE SipA and the ability of SipA to induce epithelial cell responses ...

    Abstract Salmonella enterica Typhimurium induces intestinal inflammation through the activity of type III secreted effector (T3SE) proteins. Our prior results indicate that the secretion of the T3SE SipA and the ability of SipA to induce epithelial cell responses that lead to induction of polymorphonuclear transepithelial migration are not coupled to its direct delivery into epithelial cells from Salmonella. We therefore tested the hypothesis that SipA interacts with a membrane protein located at the apical surface of intestinal epithelial cells. Employing a split ubiquitin yeast-two-hybrid screen, we identified the tetraspanning membrane protein, p53 effector related to PMP-22 (PERP), as a SipA binding partner. SipA and PERP appear to have intersecting activities as we found PERP to be involved in proinflammatory pathways shown to be regulated by SipA. In sum, our studies reveal a critical role for PERP in the pathogenesis of S. Typhimurium, and for the first time demonstrate that SipA, a T3SE protein, can engage a host protein at the epithelial surface.
    MeSH term(s) Bacterial Proteins/metabolism ; Cell Line ; Epithelial Cells/metabolism ; Epithelial Cells/microbiology ; Genes, Tumor Suppressor ; Host-Pathogen Interactions ; Humans ; Inflammation/microbiology ; Inflammation/pathology ; Membrane Proteins/metabolism ; Microfilament Proteins/metabolism ; Protein Binding ; Protein Interaction Mapping ; Salmonella typhimurium/immunology ; Transendothelial and Transepithelial Migration ; Two-Hybrid System Techniques
    Chemical Substances Bacterial Proteins ; Membrane Proteins ; Microfilament Proteins ; PERP protein, human ; SipA protein, Salmonella
    Language English
    Publishing date 2015-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 1468320-9
    ISSN 1462-5822 ; 1462-5814
    ISSN (online) 1462-5822
    ISSN 1462-5814
    DOI 10.1111/cmi.12406
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    Zs.A 5288: Show issues Location:
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