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  1. AU="Schrum, Adam G"
  2. AU="Hamann, Johann Georg"
  3. AU="Hochstrasser, Seraina"
  4. AU="Bronk, Marieke"
  5. AU=Lee Jeonghyun
  6. AU="Teshima, M"
  7. AU="Murray, Anne M"
  8. AU="Suaña Calsín, Milciades Conrado"
  9. AU="Bai, Yao" AU="Bai, Yao"
  10. AU="Strandberg, Erik"
  11. AU="Dar Dowlatshahi"
  12. AU="Capote, Ailem Rabasa"
  13. AU="Richier, Q"
  14. AU="Jamla, Monica"
  15. AU="Shimomura, Taizou"
  16. AU="Tampakakis, Emmanouil"
  17. AU="Tabares, Jeffrey V"

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  1. Artikel: Conservation and Enhanced Binding of SARS-CoV-2 Omicron Spike Protein to Coreceptor Neuropilin-1 Predicted by Docking Analysis.

    Baindara, Piyush / Roy, Dinata / Mandal, Santi M / Schrum, Adam G

    Infectious disease reports

    2022  Band 14, Heft 2, Seite(n) 243–249

    Abstract: The Omicron variant of SARS-CoV-2 bears peptide sequence alterations that correlate with a higher infectivity than was observed in the original SARS-CoV-2 isolated from Wuhan, China. We analyzed the CendR motif of spike protein and performed in silico ... ...

    Abstract The Omicron variant of SARS-CoV-2 bears peptide sequence alterations that correlate with a higher infectivity than was observed in the original SARS-CoV-2 isolated from Wuhan, China. We analyzed the CendR motif of spike protein and performed in silico molecular docking with neuropilin-1 (Nrp1), a receptor-ligand interaction known to support infection by the original variant. Our analysis predicts conserved and slightly increased energetic favorability of binding for Omicron CendR:Nrp1. We propose that the viral spike:Nrp1 coreceptor pathway may contribute to the infectivity of the Omicron variant of SARS-CoV-2.
    Sprache Englisch
    Erscheinungsdatum 2022-03-29
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ISSN 2036-7430
    ISSN 2036-7430
    DOI 10.3390/idr14020029
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Transcriptional Regulation of the Human IL5RA Gene through Alternative Promoter Usage during Eosinophil Development.

    Laffey, Kimberly G / Du, Jian / Schrum, Adam G / Ackerman, Steven J

    International journal of molecular sciences

    2021  Band 22, Heft 19

    Abstract: Regulation of the IL-5 receptor alpha ( ...

    Abstract Regulation of the IL-5 receptor alpha (
    Mesh-Begriff(e) Antigens, CD34/genetics ; Base Sequence ; CCAAT-Enhancer-Binding Proteins/genetics ; Cell Differentiation/genetics ; Cells, Cultured ; Eosinophils/physiology ; Gene Expression Regulation/genetics ; Hematopoietic Stem Cells/physiology ; Humans ; Interleukin-5 Receptor alpha Subunit/genetics ; Promoter Regions, Genetic/genetics ; Protein Isoforms/genetics ; RNA, Messenger/genetics ; Transcription Factors/genetics ; Transcription, Genetic/genetics
    Chemische Substanzen Antigens, CD34 ; CCAAT-Enhancer-Binding Proteins ; IL5RA protein, human ; Interleukin-5 Receptor alpha Subunit ; Protein Isoforms ; RNA, Messenger ; Transcription Factors
    Sprache Englisch
    Erscheinungsdatum 2021-09-23
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms221910245
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Vasoactive Intestinal Peptide Amphiphile Micelle Chemical Structure and Hydrophobic Domain Influence Immunomodulatory Potentiation.

    Wang, Xiaofei / Zhang, Rui / Lindaman, Bryce D / Leeper, Caitlin N / Schrum, Adam G / Ulery, Bret D

    ACS applied bio materials

    2022  Band 5, Heft 4, Seite(n) 1464–1475

    Abstract: Vasoactive intestinal peptide (VIP) is a neuropeptide capable of downregulating innate immune responses in antigen presenting cells (APCs) by suppressing their pro-inflammatory cytokine secretion and cell surface marker expression. Though VIP's ... ...

    Abstract Vasoactive intestinal peptide (VIP) is a neuropeptide capable of downregulating innate immune responses in antigen presenting cells (APCs) by suppressing their pro-inflammatory cytokine secretion and cell surface marker expression. Though VIP's bioactivity could possibly be leveraged as a treatment for transplant tolerance, drug delivery innovation is required to overcome its intrinsically limited cellular delivery capacity. One option is to employ peptide amphiphiles (PAs) which are lipidated peptides capable of self-assembling into micelles in water that can enhance cellular association. With this approach in mind, a series of triblock VIP amphiphiles (VIPAs) has been synthesized to explore the influence of block arrangement and hydrophobicity on micelle biocompatibility and bioactivity. VIPA formulation has been found to influence the shape, size, and surface charge of VIPA micelles (VIPAMs) as well as their cytotoxicity and immunomodulatory effects. Specifically, the enclosed work provides strong evidence that cylindrical VIPAMs with aspect ratios of 1.5-150 and moderate positive surface charge are able to potentiate the bioactivity of VIP limiting TNF-α secretion and MHC II and CD86 surface expression on APCs. With these criteria, we have identified PalmK-(EK)
    Mesh-Begriff(e) Drug Delivery Systems ; Hydrophobic and Hydrophilic Interactions ; Micelles ; Tumor Necrosis Factor-alpha/metabolism ; Vasoactive Intestinal Peptide/pharmacology
    Chemische Substanzen Micelles ; Tumor Necrosis Factor-alpha ; Vasoactive Intestinal Peptide (37221-79-7)
    Sprache Englisch
    Erscheinungsdatum 2022-03-18
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 2576-6422
    ISSN (online) 2576-6422
    DOI 10.1021/acsabm.1c00981
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: NOTCH signaling in COVID-19: a central hub controlling genes, proteins, and cells that mediate SARS-CoV-2 entry, the inflammatory response, and lung regeneration.

    Baindara, Piyush / Sarker, Md Bodruzzaman / Earhart, Alexander P / Mandal, Santi M / Schrum, Adam G

    Frontiers in cellular and infection microbiology

    2022  Band 12, Seite(n) 928704

    Abstract: In the lungs of infected individuals, the downstream molecular signaling pathways induced by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) are incompletely understood. Here, we describe and examine predictions of a model in which NOTCH may ...

    Abstract In the lungs of infected individuals, the downstream molecular signaling pathways induced by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) are incompletely understood. Here, we describe and examine predictions of a model in which NOTCH may represent a central signaling axis in lung infection in Coronavirus Disease 2019 (COVID-19). A pathway involving NOTCH signaling, furin, ADAM17, and ACE2 may be capable of increasing SARS-CoV-2 viral entry and infection. NOTCH signaling can also upregulate IL-6 and pro-inflammatory mediators induced to hyperactivation in COVID-19. Furthermore, if NOTCH signaling fails to turn down properly and stays elevated, airway regeneration during lung healing can be inhibited-a process that may be at play in COVID-19. With specific NOTCH inhibitor drugs in development and clinical trials for other diseases being conducted, the roles of NOTCH in all of these processes central to both infection and healing merit contemplation if such drugs might be applied to COVID-19 patients.
    Mesh-Begriff(e) Angiotensin-Converting Enzyme 2 ; COVID-19 ; Humans ; Lung ; Peptidyl-Dipeptidase A/metabolism ; SARS-CoV-2
    Chemische Substanzen Peptidyl-Dipeptidase A (EC 3.4.15.1) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Sprache Englisch
    Erscheinungsdatum 2022-08-04
    Erscheinungsland Switzerland
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2619676-1
    ISSN 2235-2988 ; 2235-2988
    ISSN (online) 2235-2988
    ISSN 2235-2988
    DOI 10.3389/fcimb.2022.928704
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel: Strategies to stabilize compact folding and minimize aggregation of antibody-based fragments.

    Gil, Diana / Schrum, Adam G

    Advances in bioscience and biotechnology (Print)

    2015  Band 4, Heft 4a, Seite(n) 73–84

    Abstract: Monoclonal antibodies (mAbs) have proven to be useful for development of new therapeutic drugs and diagnostic techniques. To overcome the difficulties posed by their complex structure and folding, reduce undesired immunogenicity, and improve ... ...

    Abstract Monoclonal antibodies (mAbs) have proven to be useful for development of new therapeutic drugs and diagnostic techniques. To overcome the difficulties posed by their complex structure and folding, reduce undesired immunogenicity, and improve pharmacokinetic properties, a plethora of different Ab fragments have been developed. These include recombinant Fab and Fv segments that can display improved properties over those of the original mAbs upon which they are based. Antibody (Ab) fragments such as Fabs, scFvs, diabodies, and nanobodies, all contain the variable Ig domains responsible for binding to specific antigenic epitopes, allowing for specific targeting of pathological cells and/or molecules. These fragments can be easier to produce, purify and refold than a full Ab, and due to their smaller size they can be well absorbed and distributed into target tissues. However, the physicochemical and structural properties of the immunoglobulin (Ig) domain, upon which the folding and conformation of all these Ab fragments is based, can limit the stability of Ab-based drugs. The Ig domain is fairly sensitive to unfolding and aggregation when produced out of the structural context of an intact Ab molecule. When unfolded, Ab fragments may lose their specificity as well as establish non-native interactions leading to protein aggregation. Aggregated antibody fragments display altered pharmacokinetic and immunogenic properties that can augment their toxicity. Therefore, much effort has been placed in understanding the factors impacting the stability of Ig folding at two different levels: 1) intrinsically, by studying the effects of the amino acid sequence on Ig folding; 2) extrinsically, by determining the environmental conditions that may influence the stability of Ig folding. In this review we will describe the structure of the Ig domain, and the factors that impact its stability, to set the context for the different approaches currently used to achieve stable recombinant Ig domains when pursuing the development of Ab fragment-based biotechnologies.
    Sprache Englisch
    Erscheinungsdatum 2015-01-28
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2616840-6
    ISSN 2156-8502 ; 2156-8456
    ISSN (online) 2156-8502
    ISSN 2156-8456
    DOI 10.4236/abb.2013.44A011
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Visualization of multiprotein complexes by flow cytometry.

    Schrum, Adam G

    Current protocols in immunology

    2009  Band Chapter 5, Seite(n) Unit5.9

    Abstract: Multiprotein complexes and other protein-protein interactions play important roles in virtually all cellular processes. Analysis of coimmunoprecipitation of protein complexes by flow cytometry (IP-FCM, or "the fly-p" method) provides a sensitive means to ...

    Abstract Multiprotein complexes and other protein-protein interactions play important roles in virtually all cellular processes. Analysis of coimmunoprecipitation of protein complexes by flow cytometry (IP-FCM, or "the fly-p" method) provides a sensitive means to measure these interactions in the native/nondenatured state. First, immunoprecipitating antibodies are covalently coupled to polystyrene latex beads whose low autofluorescence is compatible with flow cytometry. These antibody-coupled beads are used to immunoprecipitate a specific protein (primary analyte) present in cell lysates. Finally, the protein complexes associated with the beads are probed with fluorochrome-conjugated antibodies specific for interaction partners, or secondary analytes, that may be associated with the primary analyte. The use of quantitative flow cytometric methodology can allow the semiquantitative fluorescence data generated to be converted into estimated numbers of co-associated molecules on the beads. The method represents a robust technique to assess native protein-protein interactions without requiring genetic engineering or large sample sizes.
    Mesh-Begriff(e) Animals ; Antibodies/chemistry ; Antibodies/immunology ; Flow Cytometry/methods ; Humans ; Immunoprecipitation/methods ; Indicators and Reagents/chemistry ; Microspheres ; Multiprotein Complexes/chemistry ; Protein Interaction Mapping/methods ; Proteins/analysis ; Proteins/immunology
    Chemische Substanzen Antibodies ; Indicators and Reagents ; Multiprotein Complexes ; Proteins
    Sprache Englisch
    Erscheinungsdatum 2009-10-21
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2179059-0
    ISSN 1934-368X ; 1934-3671
    ISSN (online) 1934-368X
    ISSN 1934-3671
    DOI 10.1002/0471142735.im0509s87
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Volltext online

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  7. Artikel: Robustness and Specificity in Signal Transduction via Physiologic Protein Interaction Networks.

    Schrum, Adam G / Gil, Diana

    Clinical & experimental pharmacology

    2014  Band 2, Heft 3, Seite(n) S3.001

    Abstract: The collective Protein:Protein Interactions (PPI) of a cell are thought to represent a system with emergent network properties that integrate signals from a multiplicity of inputs into coordinated responses. It is hypothesized that the PPI network ... ...

    Abstract The collective Protein:Protein Interactions (PPI) of a cell are thought to represent a system with emergent network properties that integrate signals from a multiplicity of inputs into coordinated responses. It is hypothesized that the PPI network supplies both specificity for many distinct signals that utilize common intermediate pathways, and also robustness by allowing specific signals to be communicated by alternate routes. Progress with genetic networks points to these concepts, but the extent to which PPI networks possess these properties has not been empirically tested, due to lack of quantitative data needed for such assessments. Here, a hypothetical physiologic PPI network is used to illustrate how signaling robustness and specificity could be manifest under conditions of (i) deletion mutation, or (ii) changes in signaling due to variation in environmental conditions or stimuli. It is proposed that advances in technology enabling empirical analysis of PPI network principles will have the potential to significantly impact basic understanding of signaling mechanisms, and contribute to the generation of novel applications in drug screening and pharmacology.
    Sprache Englisch
    Erscheinungsdatum 2014-02-07
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ISSN 2161-1459
    ISSN 2161-1459
    DOI 10.4172/2161-1459.S3-001
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  8. Artikel ; Online: Lower female survival from an opportunistic infection reveals progesterone-driven sex bias in trained immunity.

    Earhart, Alexander P / Karasseva, Natalia G / Storey, Kathryn M / Olthoff, Benjamin / Sarker, Md Bodruzzaman / Laffey, Kimberly G / Lange, Margaret J / Rector, R Scott / Schulz, Laura C / Gil, Diana / Neuhauser, Claudia M / Schrum, Adam G

    Cell reports

    2023  Band 42, Heft 8, Seite(n) 113007

    Abstract: Immune responses differ between females and males, although such sex-based variance is incompletely understood. Observing that bacteremia of the opportunistic pathogen Burkholderia gladioli caused many more deaths of female than male mice bearing genetic ...

    Abstract Immune responses differ between females and males, although such sex-based variance is incompletely understood. Observing that bacteremia of the opportunistic pathogen Burkholderia gladioli caused many more deaths of female than male mice bearing genetic deficiencies in adaptive immunity, we determined that this was associated with sex bias in the innate immune memory response called trained immunity. Female attenuation of trained immunity varies with estrous cycle stage and correlates with serum progesterone, a hormone that decreases glycolytic capacity and recall cytokine secretion induced by antigen non-specific stimuli. Progesterone receptor antagonism rescues female trained immune responses and survival from controlled B. gladioli infection to magnitudes similar to those of males. These data demonstrate progesterone-dependent sex bias in trained immunity where attenuation of female responses is associated with survival outcomes from opportunistic infection.
    Mesh-Begriff(e) Female ; Male ; Animals ; Mice ; Progesterone/pharmacology ; Sexism ; Trained Immunity ; Opportunistic Infections ; Adaptive Immunity
    Chemische Substanzen Progesterone (4G7DS2Q64Y)
    Sprache Englisch
    Erscheinungsdatum 2023-08-16
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2023.113007
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  9. Artikel: Consideration of dornase alfa for the treatment of severe COVID-19 ARDS

    Earhart, Alexander P / Holliday, Zachary M / Hofmann, Hunter V / Schrum, Adam G

    New Microbes New Infect

    Schlagwörter covid19
    Verlag WHO
    Dokumenttyp Artikel
    Anmerkung WHO #Covidence: #155186
    Datenquelle COVID19

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  10. Artikel ; Online: Non-Randomized Trial of Dornase Alfa for Acute Respiratory Distress Syndrome Secondary to Covid-19.

    Holliday, Zachary M / Earhart, Alexander P / Alnijoumi, Mohammed M / Krvavac, Armin / Allen, Lee-Ann H / Schrum, Adam G

    Frontiers in immunology

    2021  Band 12, Seite(n) 714833

    Abstract: Background: The most severe cases of Coronavirus-Disease-2019 (COVID-19) develop into Acute Respiratory Distress Syndrome (ARDS). It has been proposed that oxygenation may be inhibited by extracellular deoxyribonucleic acid (DNA) in the form of ... ...

    Abstract Background: The most severe cases of Coronavirus-Disease-2019 (COVID-19) develop into Acute Respiratory Distress Syndrome (ARDS). It has been proposed that oxygenation may be inhibited by extracellular deoxyribonucleic acid (DNA) in the form of neutrophil extracellular traps (NETs). Dornase alfa (Pulmozyme, Genentech) is recombinant human deoxyribonuclease I that acts as a mucolytic by cleaving and degrading extracellular DNA. We performed a pilot study to evaluate the effects of dornase alfa in patients with ARDS secondary to COVID-19.
    Methods: We performed a pilot, non-randomized, case-controlled clinical trial of inhaled dornase for patients who developed ARDS secondary to COVID-19 pneumonia.
    Results: Improvement in arterial oxygen saturation to inhaled fraction of oxygen ratio (PaO
    Conclusion: Treatment with dornase alfa was associated with improved oxygenation and decreased DNA : MPO complexes in BALF. The positive effects, however, were limited to the time of drug delivery. These data suggest that degradation of extracellular DNA associated with NETs or other structures by inhaled dornase alfa can be beneficial. We propose a more extensive clinical trial is warranted.
    Clinical trial registration: ClinicalTrials.gov, Identifier: NCT04402970.
    Mesh-Begriff(e) Administration, Inhalation ; Adult ; Aged ; Aged, 80 and over ; COVID-19/drug therapy ; Case-Control Studies ; DNA/metabolism ; Deoxyribonuclease I/therapeutic use ; Extracellular Traps/metabolism ; Female ; Humans ; Male ; Middle Aged ; Oxygen Consumption/drug effects ; Peroxidase/metabolism ; Pilot Projects ; Recombinant Proteins/therapeutic use ; Respiratory Distress Syndrome/drug therapy ; SARS-CoV-2/physiology ; Young Adult
    Chemische Substanzen Recombinant Proteins ; DNA (9007-49-2) ; Peroxidase (EC 1.11.1.7) ; Deoxyribonuclease I (EC 3.1.21.1) ; dornase alfa (EC 3.1.21.1)
    Sprache Englisch
    Erscheinungsdatum 2021-10-20
    Erscheinungsland Switzerland
    Dokumenttyp Clinical Trial ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2021.714833
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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