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  1. Article ; Online: Using Digital Profileplasty for Surgical Planning.

    Menapace, Deanna C / Oliver, Jeremie D / Courson, Andrew / Hamilton, Grant S

    Facial plastic surgery : FPS

    2020  Volume 36, Issue 1, Page(s) 3–6

    Abstract: This paper describes a method for setting up an automated and reliable digital profileplasty technique for use in Adobe Photoshop. Digital imaging software can be used to extrapolate more exact measurements during profileplasty. The digital profileplasty ...

    Abstract This paper describes a method for setting up an automated and reliable digital profileplasty technique for use in Adobe Photoshop. Digital imaging software can be used to extrapolate more exact measurements during profileplasty. The digital profileplasty technique is helpful to provide intraoperative guidance during surgery.
    MeSH term(s) Image Processing, Computer-Assisted ; Software
    Language English
    Publishing date 2020-03-19
    Publishing country United States
    Document type Journal Article
    ZDB-ID 630090-x
    ISSN 1098-8793 ; 0736-6825
    ISSN (online) 1098-8793
    ISSN 0736-6825
    DOI 10.1055/s-0040-1701643
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  2. Article ; Online: Rapidly Display Glycan Symbols in 3D Structures: 3D-SNFG in LiteMol.

    Sehnal, David / Grant, Oliver C

    Journal of proteome research

    2018  Volume 18, Issue 2, Page(s) 770–774

    Abstract: The representation of carbohydrates in 3D space using symbols is a powerful visualization method, but such representations are lacking in currently available visualization software. The work presented here allows researchers to display carbohydrate 3D ... ...

    Abstract The representation of carbohydrates in 3D space using symbols is a powerful visualization method, but such representations are lacking in currently available visualization software. The work presented here allows researchers to display carbohydrate 3D structures as 3D-SNFG symbols using LiteMol from a web browser (e.g., v.litemol.org/?loadFromCS=5T3X ). Any PDB ID can be substituted at the end of the URL. Alternatively, the user may enter a PDB ID or upload a structure. LiteMol is available at https://v.litemol.org and automatically depicts any carbohydrate residues as 3D-SNFG symbols. To embed LiteMol in a webpage, visit https://github.com/dsehnal/LiteMol .
    MeSH term(s) Carbohydrates/chemistry ; Molecular Conformation ; Polysaccharides/chemistry ; Software
    Chemical Substances Carbohydrates ; Polysaccharides
    Language English
    Publishing date 2018-09-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.8b00473
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  3. Article ; Online: The role of microglia in 67NR mammary tumor-induced suppression of brain responses to immune challenges in female mice.

    Otto-Dobos, L D / Santos, J C / Strehle, L D / Grant, C V / Simon, L A / Oliver, B / Godbout, J P / Sheridan, J F / Barrientos, R M / Glasper, E R / Pyter, L M

    Journal of neurochemistry

    2023  

    Abstract: ... suppression of neuroinflammatory responses to a subsequent peripheral immune challenge. Here, Balb/c murine ... These data led to the hypothesis that Balb/c mammary tumors blunt the neuroinflammatory responses ... to an immune challenge via a mechanism involving tumor suppression of the peripheral humoral response. Balb/c ...

    Abstract It is poorly understood how solid peripheral tumors affect brain neuroimmune responses despite the various brain-mediated side effects and higher rates of infection reported in cancer patients. We hypothesized that chronic low-grade peripheral tumor-induced inflammation conditions microglia to drive suppression of neuroinflammatory responses to a subsequent peripheral immune challenge. Here, Balb/c murine mammary tumors attenuated the microglial inflammatory gene expression responses to lipopolysaccharide (LPS) and live Escherichia coli (E. coli) challenges and the fatigue response to an E. coli infection. In contrast, the inflammatory gene expression in response to LPS or a toll-like receptor 2 agonist of Percoll-enriched primary microglia cultures was comparable between tumor-bearing and -free mice, as were the neuroinflammatory and sickness behavioral responses to an intracerebroventricular interleukin (IL)-1β injection. These data led to the hypothesis that Balb/c mammary tumors blunt the neuroinflammatory responses to an immune challenge via a mechanism involving tumor suppression of the peripheral humoral response. Balb/c mammary tumors modestly attenuated select circulating cytokine responses to LPS and E. coli challenges. Further, a second mammary tumor/mouse strain model (E0771 tumors in C57Bl/6 mice) displayed mildly elevated inflammatory responses to an immune challenge. Taken together, these data indicate that tumor-induced suppression of neuroinflammation and sickness behaviors may be driven by a blunted microglial phenotype, partly because of an attenuated peripheral signal to the brain, which may contribute to infection responses and behavioral side effects reported in cancer patients. Finally, these neuroimmune effects likely vary based on tumor type and/or host immune phenotype.
    Language English
    Publishing date 2023-04-21
    Publishing country England
    Document type Journal Article
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/jnc.15830
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  4. Article ; Online: Sensitive and Specific Global Cell Surface

    de Haan, Noortje / Song, Ming / Grant, Oliver C / Ye, Zilu / Khoder Agha, Fawzi / Koed Møller Aasted, Mikkel / Woods, Robert J / Vakhrushev, Sergey Y / Wandall, Hans H

    Analytical chemistry

    2023  Volume 95, Issue 47, Page(s) 17328–17336

    Abstract: Cell surface glycans are essential for establishing cell communication, adhesion, and migration. However, it remains challenging to obtain cell surface-specific information about glycoconjugate structures. Acquiring this information is essential for ... ...

    Abstract Cell surface glycans are essential for establishing cell communication, adhesion, and migration. However, it remains challenging to obtain cell surface-specific information about glycoconjugate structures. Acquiring this information is essential for unraveling the functional role of glycans and for exploiting them as clinical targets. To specifically analyze the
    MeSH term(s) Humans ; Glycosylation ; Glycoproteins/chemistry ; Mass Spectrometry/methods ; Polysaccharides/chemistry
    Chemical Substances Glycoproteins ; Polysaccharides
    Language English
    Publishing date 2023-11-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/acs.analchem.3c03626
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  5. Article: Analysis of the SARS-CoV-2 spike protein glycan shield: implications for immune recognition.

    Grant, Oliver C / Montgomery, David / Ito, Keigo / Woods, Robert J

    bioRxiv : the preprint server for biology

    2020  

    Abstract: Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing those ... ...

    Abstract Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing those present in the nascent glycoproteins (prior to enzymatic modifications in the Golgi), as well as those that are commonly observed on antigens present in other viruses. These models were subjected to molecular dynamics (MD) simulation to determine the extent to which glycan microheterogeneity impacts the antigenicity of the S glycoprotein. Lastly, we have identified peptides in the S glycoprotein that are likely to be presented in human leukocyte antigen (HLA) complexes, and discuss the role of S protein glycosylation in potentially modulating the adaptive immune response to the SARS-CoV-2 virus or to a related vaccine. The 3D structures show that the protein surface is extensively shielded from antibody recognition by glycans, with the exception of the ACE2 receptor binding domain, and also that the degree of shielding is largely insensitive to the specific glycoform. Despite the relatively modest contribution of the glycans to the total molecular weight (17% for the HEK293 glycoform) the level of surface shielding is disproportionately high at 42%.
    Keywords covid19
    Language English
    Publishing date 2020-05-01
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2020.04.07.030445
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  6. Article ; Online: Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition.

    Grant, Oliver C / Montgomery, David / Ito, Keigo / Woods, Robert J

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 14991

    Abstract: Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing those ... ...

    Abstract Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing those present in the nascent glycoproteins (prior to enzymatic modifications in the Golgi), as well as those that are commonly observed on antigens present in other viruses. These models were subjected to molecular dynamics (MD) simulation to determine the extent to which glycan microheterogeneity impacts the antigenicity of the S glycoprotein. Lastly, we have identified peptides in the S glycoprotein that are likely to be presented in human leukocyte antigen (HLA) complexes, and discuss the role of S protein glycosylation in potentially modulating the innate and adaptive immune response to the SARS-CoV-2 virus or to a related vaccine. The 3D structures show that the protein surface is extensively shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain, and also that the degree of shielding is largely insensitive to the specific glycoform. Despite the relatively modest contribution of the glycans to the total molecular weight of the S trimer (17% for the HEK293 glycoform) they shield approximately 40% of the protein surface.
    MeSH term(s) Adaptive Immunity ; Amino Acid Sequence ; Angiotensin-Converting Enzyme 2 ; Antibodies, Neutralizing/immunology ; Antigen-Antibody Complex ; Betacoronavirus/immunology ; Betacoronavirus/isolation & purification ; Betacoronavirus/metabolism ; Binding Sites ; COVID-19 ; Coronavirus Infections/immunology ; Coronavirus Infections/pathology ; Coronavirus Infections/virology ; Glycosylation ; HEK293 Cells ; HLA Antigens/metabolism ; Humans ; Immunity, Innate ; Molecular Dynamics Simulation ; Pandemics ; Peptidyl-Dipeptidase A/chemistry ; Peptidyl-Dipeptidase A/metabolism ; Pneumonia, Viral/immunology ; Pneumonia, Viral/pathology ; Pneumonia, Viral/virology ; Polysaccharides/chemistry ; Protein Binding ; Protein Structure, Tertiary ; SARS-CoV-2 ; Sequence Alignment ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism
    Chemical Substances Antibodies, Neutralizing ; Antigen-Antibody Complex ; HLA Antigens ; Polysaccharides ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Keywords covid19
    Language English
    Publishing date 2020-09-14
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-71748-7
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  7. Article ; Online: 3D Models of glycosylated SARS-CoV-2 spike protein suggest challenges and opportunities for vaccine development

    Oliver C. Grant / David Montgomery / Keigo Ito / Robert J. Woods

    Abstract: AbstractHere we have generated 3D structures of glycoforms of the spike (S) protein SARS-CoV-2, based on reported 3D structures for the S protein and on reported glycomics data for the protein produced in HEK293 cells. We also report structures for ... ...

    Abstract AbstractHere we have generated 3D structures of glycoforms of the spike (S) protein SARS-CoV-2, based on reported 3D structures for the S protein and on reported glycomics data for the protein produced in HEK293 cells. We also report structures for glycoforms that represent those present in the nascent glycoproteins (prior to enzymatic modifications in the Golgi and ER), as well as those that are commonly observed on antigens present in other viruses.These models were subjected to MD simulation to take into account protein and glycan plasticity, and to determine the extent to which glycan microheterogeneity impacts antigenicity. Lastly, we have identified peptides in the S protein that are likely to be presented in human leukocyte antigen (HLA) complexes, and discuss the role of S protein glycosylation in potentially modulating the adaptive immune response to the SARS-CoV-2 virus or to a related vaccine.
    Keywords covid19
    Publisher biorxiv
    Document type Article ; Online
    DOI 10.1101/2020.04.07.030445
    Database COVID19

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  8. Article ; Online: Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition

    Oliver C. Grant / David Montgomery / Keigo Ito / Robert J. Woods

    Scientific Reports, Vol 10, Iss 1, Pp 1-

    2020  Volume 11

    Abstract: Abstract Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing ...

    Abstract Abstract Here we have generated 3D structures of glycoforms of the spike (S) glycoprotein from SARS-CoV-2, based on reported 3D structures and glycomics data for the protein produced in HEK293 cells. We also analyze structures for glycoforms representing those present in the nascent glycoproteins (prior to enzymatic modifications in the Golgi), as well as those that are commonly observed on antigens present in other viruses. These models were subjected to molecular dynamics (MD) simulation to determine the extent to which glycan microheterogeneity impacts the antigenicity of the S glycoprotein. Lastly, we have identified peptides in the S glycoprotein that are likely to be presented in human leukocyte antigen (HLA) complexes, and discuss the role of S protein glycosylation in potentially modulating the innate and adaptive immune response to the SARS-CoV-2 virus or to a related vaccine. The 3D structures show that the protein surface is extensively shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain, and also that the degree of shielding is largely insensitive to the specific glycoform. Despite the relatively modest contribution of the glycans to the total molecular weight of the S trimer (17% for the HEK293 glycoform) they shield approximately 40% of the protein surface.
    Keywords Medicine ; R ; Science ; Q ; covid19
    Subject code 612
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Corrigendum: Induction of Antibodies Directed Against Branched Core O-Mannosyl Glycopeptides-Selectivity Complimentary to the ConA Lectin.

    Yu, Jin / Grant, Oliver C / Pett, Christian / Stahl, Sabine / Woods, Robert J / Westerlind, Ulrika

    Chemistry (Weinheim an der Bergstrasse, Germany)

    2019  Volume 25, Issue 15, Page(s) 3963

    Language English
    Publishing date 2019-02-21
    Publishing country Germany
    Document type Journal Article ; Published Erratum
    ZDB-ID 1478547-x
    ISSN 1521-3765 ; 0947-6539
    ISSN (online) 1521-3765
    ISSN 0947-6539
    DOI 10.1002/chem.201900093
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  10. Article ; Online: Targeted delivery of alcohol-containing payloads with antibody-drug conjugates.

    Grier, Katja E / Hansen, Anders H / Haxvig, Christina S / Li, Xin / Krigslund, Oliver / Behrendt, Niels / Engelholm, Lars H / Rossi, Fabio / Sousa, Bebiana C / Harradence, Grant J / Camper, Nicolas / Qvortrup, Katrine M

    Chemical communications (Cambridge, England)

    2023  Volume 59, Issue 47, Page(s) 7240–7242

    Abstract: We herein describe the cell-specific release of alcohol-containing ... ...

    Abstract We herein describe the cell-specific release of alcohol-containing payloads
    MeSH term(s) Animals ; Mice ; Humans ; Immunoconjugates/pharmacology ; Ethanol ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use
    Chemical Substances Immunoconjugates ; Ethanol (3K9958V90M) ; Antineoplastic Agents
    Language English
    Publishing date 2023-06-08
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d3cc01596c
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