LIVIVO - Search results -

Search results

Result 1 - 10 of total 46

Search options

Article: Antibody-mediated cellular responses are dysregulated in Multisystem Inflammatory Syndrome in Children (MIS-C).

Dick, Jenna K / Sangala, Jules A / Krishna, Venkatramana D / Khaimraj, Aaron / Hamel, Lydia / Erickson, Spencer M / Hicks, Dustin / Soigner, Yvette / Covill, Laura E / Johnson, Alexander / Ehrhardt, Michael J / Ernste, Keenan / Brodin, Petter / Koup, Richard A / Khaitan, Alka / Baehr, Carly / Thielen, Beth K / Henzler, Christine M / Skipper, Caleb /

Miller, Jeffrey S / Bryceson, Yenan T / Wu, Jianming / John, Chandy C / Panoskaltsis-Mortari, Angela / Orioles, Alberto / Steiner, Marie E / Cheeran, Maxim C-J / Pravetoni, Marco / Hart, Geoffrey T

bioRxiv : the preprint server for biology

2024

Abstract: Multisystem Inflammatory Syndrome in Children (MIS-C) is a severe complication of SARS-CoV-2 infection characterized by multi-organ involvement and inflammation. Testing of cellular function ex vivo to understand the aberrant immune response in MIS-C is ... ...

Abstract	Multisystem Inflammatory Syndrome in Children (MIS-C) is a severe complication of SARS-CoV-2 infection characterized by multi-organ involvement and inflammation. Testing of cellular function ex vivo to understand the aberrant immune response in MIS-C is limited. Despite strong antibody production in MIS-C, SARS-CoV-2 nucleic acid testing can remain positive for 4-6 weeks after infection. Therefore, we hypothesized that dysfunctional cell-mediated antibody responses downstream of antibody production may be responsible for delayed clearance of viral products in MIS-C. In MIS-C, monocytes were hyperfunctional for phagocytosis and cytokine production, while natural killer (NK) cells were hypofunctional for both killing and cytokine production. The decreased NK cell cytotoxicity correlated with an NK exhaustion marker signature and systemic IL-6 levels. Potentially providing a therapeutic option, cellular engagers of CD16 and SARS-CoV-2 proteins were found to rescue NK cell function in vitro. Together, our results reveal dysregulation in antibody-mediated cellular responses unique to MIS-C that likely contribute to the immune pathology of this disease.
Language	English
Publishing date	2024-04-18
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.04.16.589585
Database	MEDical Literature Analysis and Retrieval System OnLINE

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Correction to "DNA-Mediated Cellular Delivery of Functional Enzymes".

Brodin, Jeffrey D / Sprangers, Anthony J / McMillan, Janet R / Mirkin, Chad A

Journal of the American Chemical Society

2016 Volume 138, Issue 1, Page(s) 459

Language	English
Publishing date	2016-01-13
Publishing country	United States
Document type	Published Erratum
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.5b12653
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Bonn / Germany

Z 4' 55/32: Show issues
Z 7.3: Show issues

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: DNA-mediated engineering of multicomponent enzyme crystals.

Brodin, Jeffrey D / Auyeung, Evelyn / Mirkin, Chad A

Proceedings of the National Academy of Sciences of the United States of America

2015 Volume 112, Issue 15, Page(s) 4564–4569

Abstract: The ability to predictably control the coassembly of multiple nanoscale building blocks, especially those with disparate chemical and physical properties such as biomolecules and inorganic nanoparticles, has far-reaching implications in catalysis, ... ...

Abstract	The ability to predictably control the coassembly of multiple nanoscale building blocks, especially those with disparate chemical and physical properties such as biomolecules and inorganic nanoparticles, has far-reaching implications in catalysis, sensing, and photonics, but a generalizable strategy for engineering specific contacts between these particles is an outstanding challenge. This is especially true in the case of proteins, where the types of possible interparticle interactions are numerous, diverse, and complex. Herein, we explore the concept of trading protein-protein interactions for DNA-DNA interactions to direct the assembly of two nucleic-acid-functionalized proteins with distinct surface chemistries into six unique lattices composed of catalytically active proteins, or of a combination of proteins and DNA-modified gold nanoparticles. The programmable nature of DNA-DNA interactions used in this strategy allows us to control the lattice symmetries and unit cell constants, as well as the compositions and habit, of the resulting crystals. This study provides a potentially generalizable strategy for constructing a unique class of materials that take advantage of the diverse morphologies, surface chemistries, and functionalities of proteins for assembling functional crystalline materials.
MeSH term(s)	Animals ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Bacterial Proteins/ultrastructure ; Catalase/chemistry ; Catalase/metabolism ; Catalase/ultrastructure ; Cattle ; Corynebacterium glutamicum/enzymology ; Crystallization ; DNA/chemistry ; DNA/metabolism ; Engineering/methods ; Gold/chemistry ; Metal Nanoparticles/chemistry ; Metal Nanoparticles/ultrastructure ; Microscopy, Electron, Transmission ; Models, Molecular ; Nanotechnology/methods ; Oligonucleotides/chemistry ; Oligonucleotides/metabolism ; Protein Interaction Mapping/methods ; Proteins/chemistry ; Proteins/metabolism ; Proteins/ultrastructure ; Reproducibility of Results ; Scattering, Small Angle ; X-Ray Diffraction
Chemical Substances	Bacterial Proteins ; Oligonucleotides ; Proteins ; Gold (7440-57-5) ; DNA (9007-49-2) ; Catalase (EC 1.11.1.6)
Language	English
Publishing date	2015-04-14
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1503533112
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Full text

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Designed, Helical Protein Nanotubes with Variable Diameters from a Single Building Block.

Brodin, Jeffrey D / Smith, Sarah J / Carr, Jessica R / Tezcan, F Akif

Journal of the American Chemical Society

2015 Volume 137, Issue 33, Page(s) 10468–10471

Abstract: Due to their structural and mechanical properties, 1D helical protein assemblies represent highly attractive design targets for biomolecular engineering and protein design. Here we present a designed, tetrameric protein building block, Zn8R4, which ... ...

Abstract	Due to their structural and mechanical properties, 1D helical protein assemblies represent highly attractive design targets for biomolecular engineering and protein design. Here we present a designed, tetrameric protein building block, Zn8R4, which assembles via Zn coordination interactions into a series of crystalline, helical nanotubes whose widths can be controlled by solution conditions. X-ray crystallography and transmission electron microscopy (TEM) measurements indicate that all classes of protein nanotubes are constructed through the same 2D arrangement of Zn8R4 tetramers held together by Zn coordination. The mechanical properties of these nanotubes are correlated with their widths. All Zn8R4 nanotubes are found to be highly flexible despite possessing crystalline order, owing to their minimal interbuilding-block interactions mediated solely by metal coordination.
MeSH term(s)	Models, Molecular ; Nanotechnology/methods ; Nanotubes/chemistry ; Protein Structure, Secondary ; Proteins/chemistry ; Zinc/chemistry
Chemical Substances	Proteins ; Zinc (J41CSQ7QDS)
Language	English
Publishing date	2015-08-13
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.5b05755
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Bonn / Germany

Z 4' 55/32: Show issues
Z 7.3: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Antibody-mediated cellular responses are dysregulated in Multisystem Inflammatory Syndrome in Children (MIS-C)

Dick, Jenna K / Sangala, Jules A / Krishna, Venkatramana D / Khaimraj, Aaron / Hamel, Lydia / Erickson, Spencer M / Hicks, Dustin / Soigner, Yvette / Covill, Laura E / Johnson, Alexander / Ehrhardt, Michael J / Ernst, Keenan / Brodin, Petter / Koup, Richard A / Khaitan, Alka / Baehr, Carly / Thielen, Beth K / Henzler, Christine M / Skipper, Caleb /

Miller, Jeffrey S / Bryceson, Yenan T / Wu, Jianming / John, Chandy C / Panoskaltsis-Mortari, Angela / Orioles, Alberto / Steiner, Marie E / Cheeran, Maxim C-J / Pravetoni, Marco / Hart, Geoffrey T

bioRxiv

Abstract	Multisystem Inflammatory Syndrome in Children (MIS-C) is a severe complication of SARS-CoV-2 infection characterized by multi-organ involvement and inflammation. Testing of cellular function ex vivo to understand the aberrant immune response in MIS-C is limited. Despite strong antibody production in MIS-C, SARS-CoV-2 nucleic acid testing can remain positive for 4-6 weeks after infection. Therefore, we hypothesized that dysfunctional cell-mediated antibody responses downstream of antibody production may be responsible for delayed clearance of viral products in MIS-C. In MIS-C, monocytes were hyperfunctional for phagocytosis and cytokine production, while natural killer (NK) cells were hypofunctional for both killing and cytokine production. The decreased NK cell cytotoxicity correlated with an NK exhaustion marker signature and systemic IL-6 levels. Potentially providing a therapeutic option, cellular engagers of CD16 and SARS-CoV-2 proteins were found to rescue NK cell function in vitro. Together, our results reveal dysregulation in antibody-mediated cellular responses unique to MIS-C that likely contribute to the immune pathology of this disease.
Keywords	covid19
Language	English
Publishing date	2024-04-18
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2024.04.16.589585
Database	COVID19

Full text online

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Antibody-mediated cellular responses are dysregulated in Multisystem Inflammatory Syndrome in Children (MIS-C)

Miller, Jeffrey S / Bryceson, Yenan T / Wu, Jianming / John, Chandy C / Panoskaltsis-Mortari, Angela / Orioles, Alberto / Steiner, Marie E / Cheeran, Maxim C-J / Pravetoni, Marco / Hart, Geoffrey T

bioRxiv

Abstract	Multisystem Inflammatory Syndrome in Children (MIS-C) is a severe complication of SARS-CoV-2 infection characterized by multi-organ involvement and inflammation. Testing of cellular function ex vivo to understand the aberrant immune response in MIS-C is limited. Despite strong antibody production in MIS-C, SARS-CoV-2 nucleic acid testing can remain positive for 4-6 weeks after infection. Therefore, we hypothesized that dysfunctional cell-mediated antibody responses downstream of antibody production may be responsible for delayed clearance of viral products in MIS-C. In MIS-C, monocytes were hyperfunctional for phagocytosis and cytokine production, while natural killer (NK) cells were hypofunctional for both killing and cytokine production. The decreased NK cell cytotoxicity correlated with an NK exhaustion marker signature and systemic IL-6 levels. Potentially providing a therapeutic option, cellular engagers of CD16 and SARS-CoV-2 proteins were found to rescue NK cell function in vitro. Together, our results reveal dysregulation in antibody-mediated cellular responses unique to MIS-C that likely contribute to the immune pathology of this disease.
Keywords	covid19
Language	English
Publishing date	2024-04-18
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2024.04.16.589585
Database	COVID19

Full text online

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: De Novo Design of an Allosteric Metalloprotein Assembly with Strained Disulfide Bonds.

Churchfield, Lewis A / Medina-Morales, Annette / Brodin, Jeffrey D / Perez, Alfredo / Tezcan, F Akif

Journal of the American Chemical Society

2016 Volume 138, Issue 40, Page(s) 13163–13166

Abstract: A major goal in metalloprotein design is to build protein scaffolds from scratch that allow precise control over metal coordination. A particular challenge in this regard is the construction of allosteric systems in which metal coordination equilibria ... ...

Abstract	A major goal in metalloprotein design is to build protein scaffolds from scratch that allow precise control over metal coordination. A particular challenge in this regard is the construction of allosteric systems in which metal coordination equilibria are coupled to other chemical events that take place elsewhere in the protein scaffold. We previously developed a metal-templated self-assembly strategy (MeTIR) to build supramolecular protein complexes with tailorable interfaces from monomeric building blocks. Here, using this strategy, we have incorporated multiple disulfide bonds into the interfaces of a Zn-templated cytochrome cb
Language	English
Publishing date	2016-10-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.6b08458
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Bonn / Germany

Z 4' 55/32: Show issues
Z 7.3: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article: DNA-Mediated Cellular Delivery of Functional Enzymes

Brodin, Jeffrey D / McMillan Janet R / Mirkin Chad A / Sprangers Anthony J

Journal of the American Chemical Society. 2015 Dec. 02, v. 137, no. 47

2015

Abstract: We report a strategy for creating a new class of protein transfection materials composed of a functional protein core chemically modified with a dense shell of oligonucleotides. These materials retain the native structure and catalytic ability of the ... ...

Abstract	We report a strategy for creating a new class of protein transfection materials composed of a functional protein core chemically modified with a dense shell of oligonucleotides. These materials retain the native structure and catalytic ability of the hydrolytic enzyme Î²-galactosidase, which serves as the protein core, despite the functionalization of its surface with â¼25 DNA strands. The covalent attachment of a shell of oligonucleotides to the surface of Î²-galactosidase enhances its cellular uptake of by up to â¼280-fold and allows for the use of working concentrations as low as 100 pM enzyme. DNA-functionalized Î²-galactosidase retains its ability to catalyze the hydrolysis of Î²-glycosidic linkages once endocytosed, whereas equal concentrations of protein show little to no intracellular catalytic activity.
Keywords	beta-galactosidase ; catalytic activity ; DNA ; hydrolysis
Language	English
Dates of publication	2015-1202
Size	p. 14838-14841.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021%2Fjacs.5b09711
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 4' 55/32: Show issues
Z 7.3: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Modulating Nanoparticle Superlattice Structure Using Proteins with Tunable Bond Distributions.

McMillan, Janet R / Brodin, Jeffrey D / Millan, Jaime A / Lee, Byeongdu / Olvera de la Cruz, Monica / Mirkin, Chad A

Journal of the American Chemical Society

2017 Volume 139, Issue 5, Page(s) 1754–1757

Abstract: Herein, we investigate the use of proteins with tunable DNA modification distributions to modulate nanoparticle superlattice structure. Using beta-galactosidase (βgal) as a model system, we have employed the orthogonal chemical reactivities of surface ... ...

Abstract	Herein, we investigate the use of proteins with tunable DNA modification distributions to modulate nanoparticle superlattice structure. Using beta-galactosidase (βgal) as a model system, we have employed the orthogonal chemical reactivities of surface amines and thiols to synthesize protein-DNA conjugates with 36 evenly distributed or 8 specifically positioned oligonucleotides. When these are assembled into crystalline superlattices with gold nanoparticles, we find that the distribution of DNA modifications modulates the favored structure: βgal with uniformly distributed DNA bonding elements results in body-centered cubic crystals, whereas DNA functionalization of cysteines results in AB
Language	English
Publishing date	2017-02-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.6b11893
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Bonn / Germany

Z 4' 55/32: Show issues
Z 7.3: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Exceptionally stable, redox-active supramolecular protein assemblies with emergent properties.

Brodin, Jeffrey D / Carr, Jessica R / Sontz, Pamela A / Tezcan, F Akif

Proceedings of the National Academy of Sciences of the United States of America

2014 Volume 111, Issue 8, Page(s) 2897–2902

Abstract: The designed assembly of proteins into well-defined supramolecular architectures not only tests our understanding of protein-protein interactions, but it also provides an opportunity to tailor materials with new physical and chemical properties. ... ...

Abstract	The designed assembly of proteins into well-defined supramolecular architectures not only tests our understanding of protein-protein interactions, but it also provides an opportunity to tailor materials with new physical and chemical properties. Previously, we described that RIDC3, a designed variant of the monomeric electron transfer protein cytochrome cb562, could self-assemble through Zn(2+) coordination into uniform 1D nanotubes or 2D arrays with crystalline order. Here we show that these 1D and 2D RIDC3 assemblies display very high chemical stabilities owing to their metal-mediated frameworks, maintaining their structural order in ≥90% (vol/vol) of several polar organic solvents including tetrahydrofuran (THF) and isopropanol (iPrOH). In contrast, the unassembled RIDC3 monomers denature in ∼30% THF and 50% iPrOH, indicating that metal-mediated self-assembly also leads to considerable stabilization of the individual building blocks. The 1D and 2D RIDC3 assemblies are highly thermostable as well, remaining intact at up to ∼70 °C and ∼90 °C, respectively. The 1D nanotubes cleanly convert into the 2D arrays on heating above 70 °C, a rare example of a thermal crystalline-to-crystalline conversion in a biomolecular assembly. Finally, we demonstrate that the Zn-directed RIDC3 assemblies can be used to spatiotemporally control the templated growth of small Pt(0) nanocrystals. This emergent function is enabled by and absolutely dependent on both the supramolecular assembly of RIDC3 molecules (to form a periodically organized structural template) and their innate redox activities (to direct Pt(2+) reduction).
MeSH term(s)	2-Propanol ; Fluorescence ; Furans ; Metals/chemistry ; Microscopy, Atomic Force ; Microscopy, Electron, Transmission ; Multiprotein Complexes/chemical synthesis ; Nanotubes/chemistry ; Oxidation-Reduction ; Platinum ; Protein Interaction Domains and Motifs ; Protein Stability
Chemical Substances	Furans ; Metals ; Multiprotein Complexes ; tetrahydrofuran (3N8FZZ6PY4) ; Platinum (49DFR088MY) ; 2-Propanol (ND2M416302)
Language	English
Publishing date	2014-02-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1319866111
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

Kategorien

Inter-library loan at ZB MED

Full text online

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito