LIVIVO - Search results -

Search results

Result 1 - 8 of total 8

Search options

Article ; Online: NETosis Drives Blood Pressure Elevation and Vascular Dysfunction in Hypertension.

Krishnan, Jaya / Hennen, Elizabeth M / Ao, Mingfang / Kirabo, Annet / Ahmad, Taseer / de la Visitación, Néstor / Patrick, David M

Circulation research

2024

Abstract: Background: Neutrophil extracellular traps (NETs) are composed of nDNA, enzymes, and citrullinated histones that are expelled by neutrophils in the process of NETosis. NETs accumulate in the aorta and kidneys in hypertension. PAD4 (protein-arginine ... ...

Abstract	Background: Neutrophil extracellular traps (NETs) are composed of nDNA, enzymes, and citrullinated histones that are expelled by neutrophils in the process of NETosis. NETs accumulate in the aorta and kidneys in hypertension. PAD4 (protein-arginine deiminase-4) is a calcium-dependent enzyme that is essential for NETosis. TRPV4 (transient receptor potential cation channel subfamily V member 4) is a mechanosensitive calcium channel expressed in neutrophils. Thus, we hypothesize that NETosis contributes to hypertension via NET-mediated endothelial cell (EC) dysfunction. Methods: NETosis-deficient Results: Padi4 Conclusions: These observations identify a role of NETosis in the pathogenesis of hypertension. Moreover, they define an important role of EC stretch and TRPV4 as initiators of NETosis. Finally, they define a role of citrullinated histones as drivers of EC dysfunction in hypertension.
Language	English
Publishing date	2024-04-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.123.323897
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ui IV Zs.70: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Ui IV Zs.60: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)

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.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Immunoproteasomal Processing of IsoLG-Adducted Proteins Is Essential for Hypertension.

de la Visitación, Néstor / Chen, Wei / Krishnan, Jaya / Van Beusecum, Justin P / Amarnath, Venkataraman / Hennen, Elizabeth M / Zhao, Shilin / Saleem, Mohammad / Ao, Mingfang / Dikalov, Sergey I / Dikalova, Anna E / Harrison, David G / Patrick, David M

Circulation research

2024 Volume 134, Issue 10, Page(s) 1276–1291

Abstract: Background: Hypertension is characterized by CD8: Methods: IsoLG adduct processing was studied in murine dendritic cells (DCs), endothelial cells (ECs), and B8 fibroblasts. The role of the proteasome and the immunoproteasome in Ang II (angiotensin II) ...

Abstract	Background: Hypertension is characterized by CD8 Methods: IsoLG adduct processing was studied in murine dendritic cells (DCs), endothelial cells (ECs), and B8 fibroblasts. The role of the proteasome and the immunoproteasome in Ang II (angiotensin II)-induced hypertension was studied in Results: We found that oxidant stress increases the presence of isoLG adducts within MHC-I (class I major histocompatibility complex), and immunoproteasome overexpression augments this. Pharmacological or genetic inhibition of the immunoproteasome attenuated hypertension and tissue inflammation. Conditional deletion of LMP7 in either DCs or ECs attenuated hypertension and vascular inflammation. Finally, we defined the role of the innate immune receptors STING (stimulator of interferon genes) and TLR7/8 (toll-like receptor 7/8) as drivers of LMP7 expression in ECs. Conclusions: These studies define a previously unknown role of the immunoproteasome in DCs and ECs in CD8
MeSH term(s)	Animals ; Proteasome Endopeptidase Complex/metabolism ; Hypertension/metabolism ; Hypertension/immunology ; Mice, Inbred C57BL ; Dendritic Cells/immunology ; Dendritic Cells/metabolism ; Mice ; Mice, Knockout ; CD8-Positive T-Lymphocytes/immunology ; Bortezomib/pharmacology ; Angiotensin II ; Male ; Oxidative Stress ; Proteasome Inhibitors/pharmacology ; Histocompatibility Antigens Class I/metabolism ; Histocompatibility Antigens Class I/genetics ; Lymphocyte Activation ; Cells, Cultured ; Fibroblasts/metabolism ; Endothelial Cells/metabolism ; Endothelial Cells/immunology ; Oligopeptides
Chemical Substances	Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Bortezomib (69G8BD63PP) ; LMP7 protein (EC 3.4.25.1) ; Angiotensin II (11128-99-7) ; PR-957 ; Proteasome Inhibitors ; Histocompatibility Antigens Class I ; Oligopeptides
Language	English
Publishing date	2024-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80100-8
ISSN	1524-4571 ; 0009-7330 ; 0931-6876
ISSN (online)	1524-4571
ISSN	0009-7330 ; 0931-6876
DOI	10.1161/CIRCRESAHA.124.324068
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ui IV Zs.70: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Ui IV Zs.60: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: IsoLGs (Isolevuglandins) Drive Neutrophil Migration in Hypertension and Are Essential for the Formation of Neutrophil Extracellular Traps.

Krishnan, Jaya / de la Visitación, Néstor / Hennen, Elizabeth M / Amarnath, Venkataraman / Harrison, David G / Patrick, David M

Hypertension (Dallas, Tex. : 1979)

2022 Volume 79, Issue 8, Page(s) 1644–1655

Abstract: Background: IsoLGs (isolevuglandins) are electrophilic products of lipid peroxidation formed in the presence of reactive oxygen species. IsoLGs contribute to hypertension by an unknown mechanism. Studies have shown that reactive oxygen species ... ...

Abstract	Background: IsoLGs (isolevuglandins) are electrophilic products of lipid peroxidation formed in the presence of reactive oxygen species. IsoLGs contribute to hypertension by an unknown mechanism. Studies have shown that reactive oxygen species production drives the formation of neutrophil extracellular traps (NETs) and that NETs accumulate within the aorta and kidneys of patients with hypertension. The purpose of this study was to determine the role of isoLGs in neutrophil migration and NET formation (NETosis) in hypertension. Methods: Mice were treated with Ang II (angiotensin II) and the specific isoLG scavenger 2-hydroxybenzylamine and examined for tissue neutrophil and NET accumulation by single-cell sequencing and flow cytometry. Isolated human neutrophils were studied to determine the role of isoLGs in NETosis and neutrophil chromatin expansion by immunofluorescence and live cell confocal microscopy. Results: Single-cell sequencing performed on sham, Ang II, and Ang II+2-hydroxybenzylamine treated mice revealed neutrophils as a primary target of 2-hydroxybenzylamine. Peripheral neutrophil migration, aortic NET accumulation, and renal NET accumulation is blocked with 2-hydroxybenzylamine treatment. In isolated human neutrophils, isoLGs accumulate during NETosis and scavenging of isoLGs prevents NETosis. IsoLGs drive neutrophil chromatin expansion during NETosis and disrupt nucleosome structure. Conclusions: These observations identified a critical role of isoLGs in neutrophil migration and NETosis in hypertension and provide a potential therapy for NET-associated diseases including hypertension and associated end organ damage.
MeSH term(s)	Animals ; Chromatin ; Extracellular Traps ; Humans ; Hypertension ; Lipids ; Mice ; Neutrophils ; Reactive Oxygen Species
Chemical Substances	Chromatin ; Lipids ; Reactive Oxygen Species ; isolevuglandin
Language	English
Publishing date	2022-06-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	423736-5
ISSN	1524-4563 ; 0194-911X ; 0362-4323
ISSN (online)	1524-4563
ISSN	0194-911X ; 0362-4323
DOI	10.1161/HYPERTENSIONAHA.122.19305
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1488: 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

Article ; Online: Rac1 promotes kidney collecting duct repair by mechanically coupling cell morphology to mitotic entry.

Bock, Fabian / Dong, Xinyu / Li, Shensen / Viquez, Olga M / Sha, Eric / Tantengco, Matthew / Hennen, Elizabeth M / Plosa, Erin / Ramezani, Alireza / Brown, Kyle L / Whang, Young Mi / Terker, Andrew S / Arroyo, Juan Pablo / Harrison, David G / Fogo, Agnes / Brakebusch, Cord H / Pozzi, Ambra / Zent, Roy

Science advances

2024 Volume 10, Issue 6, Page(s) eadi7840

Abstract: Prolonged obstruction of the ureter, which leads to injury of the kidney collecting ducts, results in permanent structural damage, while early reversal allows for repair. Cell structure is defined by the actin cytoskeleton, which is dynamically organized ...

Abstract	Prolonged obstruction of the ureter, which leads to injury of the kidney collecting ducts, results in permanent structural damage, while early reversal allows for repair. Cell structure is defined by the actin cytoskeleton, which is dynamically organized by small Rho guanosine triphosphatases (GTPases). In this study, we identified the Rho GTPase, Rac1, as a driver of postobstructive kidney collecting duct repair. After the relief of ureteric obstruction, Rac1 promoted actin cytoskeletal reconstitution, which was required to maintain normal mitotic morphology allowing for successful cell division. Mechanistically, Rac1 restricted excessive actomyosin activity that stabilized the negative mitotic entry kinase Wee1. This mechanism ensured mechanical G
MeSH term(s)	Kidney Tubules, Collecting/metabolism ; rac1 GTP-Binding Protein/metabolism ; Cytoskeleton/metabolism ; Actins/metabolism ; Actin Cytoskeleton/metabolism
Chemical Substances	rac1 GTP-Binding Protein (EC 3.6.5.2) ; Actins
Language	English
Publishing date	2024-02-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.adi7840
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Immunoproteasomal Processing of Isolevuglandin Adducts in Hypertension.

de la Visitación, Néstor / Chen, Wei / Krishnan, Jaya / Van Beusecum, Justin P / Amarnath, Venkataraman / Hennen, Elizabeth M / Zhao, Shilin / Saleem, Mohammad / Ao, Mingfang / Harrison, David G / Patrick, David M

bioRxiv : the preprint server for biology

2023

Abstract: Isolevuglandins (isoLGs) are lipid aldehydes that form in the presence of reactive oxygen species (ROS) and drive immune activation. We found that isoLG-adducts are presented within the context of major histocompatibility complexes (MHC-I) by an ... ...

Abstract	Isolevuglandins (isoLGs) are lipid aldehydes that form in the presence of reactive oxygen species (ROS) and drive immune activation. We found that isoLG-adducts are presented within the context of major histocompatibility complexes (MHC-I) by an immunoproteasome dependent mechanism. Pharmacologic inhibition of LMP7, the chymotrypsin subunit of the immunoproteasome, attenuates hypertension and tissue inflammation in the angiotensin II (Ang II) model of hypertension. Genetic loss of function of all immunoproteasome subunits or conditional deletion of LMP7 in dendritic cell (DCs) or endothelial cells (ECs) attenuated hypertension, reduced aortic T cell infiltration, and reduced isoLG-adduct MHC-I interaction. Furthermore, isoLG adducts structurally resemble double-stranded DNA and contribute to the activation of STING in ECs. These studies define a critical role of the immunoproteasome in the processing and presentation of isoLG-adducts. Moreover they define a role of LMP7 as a regulator of T cell activation and tissue infiltration in hypertension.
Language	English
Publishing date	2023-04-12
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.04.10.536054
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: Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first 6 months of the COVID-19 pandemic.

Lubin, Joseph H / Zardecki, Christine / Dolan, Elliott M / Lu, Changpeng / Shen, Zhuofan / Dutta, Shuchismita / Westbrook, John D / Hudson, Brian P / Goodsell, David S / Williams, Jonathan K / Voigt, Maria / Sarma, Vidur / Xie, Lingjun / Venkatachalam, Thejasvi / Arnold, Steven / Alfaro Alvarado, Luz Helena / Catalfano, Kevin / Khan, Aaliyah / McCarthy, Erika /

Staggers, Sophia / Tinsley, Brea / Trudeau, Alan / Singh, Jitendra / Whitmore, Lindsey / Zheng, Helen / Benedek, Matthew / Currier, Jenna / Dresel, Mark / Duvvuru, Ashish / Dyszel, Britney / Fingar, Emily / Hennen, Elizabeth M / Kirsch, Michael / Khan, Ali A / Labrie-Cleary, Charlotte / Laporte, Stephanie / Lenkeit, Evan / Martin, Kailey / Orellana, Marilyn / Ortiz-Alvarez de la Campa, Melanie / Paredes, Isaac / Wheeler, Baleigh / Rupert, Allison / Sam, Andrew / See, Katherine / Soto Zapata, Santiago / Craig, Paul A / Hall, Bonnie L / Jiang, Jennifer / Koeppe, Julia R / Mills, Stephen A / Pikaart, Michael J / Roberts, Rebecca / Bromberg, Yana / Hoyer, J Steen / Duffy, Siobain / Tischfield, Jay / Ruiz, Francesc X / Arnold, Eddy / Baum, Jean / Sandberg, Jesse / Brannigan, Grace / Khare, Sagar D / Burley, Stephen K

Proteins

2021 Volume 90, Issue 5, Page(s) 1054–1080

Abstract: Understanding the molecular evolution of the SARS-CoV-2 virus as it continues to spread in communities around the globe is important for mitigation and future pandemic preparedness. Three-dimensional structures of SARS-CoV-2 proteins and those of other ... ...

Abstract	Understanding the molecular evolution of the SARS-CoV-2 virus as it continues to spread in communities around the globe is important for mitigation and future pandemic preparedness. Three-dimensional structures of SARS-CoV-2 proteins and those of other coronavirusess archived in the Protein Data Bank were used to analyze viral proteome evolution during the first 6 months of the COVID-19 pandemic. Analyses of spatial locations, chemical properties, and structural and energetic impacts of the observed amino acid changes in >48 000 viral isolates revealed how each one of 29 viral proteins have undergone amino acid changes. Catalytic residues in active sites and binding residues in protein-protein interfaces showed modest, but significant, numbers of substitutions, highlighting the mutational robustness of the viral proteome. Energetics calculations showed that the impact of substitutions on the thermodynamic stability of the proteome follows a universal bi-Gaussian distribution. Detailed results are presented for potential drug discovery targets and the four structural proteins that comprise the virion, highlighting substitutions with the potential to impact protein structure, enzyme activity, and protein-protein and protein-nucleic acid interfaces. Characterizing the evolution of the virus in three dimensions provides testable insights into viral protein function and should aid in structure-based drug discovery efforts as well as the prospective identification of amino acid substitutions with potential for drug resistance.
MeSH term(s)	Amino Acids ; COVID-19 ; Humans ; Pandemics ; Prospective Studies ; Proteome ; SARS-CoV-2 ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemical Substances	Amino Acids ; Proteome ; Viral Proteins
Language	English
Publishing date	2021-10-09
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	806683-8
ISSN	1097-0134 ; 0887-3585
ISSN (online)	1097-0134
ISSN	0887-3585
DOI	10.1002/prot.26250
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 2291: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article: Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first six months of the COVID-19 pandemic.

Lubin, Joseph H / Zardecki, Christine / Dolan, Elliott M / Lu, Changpeng / Shen, Zhuofan / Dutta, Shuchismita / Westbrook, John D / Hudson, Brian P / Goodsell, David S / Williams, Jonathan K / Voigt, Maria / Sarma, Vidur / Xie, Lingjun / Venkatachalam, Thejasvi / Arnold, Steven / Alvarado, Luz Helena Alfaro / Catalfano, Kevin / Khan, Aaliyah / McCarthy, Erika /

Staggers, Sophia / Tinsley, Brea / Trudeau, Alan / Singh, Jitendra / Whitmore, Lindsey / Zheng, Helen / Benedek, Matthew / Currier, Jenna / Dresel, Mark / Duvvuru, Ashish / Dyszel, Britney / Fingar, Emily / Hennen, Elizabeth M / Kirsch, Michael / Khan, Ali A / Labrie-Cleary, Charlotte / Laporte, Stephanie / Lenkeit, Evan / Martin, Kailey / Orellana, Marilyn / de la Campa, Melanie Ortiz-Alvarez / Paredes, Isaac / Wheeler, Baleigh / Rupert, Allison / Sam, Andrew / See, Katherine / Zapata, Santiago Soto / Craig, Paul A / Hall, Bonnie L / Jiang, Jennifer / Koeppe, Julia R / Mills, Stephen A / Pikaart, Michael J / Roberts, Rebecca / Bromberg, Yana / Hoyer, J Steen / Duffy, Siobain / Tischfield, Jay / Ruiz, Francesc X / Arnold, Eddy / Baum, Jean / Sandberg, Jesse / Brannigan, Grace / Khare, Sagar D / Burley, Stephen K

bioRxiv : the preprint server for biology

2020

Abstract: Three-dimensional structures of SARS-CoV-2 and other coronaviral proteins archived in the Protein Data Bank were used to analyze viral proteome evolution during the first six months of the COVID-19 pandemic. Analyses of spatial locations, chemical ... ...

Abstract	Three-dimensional structures of SARS-CoV-2 and other coronaviral proteins archived in the Protein Data Bank were used to analyze viral proteome evolution during the first six months of the COVID-19 pandemic. Analyses of spatial locations, chemical properties, and structural and energetic impacts of the observed amino acid changes in >48,000 viral proteome sequences showed how each one of the 29 viral study proteins have undergone amino acid changes. Structural models computed for every unique sequence variant revealed that most substitutions map to protein surfaces and boundary layers with a minority affecting hydrophobic cores. Conservative changes were observed more frequently in cores
Language	English
Publishing date	2020-12-07
Publishing country	United States
Document type	Preprint
DOI	10.1101/2020.12.01.406637
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: Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first six months of the COVID-19 pandemic

Lubin, Joseph H. / Zardecki, Christine / Dolan, Elliott M. / Lu, Changpeng / Shen, Zhuofan / Dutta, Shuchismita / Westbrook, John D. / Hudson, Brian P. / Goodsell, David S. / Williams, Jonathan K. / Voigt, Maria / Sarma, Vidur / Xie, Lingjun / Venkatachalam, Thejasvi / Arnold, Steven / Alfaro Alvarado, Luz Helena / Catalfano, Kevin / Khan, Aaliyah / McCarthy, Erika /

Staggers, Sophia / Tinsley, Brea / Trudeau, Alan / Singh, Jitendra / Whitmore, Lindsey / Zheng, Helen / Benedek, Matthew / Currier, Jenna / Dresel, Mark / Duvvuru, Ashish / Dyszel, Britney / Fingar, Emily / Hennen, Elizabeth M. / Kirsch, Michael / Khan, Ali A. / Labrie-Cleary, Charlotte / Laporte, Stephanie / Lenkeit, Evan / Martin, Kailey / Orellana, Marilyn / Ortiz-Alvarez de la Campa, Melanie / Paredes, Isaac / Wheeler, Baleigh / Rupert, Allison / Sam, Andrew / See, Katherine / Soto Zapata, Santiago / Craig, Paul A. / Hall, Bonnie L. / Jiang, Jennifer / Koeppe, Julia R. / Mills, Stephen A. / Pikaart, Michael J. / Roberts, Rebecca / Bromberg, Yana / Hoyer, J. Steen / Duffy, Siobain / Tischfield, Jay / Ruiz, Francesc X. / Arnold, Eddy / Baum, Jean / Sandberg, Jesse / Brannigan, Grace / Khare, Sagar D. / Burley, Stephen K.

bioRxiv

Abstract	Three-dimensional structures of SARS-CoV-2 and other coronaviral proteins archived in the Protein Data Bank were used to analyze viral proteome evolution during the first six months of the COVID-19 pandemic. Analyses of spatial locations, chemical properties, and structural and energetic impacts of the observed amino acid changes in >48,000 viral proteome sequences showed how each one of the 29 viral study proteins have undergone amino acid changes. Structural models computed for every unique sequence variant revealed that most substitutions map to protein surfaces and boundary layers with a minority affecting hydrophobic cores. Conservative changes were observed more frequently in cores versus boundary layers/surfaces. Active sites and protein-protein interfaces showed modest numbers of substitutions. Energetics calculations showed that the impact of substitutions on the thermodynamic stability of the proteome follows a universal bi-Gaussian distribution. Detailed results are presented for six drug discovery targets and four structural proteins comprising the virion, highlighting substitutions with the potential to impact protein structure, enzyme activity, and functional interfaces. Characterizing the evolution of the virus in three dimensions provides testable insights into viral protein function and should aid in structure-based drug discovery efforts as well as the prospective identification of amino acid substitutions with potential for drug resistance.
Keywords	covid19
Language	English
Publishing date	2020-12-01
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.12.01.406637
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.

To top

Search results

Search options

Article ; Online: NETosis Drives Blood Pressure Elevation and Vascular Dysfunction in Hypertension.

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Article ; Online: Immunoproteasomal Processing of IsoLG-Adducted Proteins Is Essential for Hypertension.

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Article ; Online: IsoLGs (Isolevuglandins) Drive Neutrophil Migration in Hypertension and Are Essential for the Formation of Neutrophil Extracellular Traps.

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Article ; Online: Rac1 promotes kidney collecting duct repair by mechanically coupling cell morphology to mitotic entry.

More links

Kategorien

Order via subito

Article: Immunoproteasomal Processing of Isolevuglandin Adducts in Hypertension.

More links

Kategorien

Inter-library loan at ZB MED

Article ; Online: Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first 6 months of the COVID-19 pandemic.

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Article: Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first six months of the COVID-19 pandemic.

More links

Kategorien

Inter-library loan at ZB MED

Article ; Online: Evolution of the SARS-CoV-2 proteome in three dimensions (3D) during the first six months of the COVID-19 pandemic

Full text online

Kategorien

Inter-library loan at ZB MED