LIVIVO - Search results -

Search results

Result 1 - 10 of total 111

Search options

Article ; Online: SPFH protein cage - one ring to rule them all.

Daumke, Oliver / Lewin, Gary R

2021 Volume 32, Issue 2, Page(s) 117–118

MeSH term(s)	Amino Acid Sequence ; Membrane Proteins/metabolism
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2021-12-18
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	1319303-x
ISSN	1748-7838 ; 1001-0602
ISSN (online)	1748-7838
ISSN	1001-0602
DOI	10.1038/s41422-021-00605-7
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 5283: 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

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 ▾

Article ; Online: Structural insights into the activation mechanism of antimicrobial GBP1.

Weismehl, Marius / Chu, Xiaofeng / Kutsch, Miriam / Lauterjung, Paul / Herrmann, Christian / Kudryashev, Misha / Daumke, Oliver

The EMBO journal

2024 Volume 43, Issue 4, Page(s) 615–636

Abstract: The dynamin-related human guanylate-binding protein 1 (GBP1) mediates host defenses against microbial pathogens. Upon GTP binding and hydrolysis, auto-inhibited GBP1 monomers dimerize and assemble into soluble and membrane-bound oligomers, which are ... ...

Abstract	The dynamin-related human guanylate-binding protein 1 (GBP1) mediates host defenses against microbial pathogens. Upon GTP binding and hydrolysis, auto-inhibited GBP1 monomers dimerize and assemble into soluble and membrane-bound oligomers, which are crucial for innate immune responses. How higher-order GBP1 oligomers are built from dimers, and how assembly is coordinated with nucleotide-dependent conformational changes, has remained elusive. Here, we present cryo-electron microscopy-based structural data of soluble and membrane-bound GBP1 oligomers, which show that GBP1 assembles in an outstretched dimeric conformation. We identify a surface-exposed helix in the large GTPase domain that contributes to the oligomerization interface, and we probe its nucleotide- and dimerization-dependent movements that facilitate the formation of an antimicrobial protein coat on a gram-negative bacterial pathogen. Our results reveal a sophisticated activation mechanism for GBP1, in which nucleotide-dependent structural changes coordinate dimerization, oligomerization, and membrane binding to allow encapsulation of pathogens within an antimicrobial protein coat.
MeSH term(s)	Humans ; Cryoelectron Microscopy ; GTP Phosphohydrolases/metabolism ; Dynamins/metabolism ; Nucleotides/metabolism ; Anti-Infective Agents ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/metabolism
Chemical Substances	GTP Phosphohydrolases (EC 3.6.1.-) ; Dynamins (EC 3.6.5.5) ; Nucleotides ; Anti-Infective Agents ; GBP1 protein, human ; GTP-Binding Proteins (EC 3.6.1.-)
Language	English
Publishing date	2024-01-24
Publishing country	England
Document type	Journal Article
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.1038/s44318-023-00023-y
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1808: 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)
Zs.MG 100: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Pathogenic mutations of human phosphorylation sites affect protein-protein interactions.

Rrustemi, Trendelina / Meyer, Katrina / Roske, Yvette / Uyar, Bora / Akalin, Altuna / Imami, Koshi / Ishihama, Yasushi / Daumke, Oliver / Selbach, Matthias

Nature communications

2024 Volume 15, Issue 1, Page(s) 3146

Abstract: Despite their lack of a defined 3D structure, intrinsically disordered regions (IDRs) of proteins play important biological roles. Many IDRs contain short linear motifs (SLiMs) that mediate protein-protein interactions (PPIs), which can be regulated by ... ...

Abstract	Despite their lack of a defined 3D structure, intrinsically disordered regions (IDRs) of proteins play important biological roles. Many IDRs contain short linear motifs (SLiMs) that mediate protein-protein interactions (PPIs), which can be regulated by post-translational modifications like phosphorylation. 20% of pathogenic missense mutations are found in IDRs, and understanding how such mutations affect PPIs is essential for unraveling disease mechanisms. Here, we employ peptide-based interaction proteomics to investigate 36 disease-associated mutations affecting phosphorylation sites. Our results unveil significant differences in interactomes between phosphorylated and non-phosphorylated peptides, often due to disrupted phosphorylation-dependent SLiMs. We focused on a mutation of a serine phosphorylation site in the transcription factor GATAD1, which causes dilated cardiomyopathy. We find that this phosphorylation site mediates interaction with 14-3-3 family proteins. Follow-up experiments reveal the structural basis of this interaction and suggest that 14-3-3 binding affects GATAD1 nucleocytoplasmic transport by masking a nuclear localisation signal. Our results demonstrate that pathogenic mutations of human phosphorylation sites can significantly impact protein-protein interactions, offering insights into potential molecular mechanisms underlying pathogenesis.
MeSH term(s)	Humans ; Phosphorylation ; Peptides/metabolism ; Protein Processing, Post-Translational ; Gene Expression Regulation ; Mutation ; Intrinsically Disordered Proteins/metabolism ; Protein Binding ; Binding Sites ; Eye Proteins/genetics
Chemical Substances	Peptides ; Intrinsically Disordered Proteins ; GATAD1 protein, human ; Eye Proteins
Language	English
Publishing date	2024-04-11
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-024-46794-8
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Competitively disrupting the neutrophil-specific receptor-autoantigen CD177:proteinase 3 membrane complex reduces anti-PR3 antibody-induced neutrophil activation.

Marino, Stephen F / Jerke, Uwe / Rolle, Susanne / Daumke, Oliver / Kettritz, Ralph

The Journal of biological chemistry

2022 Volume 298, Issue 3, Page(s) 101598

Abstract: CD177 is a neutrophil-specific receptor presenting the proteinase 3 (PR3) autoantigen on the neutrophil surface. CD177 expression is restricted to a neutrophil subset, resulting in ... ...

Abstract	CD177 is a neutrophil-specific receptor presenting the proteinase 3 (PR3) autoantigen on the neutrophil surface. CD177 expression is restricted to a neutrophil subset, resulting in CD177
MeSH term(s)	Antibodies, Antineutrophil Cytoplasmic/immunology ; Antibodies, Monoclonal ; Autoantigens/immunology ; Cell Membrane/immunology ; GPI-Linked Proteins/immunology ; Granulomatosis with Polyangiitis/immunology ; Humans ; Isoantigens/metabolism ; Myeloblastin/metabolism ; Neutrophil Activation ; Neutrophils/immunology ; Receptors, Cell Surface/immunology ; Superoxides/immunology
Chemical Substances	Antibodies, Antineutrophil Cytoplasmic ; Antibodies, Monoclonal ; Autoantigens ; CD177 protein, human ; GPI-Linked Proteins ; Isoantigens ; Receptors, Cell Surface ; Superoxides (11062-77-4) ; Myeloblastin (EC 3.4.21.76)
Language	English
Publishing date	2022-01-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.101598
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: 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: Mitochondrial Homeostasis: How Do Dimers of Mitofusins Mediate Mitochondrial Fusion?

Daumke, Oliver / Roux, Aurélien

Current biology : CB

2017 Volume 27, Issue 9, Page(s) R353–R356

Abstract: Mitochondria have high fusion and fission rates to maintain their size and number throughout the cell cycle. How is fusion mediated? New structural studies propose mechanisms by which the dynamin-like mitofusin proteins promote fusion of mitochondria. ...

Abstract	Mitochondria have high fusion and fission rates to maintain their size and number throughout the cell cycle. How is fusion mediated? New structural studies propose mechanisms by which the dynamin-like mitofusin proteins promote fusion of mitochondria.
MeSH term(s)	Homeostasis ; Membrane Fusion ; Mitochondria/metabolism ; Mitochondrial Dynamics ; Mitochondrial Membrane Transport Proteins/chemistry ; Mitochondrial Membrane Transport Proteins/metabolism ; Mitochondrial Membranes/metabolism ; Protein Multimerization
Chemical Substances	Mitochondrial Membrane Transport Proteins
Language	English
Publishing date	2017-05-08
Publishing country	England
Document type	Journal Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2017.03.024
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3208: 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 ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Structural analysis of PLD3 reveals insights into the mechanism of lysosomal 5' exonuclease-mediated nucleic acid degradation.

Roske, Yvette / Cappel, Cedric / Cremer, Nils / Hoffmann, Patrick / Koudelka, Tomas / Tholey, Andreas / Heinemann, Udo / Daumke, Oliver / Damme, Markus

Nucleic acids research

2023 Volume 52, Issue 1, Page(s) 370–384

Abstract: The phospholipase D (PLD) family is comprised of enzymes bearing phospholipase activity towards lipids or endo- and exonuclease activity towards nucleic acids. PLD3 is synthesized as a type II transmembrane protein and proteolytically cleaved in ... ...

Abstract	The phospholipase D (PLD) family is comprised of enzymes bearing phospholipase activity towards lipids or endo- and exonuclease activity towards nucleic acids. PLD3 is synthesized as a type II transmembrane protein and proteolytically cleaved in lysosomes, yielding a soluble active form. The deficiency of PLD3 leads to the slowed degradation of nucleic acids in lysosomes and chronic activation of nucleic acid-specific intracellular toll-like receptors. While the mechanism of PLD phospholipase activity has been extensively characterized, not much is known about how PLDs bind and hydrolyze nucleic acids. Here, we determined the high-resolution crystal structure of the luminal N-glycosylated domain of human PLD3 in its apo- and single-stranded DNA-bound forms. PLD3 has a typical phospholipase fold and forms homodimers with two independent catalytic centers via a newly identified dimerization interface. The structure of PLD3 in complex with an ssDNA-derived thymidine product in the catalytic center provides insights into the substrate binding mode of nucleic acids in the PLD family. Our structural data suggest a mechanism for substrate binding and nuclease activity in the PLD family and provide the structural basis to design immunomodulatory drugs targeting PLD3.
MeSH term(s)	Humans ; Lysosomes/metabolism ; Phospholipase D/chemistry ; Phospholipases ; Exodeoxyribonucleases/chemistry
Chemical Substances	Phospholipase D (EC 3.1.4.4) ; Phospholipases (EC 3.1.-) ; PLD3 protein, human (EC 3.1.4.4) ; Exodeoxyribonucleases (EC 3.1.-)
Language	English
Publishing date	2023-11-23
Publishing country	England
Document type	Journal Article
ZDB-ID	186809-3
ISSN	1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
ISSN (online)	1362-4962 ; 1362-4954
ISSN	0301-5610 ; 0305-1048
DOI	10.1093/nar/gkad1114
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1067: 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: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.

Daumke, Oliver / Praefcke, Gerrit J K

Biopolymers

2017 Volume 109, Issue 2

Language	English
Publishing date	2017-11-17
Publishing country	United States
Document type	Journal Article ; Published Erratum
ZDB-ID	1123-x
ISSN	1097-0282 ; 0006-3525
ISSN (online)	1097-0282
ISSN	0006-3525
DOI	10.1002/bip.23079
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 77: 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: hGBP1 Coordinates Chlamydia Restriction and Inflammasome Activation through Sequential GTP Hydrolysis.

Xavier, Audrey / Al-Zeer, Munir A / Meyer, Thomas F / Daumke, Oliver

Cell reports

2020 Volume 31, Issue 7, Page(s) 107667

Abstract: Human guanylate binding protein 1 (hGBP1) belongs to the dynamin superfamily of GTPases and conveys host defense against intracellular bacteria and parasites. During infection, hGBP1 is recruited to pathogen-containing vacuoles, such as Chlamydia ... ...

Abstract	Human guanylate binding protein 1 (hGBP1) belongs to the dynamin superfamily of GTPases and conveys host defense against intracellular bacteria and parasites. During infection, hGBP1 is recruited to pathogen-containing vacuoles, such as Chlamydia trachomatis inclusions, restricts pathogenic growth, and induces the activation of the inflammasome pathway. hGBP1 has a unique catalytic activity to hydrolyze guanosine triphosphate (GTP) to guanosine monophosphate (GMP) in two consecutive cleavage steps. However, the functional significance of this activity in host defense remains elusive. Here, we generate a structure-guided mutant that specifically abrogates GMP production, while maintaining fast cooperative GTP hydrolysis. Complementation experiments in human monocytes/macrophages show that hGBP1-mediated GMP production is dispensable for restricting Chlamydia trachomatis growth but is necessary for inflammasome activation. Mechanistically, GMP is catabolized to uric acid, which in turn activates the NLRP3 inflammasome. Our study demonstrates that the unique enzymology of hGBP1 coordinates bacterial growth restriction and inflammasome signaling.
MeSH term(s)	Chlamydia Infections/immunology ; Chlamydia Infections/metabolism ; Chlamydia Infections/microbiology ; Chlamydia trachomatis/growth & development ; Cyclic GMP ; GTP-Binding Proteins/chemistry ; GTP-Binding Proteins/genetics ; GTP-Binding Proteins/immunology ; GTP-Binding Proteins/metabolism ; Guanine Nucleotides/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Hydrolysis ; Inflammasomes/immunology ; Inflammasomes/metabolism ; Macrophages/immunology ; Macrophages/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein ; Signal Transduction ; THP-1 Cells ; Uric Acid/metabolism
Chemical Substances	GBP1 protein, human ; Guanine Nucleotides ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Uric Acid (268B43MJ25) ; Guanosine Triphosphate (86-01-1) ; GTP-Binding Proteins (EC 3.6.1.-) ; Cyclic GMP (H2D2X058MU)
Language	English
Publishing date	2020-05-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2020.107667
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Protein-mediated membrane remodeling.

Daumke, Oliver / Unger, Vinzenz M

Journal of structural biology

2016 Volume 196, Issue 1, Page(s) 1–2

MeSH term(s)	Animals ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Cell Membrane/ultrastructure ; Cell Physiological Phenomena ; Humans ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Microscopy, Electron ; Models, Molecular ; Organelles/metabolism ; Organelles/ultrastructure ; Protein Conformation
Chemical Substances	Membrane Proteins
Language	English
Publishing date	2016-09-13
Publishing country	United States
Document type	Editorial ; Introductory Journal Article
ZDB-ID	1032718-6
ISSN	1095-8657 ; 1047-8477
ISSN (online)	1095-8657
ISSN	1047-8477
DOI	10.1016/j.jsb.2016.09.002
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1428: 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: Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.

Daumke, Oliver / Praefcke, Gerrit J K

Biopolymers

2016 Volume 105, Issue 8, Page(s) 580–593

Abstract: Dynamin superfamily proteins are multidomain mechano-chemical GTPases which are implicated in nucleotide-dependent membrane remodeling events. A prominent feature of these proteins is their assembly- stimulated mechanism of GTP hydrolysis. The molecular ... ...

Abstract	Dynamin superfamily proteins are multidomain mechano-chemical GTPases which are implicated in nucleotide-dependent membrane remodeling events. A prominent feature of these proteins is their assembly- stimulated mechanism of GTP hydrolysis. The molecular basis for this reaction has been initially clarified for the dynamin-related guanylate binding protein 1 (GBP1) and involves the transient dimerization of the GTPase domains in a parallel head-to-head fashion. A catalytic arginine finger from the phosphate binding (P-) loop is repositioned toward the nucleotide of the same molecule to stabilize the transition state of GTP hydrolysis. Dynamin uses a related dimerization-dependent mechanism, but instead of the catalytic arginine, a monovalent cation is involved in catalysis. Still another variation of the GTP hydrolysis mechanism has been revealed for the dynamin-like Irga6 which bears a glycine at the corresponding position in the P-loop. Here, we highlight conserved and divergent features of GTP hydrolysis in dynamin superfamily proteins and show how nucleotide binding and hydrolysis are converted into mechano-chemical movements. We also describe models how the energy of GTP hydrolysis can be harnessed for diverse membrane remodeling events, such as membrane fission or fusion. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 580-593, 2016.
MeSH term(s)	Animals ; Dynamins/chemistry ; Dynamins/metabolism ; GTP-Binding Proteins/chemistry ; GTP-Binding Proteins/metabolism ; Guanosine Triphosphate/chemistry ; Guanosine Triphosphate/metabolism ; Humans ; Hydrolysis ; Models, Chemical ; Protein Domains ; Protein Multimerization ; Protein Structure, Secondary
Chemical Substances	GBP1 protein, human ; Guanosine Triphosphate (86-01-1) ; GTP-Binding Proteins (EC 3.6.1.-) ; Dynamins (EC 3.6.5.5)
Language	English
Publishing date	2016-04-09
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1123-x
ISSN	1097-0282 ; 0006-3525
ISSN (online)	1097-0282
ISSN	0006-3525
DOI	10.1002/bip.22855
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 77: 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 ▾

To top

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito