LIVIVO - Search results -

Search results

Result 1 - 10 of total 81

Search options

Article ; Online: Unraveling the mechanisms of calcium-dependent secretion.

Anantharam, Arun / Kreutzberger, Alex J B

2019 Volume 151, Issue 4, Page(s) 417–434

Abstract: ... ...

Abstract	Ca
MeSH term(s)	Animals ; Biological Transport ; Calcium/metabolism ; Cell Membrane/physiology ; Exocytosis/physiology ; Liposomes ; Signal Transduction/physiology
Chemical Substances	Liposomes ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2019-02-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	3118-5
ISSN	1540-7748 ; 0022-1295
ISSN (online)	1540-7748
ISSN	0022-1295
DOI	10.1085/jgp.201812298
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.150: 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: Single-Molecule Analyses Reveal Rhomboid Proteins Are Strict and Functional Monomers in the Membrane.

Kreutzberger, Alex J B / Urban, Siniša

Biophysical journal

2018 Volume 115, Issue 9, Page(s) 1755–1761

Abstract: Intramembrane proteases hydrolyze peptide bonds within the membrane as a regulatory paradigm that is conserved across all forms of cellular life. Many of these enzymes are thought to be oligomeric, and that their resulting quaternary interactions form ... ...

Abstract	Intramembrane proteases hydrolyze peptide bonds within the membrane as a regulatory paradigm that is conserved across all forms of cellular life. Many of these enzymes are thought to be oligomeric, and that their resulting quaternary interactions form the basis of their regulation. However, technical limitations have precluded directly determining the oligomeric state of intramembrane proteases in any membrane. Using single-molecule photobleaching, we determined the quaternary structure of 10 different rhomboid proteins (the largest superfamily of intramembrane proteases) and six unrelated control proteins in parallel detergent micelle, planar supported lipid bilayer, and whole-cell systems. Bacterial, parasitic, insect, and human rhomboid proteases and inactive rhomboid pseudoproteases all proved to be monomeric in all membrane conditions but dimeric in detergent micelles. These analyses establish that rhomboid proteins are, as a strict family rule, structurally and functionally monomeric by nature and that rhomboid dimers are unphysiological.
MeSH term(s)	Membrane Proteins/chemistry ; Micelles ; Models, Molecular ; Photobleaching ; Protein Multimerization ; Protein Structure, Quaternary
Chemical Substances	Membrane Proteins ; Micelles
Language	English
Publishing date	2018-10-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2018.09.024
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 235: 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.MO 2: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Hollow Octadecameric Self-Assembly of Collagen-like Peptides.

Yu, Le Tracy / Hancu, Maria C / Kreutzberger, Mark A B / Henrickson, Amy / Demeler, Borries / Egelman, Edward H / Hartgerink, Jeffrey D

Journal of the American Chemical Society

2023 Volume 145, Issue 9, Page(s) 5285–5296

Abstract: The folding of collagen is a hierarchical process that starts with three peptides associating into the characteristic triple helical fold. Depending on the specific collagen in question, these triple helices then assemble into bundles reminiscent of α- ... ...

Abstract	The folding of collagen is a hierarchical process that starts with three peptides associating into the characteristic triple helical fold. Depending on the specific collagen in question, these triple helices then assemble into bundles reminiscent of α-helical coiled-coils. Unlike α-helices, however, the bundling of collagen triple helices is very poorly understood with almost no direct experimental data available. In order to shed light on this critical step of collagen hierarchical assembly, we have examined the collagenous region of complement component 1q. Thirteen synthetic peptides were prepared to dissect the critical regions allowing for its octadecameric self-assembly. We find that short peptides (under 40 amino acids) are able to self-assemble into specific (ABC)
MeSH term(s)	Amino Acid Sequence ; Cryoelectron Microscopy ; Peptides/chemistry ; Collagen/chemistry ; Protein Conformation, alpha-Helical
Chemical Substances	Peptides ; Collagen (9007-34-5)
Language	English
Publishing date	2023-02-22
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	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.2c12931
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: Structure-based design of a SARS-CoV-2 Omicron-specific inhibitor.

Yang, Kailu / Wang, Chuchu / Kreutzberger, Alex J B / White, K Ian / Pfuetzner, Richard A / Esquivies, Luis / Kirchhausen, Tomas / Brunger, Axel T

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

2023 Volume 120, Issue 13, Page(s) e2300360120

Abstract: The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) introduced a relatively large number of mutations, including three mutations in the highly conserved heptad repeat 1 (HR1) region of the spike glycoprotein (S) critical ... ...

Abstract	The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) introduced a relatively large number of mutations, including three mutations in the highly conserved heptad repeat 1 (HR1) region of the spike glycoprotein (S) critical for its membrane fusion activity. We show that one of these mutations, N969K induces a substantial displacement in the structure of the heptad repeat 2 (HR2) backbone in the HR1HR2 postfusion bundle. Due to this mutation, fusion-entry peptide inhibitors based on the Wuhan strain sequence are less efficacious. Here, we report an Omicron-specific peptide inhibitor designed based on the structure of the Omicron HR1HR2 postfusion bundle. Specifically, we inserted an additional residue in HR2 near the Omicron HR1 K969 residue to better accommodate the N969K mutation and relieve the distortion in the structure of the HR1HR2 postfusion bundle it introduced. The designed inhibitor recovers the loss of inhibition activity of the original longHR2_42 peptide with the Wuhan strain sequence against the Omicron variant in both a cell-cell fusion assay and a vesicular stomatitis virus (VSV)-SARS-CoV-2 chimera infection assay, suggesting that a similar approach could be used to combat future variants. From a mechanistic perspective, our work suggests the interactions in the extended region of HR2 may mediate the initial landing of HR2 onto HR1 during the transition of the S protein from the prehairpin intermediate to the postfusion state.
MeSH term(s)	Humans ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; Viral Envelope Proteins/genetics ; Amino Acid Sequence ; COVID-19 ; Protein Structure, Secondary ; Spike Glycoprotein, Coronavirus/metabolism ; Peptides/genetics ; Peptides/pharmacology ; Peptides/chemistry ; Anti-Retroviral Agents
Chemical Substances	Viral Envelope Proteins ; Spike Glycoprotein, Coronavirus ; Peptides ; Anti-Retroviral Agents ; spike protein, SARS-CoV-2
Language	English
Publishing date	2023-03-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2300360120
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

Article ; Online: An extensive disulfide bond network prevents tail contraction in Agrobacterium tumefaciens phage Milano.

Sonani, Ravi R / Palmer, Lee K / Esteves, Nathaniel C / Horton, Abigail A / Sebastian, Amanda L / Kelly, Rebecca J / Wang, Fengbin / Kreutzberger, Mark A B / Russell, William K / Leiman, Petr G / Scharf, Birgit E / Egelman, Edward H

Nature communications

2024 Volume 15, Issue 1, Page(s) 756

Abstract: A contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, contraction of an external sheath powers the motion of an ...

Abstract	A contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, contraction of an external sheath powers the motion of an inner tube through the membrane. The structure, energetics, and mechanism of the machinery imply rigidity and straightness. The contractile tail of Agrobacterium tumefaciens bacteriophage Milano is flexible and bent to varying degrees, which sets it apart from other contractile tail-like systems. Here, we report structures of the Milano tail including the sheath-tube complex, baseplate, and putative receptor-binding proteins. The flexible-to-rigid transformation of the Milano tail upon contraction can be explained by unique electrostatic properties of the tail tube and sheath. All components of the Milano tail, including sheath subunits, are crosslinked by disulfides, some of which must be reduced for contraction to occur. The putative receptor-binding complex of Milano contains a tailspike, a tail fiber, and at least two small proteins that form a garland around the distal ends of the tailspikes and tail fibers. Despite being flagellotropic, Milano lacks thread-like tail filaments that can wrap around the flagellum, and is thus likely to employ a different binding mechanism.
MeSH term(s)	Bacteriophages/genetics ; Agrobacterium tumefaciens/genetics ; Type VI Secretion Systems/metabolism ; Cell Membrane/metabolism
Chemical Substances	Type VI Secretion Systems
Language	English
Publishing date	2024-01-26
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/s41467-024-44959-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Drunken lipid membranes, not drunken SNARE proteins, promote fusion in a model of neurotransmitter release.

Coffman, Robert E / Kraichely, Katelyn N / Kreutzberger, Alex J B / Kiessling, Volker / Tamm, Lukas K / Woodbury, Dixon J

Frontiers in molecular neuroscience

2022 Volume 15, Page(s) 1022756

Abstract: Alcohol affects many neuronal proteins that are upstream or down-stream of synaptic vesicle fusion and neurotransmitter release. Less well studied is alcohol's effect on the fusion machinery including SNARE proteins and lipid membranes. Using a SNARE- ... ...

Abstract	Alcohol affects many neuronal proteins that are upstream or down-stream of synaptic vesicle fusion and neurotransmitter release. Less well studied is alcohol's effect on the fusion machinery including SNARE proteins and lipid membranes. Using a SNARE-driven fusion assay we show that fusion probability is significantly increased at 0.4% v/v (68 mM) ethanol; but not with methanol up to 10%. Ethanol appears to act directly on membrane lipids since experiments focused on protein properties [circular dichroism spectrometry, site-directed fluorescence interference contrast (sdFLIC) microscopy, and vesicle docking results] showed no significant changes up to 5% ethanol, but a protein-free fusion assay also showed increased lipid membrane fusion rates with 0.4% ethanol. These data show that the effects of high physiological doses of ethanol on SNARE-driven fusion are mediated through ethanol's interaction with the lipid bilayer of membranes and not SNARE proteins, and that methanol affects lipid membranes and SNARE proteins only at high doses.
Language	English
Publishing date	2022-10-14
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2452967-9
ISSN	1662-5099
ISSN	1662-5099
DOI	10.3389/fnmol.2022.1022756
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids.

Kreutzberger, Mark A B / Wang, Shengyuan / Beltran, Leticia C / Tuachi, Abraham / Zuo, Xiaobing / Egelman, Edward H / Conticello, Vincent P

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

2022 Volume 119, Issue 20, Page(s) e2121586119

Abstract: Phenol-soluble modulins (PSMs) are peptide-based virulence factors that play significant roles in the pathogenesis of staphylococcal strains in community-associated and hospital-associated infections. In addition to cytotoxicity, PSMs display the ... ...

Abstract	Phenol-soluble modulins (PSMs) are peptide-based virulence factors that play significant roles in the pathogenesis of staphylococcal strains in community-associated and hospital-associated infections. In addition to cytotoxicity, PSMs display the propensity to self-assemble into fibrillar species, which may be mediated through the formation of amphipathic conformations. Here, we analyze the self-assembly behavior of two PSMs, PSMα3 and PSMβ2, which are derived from peptides expressed by methicillin-resistant Staphylococcus aureus (MRSA), a significant human pathogen. In both cases, we observed the formation of a mixture of self-assembled species including twisted filaments, helical ribbons, and nanotubes, which can reversibly interconvert in vitro. Cryo–electron microscopy structural analysis of three PSM nanotubes, two derived from PSMα3 and one from PSMβ2, revealed that the assemblies displayed remarkably similar structures based on lateral association of cross-α amyloid protofilaments. The amphipathic helical conformations of PSMα3 and PSMβ2 enforced a bilayer arrangement within the protofilaments that defined the structures of the respective PSMα3 and PSMβ2 nanotubes. We demonstrate that, similar to amyloids based on cross-β protofilaments, cross-α amyloids derived from these PSMs display polymorphism, not only in terms of the global morphology (e.g., twisted filament, helical ribbon, and nanotube) but also with respect to the number of protofilaments within a given peptide assembly. These results suggest that the folding landscape of PSM derivatives may be more complex than originally anticipated and that the assemblies are able to sample a wide range of supramolecular structural space.
MeSH term(s)	Amyloid/chemistry ; Bacterial Toxins ; Cryoelectron Microscopy ; Humans ; Nanotubes ; Peptides/chemistry ; Staphylococcus aureus/metabolism
Chemical Substances	Amyloid ; Bacterial Toxins ; Peptides ; staphylococcal delta toxin
Language	English
Publishing date	2022-05-09
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.2121586119
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

Article ; Online: Complexin-1 and synaptotagmin-1 compete for binding sites on membranes containing PtdInsP

Liang, Qian / Ofosuhene, Akosua P / Kiessling, Volker / Liang, Binyong / Kreutzberger, Alex J B / Tamm, Lukas K / Cafiso, David S

Biophysical journal

2022 Volume 121, Issue 18, Page(s) 3370–3380

Abstract: Complexin-1 is an essential protein for neuronal exocytosis that acts to depress spontaneous fusion events while enhancing evoked neurotransmitter release. In addition to binding soluble N-ethylmaleimide-sensitive factor attachment protein receptors, it ... ...

Abstract	Complexin-1 is an essential protein for neuronal exocytosis that acts to depress spontaneous fusion events while enhancing evoked neurotransmitter release. In addition to binding soluble N-ethylmaleimide-sensitive factor attachment protein receptors, it is well established that complexin associates with membranes in a manner that depends upon membrane curvature. In the present work, we examine the membrane binding of complexin using electron paramagnetic resonance spectroscopy, fluorescence anisotropy, and total internal reflection fluorescence microscopy. The apparent membrane affinity of complexin is found to strongly depend upon the concentration of protein used in the binding assay, and this is a result of a limited number of binding sites for complexin on the membrane interface. Although both the N- and C-terminal regions of complexin associate with the membrane interface, membrane affinity is driven by its C-terminus. Complexin prefers to bind liquid-disordered membrane phases and shows an enhanced affinity toward membranes containing phosphatidylinositol 4-5-bisphosphate (PI(4,5)P
MeSH term(s)	Adaptor Proteins, Vesicular Transport/chemistry ; Binding Sites ; Calcium/metabolism ; Exocytosis ; Nerve Tissue Proteins/chemistry ; Neurotransmitter Agents ; Phosphatidylinositol 4,5-Diphosphate ; SNARE Proteins/metabolism ; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins/metabolism ; Synaptotagmin I/chemistry
Chemical Substances	Adaptor Proteins, Vesicular Transport ; Nerve Tissue Proteins ; Neurotransmitter Agents ; Phosphatidylinositol 4,5-Diphosphate ; SNARE Proteins ; Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins ; Synaptotagmin I ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2022-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	218078-9
ISSN	1542-0086 ; 0006-3495
ISSN (online)	1542-0086
ISSN	0006-3495
DOI	10.1016/j.bpj.2022.08.023
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 235: 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.MO 2: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Two dramatically distinct archaeal type IV pili structures formed by the same pilin.

Liu, Junfeng / Eastep, Gunnar N / Cvirkaite-Krupovic, Virginija / Rich-New, Shane T / Kreutzberger, Mark A B / Egelman, Edward H / Krupovic, Mart / Wang, Fengbin

bioRxiv : the preprint server for biology

2023

Abstract: Type IV pili (T4P) represent one of the most common varieties of surface appendages in archaea. These filaments, assembled from relatively small pilin proteins, can be many microns long and serve diverse functions, including adhesion, biofilm formation, ... ...

Abstract	Type IV pili (T4P) represent one of the most common varieties of surface appendages in archaea. These filaments, assembled from relatively small pilin proteins, can be many microns long and serve diverse functions, including adhesion, biofilm formation, motility, and intercellular communication. Using cryo-electron microscopy (cryo-EM), we determined atomic structures of two dramatically different T4P from
Language	English
Publishing date	2023-08-07
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.08.07.552285
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: Membrane lipids couple synaptotagmin to SNARE-mediated granule fusion in insulin-secreting cells.

Amos, Chase / Kiessling, Volker / Kreutzberger, Alex J B / Schenk, Noah A / Mohan, Ramkumar / Nyenhuis, Sarah / Doyle, Catherine A / Wang, Hong-Yin / Levental, Kandice / Levental, Ilya / Anantharam, Arun / Tamm, Lukas K

Molecular biology of the cell

2023 Volume 35, Issue 3, Page(s) ar12

Abstract: Insulin secretion depends on the ... ...

Abstract	Insulin secretion depends on the Ca
MeSH term(s)	Membrane Fusion ; Membrane Lipids/metabolism ; SNARE Proteins/metabolism ; Insulin-Secreting Cells/metabolism ; Cell Membrane/metabolism ; Synaptotagmin I/chemistry ; Synaptotagmin I/metabolism ; Exocytosis ; Recombinant Proteins/metabolism ; Calcium/metabolism
Chemical Substances	Membrane Lipids ; SNARE Proteins ; Synaptotagmin I ; Recombinant Proteins ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2023-12-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	1098979-1
ISSN	1939-4586 ; 1059-1524
ISSN (online)	1939-4586
ISSN	1059-1524
DOI	10.1091/mbc.E23-06-0225
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2853: 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)
Zs.MO 410: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

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 Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

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

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito