LIVIVO - Search results -

Search results

Result 1 - 10 of total 25

Search options

Article: Electron count and ligand composition influence the optical and chiroptical signatures of far-red and NIR-emissive DNA-stabilized silver nanoclusters.

Guha, Rweetuparna / Gonzàlez-Rosell, Anna / Rafik, Malak / Arevalos, Nery / Katz, Benjamin B / Copp, Stacy M

2023 Volume 14, Issue 41, Page(s) 11340–11350

Abstract: Near-infrared (NIR) emissive DNA-stabilized silver nanoclusters ( ... ...

Abstract	Near-infrared (NIR) emissive DNA-stabilized silver nanoclusters (Ag
Language	English
Publishing date	2023-09-11
Publishing country	England
Document type	Journal Article
ZDB-ID	2559110-1
ISSN	2041-6539 ; 2041-6520
ISSN (online)	2041-6539
ISSN	2041-6520
DOI	10.1039/d3sc02931j
Database	MEDical Literature Analysis and Retrieval System OnLINE

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.

Article ; Online: Formation and Nanomechanical Properties of Silver-Mediated Guanine DNA Duplexes in Aqueous Solution.

Bethur, Eshana / Guha, Rweetuparna / Zhao, Ziqian / Katz, Benjamin B / Ashby, Paul D / Zeng, Hongbo / Copp, Stacy M

ACS nano

2024 Volume 18, Issue 4, Page(s) 3002–3010

Abstract: Silver cations can mediate base pairing of guanine (G) DNA oligomers, yielding linear parallel G- ... ...

Abstract	Silver cations can mediate base pairing of guanine (G) DNA oligomers, yielding linear parallel G-Ag
MeSH term(s)	Guanine/chemistry ; Silver/chemistry ; DNA/chemistry ; Base Pairing ; Temperature ; Nucleic Acid Conformation
Chemical Substances	Guanine (5Z93L87A1R) ; Silver (3M4G523W1G) ; DNA (9007-49-2)
Language	English
Publishing date	2024-01-16
Publishing country	United States
Document type	Journal Article
ISSN	1936-086X
ISSN (online)	1936-086X
DOI	10.1021/acsnano.3c08008
Database	MEDical Literature Analysis and Retrieval System OnLINE

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.

Article ; Online: Synthesis of site-specific Fab-drug conjugates using ADP-ribosyl cyclases.

Kim, Hyo Sun / Hariri, Kimia / Zhang, Xiao-Nan / Chen, Liang-Chieh / Katz, Benjamin B / Pei, Hua / Louie, Stan G / Zhang, Yong

Protein science : a publication of the Protein Society

2023 Volume 33, Issue 4, Page(s) e4924

Abstract: Targeted delivery of small-molecule drugs via covalent attachments to monoclonal antibodies has proved successful in clinic. For this purpose, full-length antibodies are mainly used as drug-carrying vehicles. Despite their flexible conjugation sites and ... ...

Abstract	Targeted delivery of small-molecule drugs via covalent attachments to monoclonal antibodies has proved successful in clinic. For this purpose, full-length antibodies are mainly used as drug-carrying vehicles. Despite their flexible conjugation sites and versatile biological activities, intact immunoglobulins with conjugated drugs, which feature relatively large molecular weights, tend to have restricted tissue distribution and penetration and low fractions of payloads. Linking small-molecule therapeutics to other formats of antibody may lead to conjugates with optimal properties. Here, we designed and synthesized ADP-ribosyl cyclase-enabled fragment antigen-binding (Fab) drug conjugates (ARC-FDCs) by utilizing CD38 catalytic activity. Through rapidly forming a stable covalent bond with a nicotinamide adenine dinucleotide (NAD
MeSH term(s)	ADP-ribosyl Cyclase ; ADP-ribosyl Cyclase 1 ; Antigens, CD/chemistry ; NAD+ Nucleosidase/chemistry ; Pharmaceutical Preparations ; NAD/chemistry
Chemical Substances	ADP-ribosyl Cyclase (EC 3.2.2.5) ; ADP-ribosyl Cyclase 1 (EC 3.2.2.6) ; Antigens, CD ; NAD+ Nucleosidase (EC 3.2.2.5) ; Pharmaceutical Preparations ; NAD (0U46U6E8UK)
Language	English
Publishing date	2023-12-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4924
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3407: 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 1: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: DNA Stabilizes Eight-Electron Superatom Silver Nanoclusters with Broadband Downconversion and Microsecond-Lived Luminescence.

Gonzàlez-Rosell, Anna / Guha, Rweetuparna / Cerretani, Cecilia / Rück, Vanessa / Liisberg, Mikkel B / Katz, Benjamin B / Vosch, Tom / Copp, Stacy M

The journal of physical chemistry letters

2022 Volume 13, Issue 35, Page(s) 8305–8311

Abstract: DNA oligomers are known to serve as stabilizing ligands for silver nanoclusters ( ... ...

Abstract	DNA oligomers are known to serve as stabilizing ligands for silver nanoclusters (Ag
MeSH term(s)	DNA/chemistry ; Electrons ; Fluorescence ; Luminescence ; Silver/chemistry
Chemical Substances	Silver (3M4G523W1G) ; DNA (9007-49-2)
Language	English
Publishing date	2022-08-29
Publishing country	United States
Document type	Journal Article
ISSN	1948-7185
ISSN (online)	1948-7185
DOI	10.1021/acs.jpclett.2c02207
Database	MEDical Literature Analysis and Retrieval System OnLINE

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.

Article: A Disulfide-Stabilized Aβ that Forms Dimers but Does Not Form Fibrils

Zhang, Sheng / Yoo, Stan / Snyder, Dalton T. / Katz, Benjamin B. / Henrickson, Amy / Demeler, Borries / Wysocki, Vicki H. / Kreutzer, Adam G. / Nowick, James S.

Biochemistry. 2022 Jan. 26, v. 61, no. 4

2022

Abstract: Aβ dimers are a basic building block of many larger Aβ oligomers and are among the most neurotoxic and pathologically relevant species in Alzheimer’s disease. Homogeneous Aβ dimers are difficult to prepare, characterize, and study because Aβ forms ... ...

Abstract	Aβ dimers are a basic building block of many larger Aβ oligomers and are among the most neurotoxic and pathologically relevant species in Alzheimer’s disease. Homogeneous Aβ dimers are difficult to prepare, characterize, and study because Aβ forms heterogeneous mixtures of oligomers that vary in size and can rapidly aggregate into more stable fibrils. This paper introduces AβC₁₈C₃₃ as a disulfide-stabilized analogue of Aβ₄₂ that forms stable homogeneous dimers in lipid environments but does not aggregate to form insoluble fibrils. The AβC₁₈C₃₃ peptide is readily expressed in Escherichia coli and purified by reverse-phase HPLC to give ca. 8 mg of pure peptide per liter of bacterial culture. SDS-PAGE establishes that AβC₁₈C₃₃ forms homogeneous dimers in the membrane-like environment of SDS and that conformational stabilization of the peptide with a disulfide bond prevents the formation of heterogeneous mixtures of oligomers. Mass spectrometric (MS) studies in the presence of dodecyl maltoside (DDM) further confirm the formation of stable noncovalent dimers. Circular dichroism (CD) spectroscopy establishes that AβC₁₈C₃₃ adopts a β-sheet conformation in detergent solutions and supports a model in which the intramolecular disulfide bond induces β-hairpin folding and dimer formation in lipid environments. Thioflavin T (ThT) fluorescence assays and transmission electron microscopy (TEM) studies indicate that AβC₁₈C₃₃ does not undergo fibril formation in aqueous buffer solutions and demonstrate that the intramolecular disulfide bond prevents fibril formation. The recently published NMR structure of an Aβ₄₂ tetramer (PDB: 6RHY) provides a working model for the AβC₁₈C₃₃ dimer, in which two β-hairpins assemble through hydrogen bonding to form a four-stranded antiparallel β-sheet. It is anticipated that AβC₁₈C₃₃ will serve as a stable, nonfibrilizing, and noncovalent Aβ dimer model for amyloid and Alzheimer’s disease research.
Keywords	Escherichia coli ; amyloid ; bacterial culture ; circular dichroism spectroscopy ; detergents ; disulfide bonds ; fluorescence ; hydrogen ; lipids ; mass spectrometry ; models ; neurotoxicity ; peptides ; polyacrylamide gel electrophoresis ; reversed-phase high performance liquid chromatography ; transmission electron microscopy
Language	English
Dates of publication	2022-0126
Size	p. 252-264.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.1c00739
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Cologne/Königswinter

Zs.A 217: 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: Spatially resolved detection of small molecules from press-dried plant tissue using MALDI imaging.

Long, Zane G / Le, Jonathan V / Katz, Benjamin B / Lopez, Belen G / Tenenbaum, Emily D / Semmling, Bonnie / Schmidt, Ryan J / Grün, Felix / Butts, Carter T / Martin, Rachel W

Applications in plant sciences

2023 Volume 11, Issue 5, Page(s) e11539

Abstract: Premise: Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) is a chemical imaging method that can visualize spatial distributions of particular molecules. Plant tissue imaging has so far mostly used cryosectioning, which ... ...

Abstract	Premise: Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI-MSI) is a chemical imaging method that can visualize spatial distributions of particular molecules. Plant tissue imaging has so far mostly used cryosectioning, which can be impractical for the preparation of large-area imaging samples, such as full flower petals. Imaging unsectioned plant tissue presents its own difficulties in extracting metabolites to the surface due to the waxy cuticle. Methods: We address this by using established delipidation techniques combined with a solvent vapor extraction prior to applying the matrix with many low-concentration sprays. Results: Using this procedure, we imaged tissue from three different plant species (two flowers and one carnivorous plant leaf). Material factorization analysis of the resulting data reveals a wide range of plant-specific small molecules with varying degrees of localization to specific portions of the tissue samples, while facilitating detection and removal of signal from background sources. Conclusions: This work demonstrates applicability of MALDI-MSI to press-dried plant samples without freezing or cryosectioning, setting the stage for spatially resolved molecule identification. Increased mass resolution and inclusion of tandem mass spectrometry are necessary next steps to allow more specific and reliable compound identification.
Language	English
Publishing date	2023-09-11
Publishing country	United States
Document type	Journal Article
ZDB-ID	2699923-7
ISSN	2168-0450
ISSN	2168-0450
DOI	10.1002/aps3.11539
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Chloride Ligands on DNA-Stabilized Silver Nanoclusters.

Gonzàlez-Rosell, Anna / Malola, Sami / Guha, Rweetuparna / Arevalos, Nery R / Matus, María Francisca / Goulet, Meghen E / Haapaniemi, Esa / Katz, Benjamin B / Vosch, Tom / Kondo, Jiro / Häkkinen, Hannu / Copp, Stacy M

Journal of the American Chemical Society

2023 Volume 145, Issue 19, Page(s) 10721–10729

Abstract: DNA-stabilized silver nanoclusters ( ... ...

Abstract	DNA-stabilized silver nanoclusters (Ag
MeSH term(s)	Chlorides/chemistry ; Silver/chemistry ; Ligands ; Crystallography, X-Ray ; DNA/chemistry
Chemical Substances	Chlorides ; Silver (3M4G523W1G) ; Ligands ; DNA (9007-49-2)
Language	English
Publishing date	2023-05-08
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, Non-U.S. Gov't
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.3c01366
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: A Disulfide-Stabilized Aβ that Forms Dimers but Does Not Form Fibrils.

Zhang, Sheng / Yoo, Stan / Snyder, Dalton T / Katz, Benjamin B / Henrickson, Amy / Demeler, Borries / Wysocki, Vicki H / Kreutzer, Adam G / Nowick, James S

Biochemistry

2022 Volume 61, Issue 4, Page(s) 252–264

Abstract: Aβ dimers are a basic building block of many larger Aβ oligomers and are among the most neurotoxic and pathologically relevant species in Alzheimer's disease. Homogeneous Aβ dimers are difficult to prepare, characterize, and study because Aβ forms ... ...

Abstract	Aβ dimers are a basic building block of many larger Aβ oligomers and are among the most neurotoxic and pathologically relevant species in Alzheimer's disease. Homogeneous Aβ dimers are difficult to prepare, characterize, and study because Aβ forms heterogeneous mixtures of oligomers that vary in size and can rapidly aggregate into more stable fibrils. This paper introduces Aβ
MeSH term(s)	Alzheimer Disease/metabolism ; Amyloid/chemistry ; Amyloid/metabolism ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Circular Dichroism/methods ; Disulfides/chemistry ; Disulfides/metabolism ; Humans ; Hydrogen Bonding ; Microscopy, Electron, Transmission/methods ; Models, Molecular ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Protein Conformation ; Protein Conformation, beta-Strand
Chemical Substances	Amyloid ; Amyloid beta-Peptides ; Disulfides ; Peptide Fragments ; amyloid beta-protein (40-42)
Language	English
Publishing date	2022-01-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.1c00739
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 217: 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: KCNQ5 activation is a unifying molecular mechanism shared by genetically and culturally diverse botanical hypotensive folk medicines.

Manville, Rían W / van der Horst, Jennifer / Redford, Kaitlyn E / Katz, Benjamin B / Jepps, Thomas A / Abbott, Geoffrey W

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

2019 Volume 116, Issue 42, Page(s) 21236–21245

Abstract: Botanical folk medicines have been used throughout human history to treat common disorders such as hypertension, often with unknown underlying mechanisms. Here, we discovered that hypotensive folk medicines from a genetically diverse range of plant ... ...

Abstract	Botanical folk medicines have been used throughout human history to treat common disorders such as hypertension, often with unknown underlying mechanisms. Here, we discovered that hypotensive folk medicines from a genetically diverse range of plant species each selectively activated the vascular-expressed KCNQ5 potassium channel, a feature lacking in the modern synthetic pharmacopeia, whereas nonhypotensive plant extracts did not. Analyzing constituents of the hypotensive
MeSH term(s)	Animals ; KCNQ Potassium Channels/metabolism ; Male ; Medicine, Traditional/methods ; Plant Roots/chemistry ; Rats ; Rats, Wistar
Chemical Substances	KCNQ Potassium Channels ; Kcnq5 protein, rat
Language	English
Publishing date	2019-09-30
Publishing country	United States
Document type	Journal Article ; 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.1907511116
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: The structural basis for inhibition of the classical and lectin complement pathways by S. aureus extracellular adherence protein.

Woehl, Jordan L / Ramyar, Kasra X / Katz, Benjamin B / Walker, John K / Geisbrecht, Brian V

Protein science : a publication of the Protein Society

2017 Volume 26, Issue 8, Page(s) 1595–1608

Abstract: The extracellular adherence protein (Eap) plays a crucial role in pathogenesis and survival of Staphylococcus aureus by inhibiting the classical and lectin pathways of complement. We have previously shown that Eap binds with nanomolar affinity to ... ...

Abstract	The extracellular adherence protein (Eap) plays a crucial role in pathogenesis and survival of Staphylococcus aureus by inhibiting the classical and lectin pathways of complement. We have previously shown that Eap binds with nanomolar affinity to complement C4b and disrupts the initial interaction between C4b and C2, thereby inhibiting formation of the classical and lectin pathway C3 pro-convertase. Although an underlying mechanism has been identified, the structural basis for Eap binding to C4b is poorly understood. Here, we show that Eap domains 3 and 4 each contain a low-affinity, but saturable binding site for C4b. Taking advantage of the high lysine content of Eap, we used a zero-length crosslinking approach to map the Eap binding site to both the α'- and γ-chains of C4b. We also probed the C4b/Eap interface through a chemical footprinting approach involving lysine modification, proteolytic digestion, and mass spectrometry. This identified seven lysines in Eap that undergo changes in solvent exposure upon C4b binding. We found that simultaneous mutation of these lysines to either alanine or glutamate diminished C4b binding and complement inhibition by Eap. Together, our results provide insight into Eap recognition of C4b, and suggest that the repeating domains that comprise Eap are capable of multiple ligand-binding modes.
MeSH term(s)	Alanine/chemistry ; Alanine/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; Carbodiimides/chemistry ; Complement C4b/chemistry ; Complement C4b/genetics ; Complement C4b/metabolism ; Complement Pathway, Classical ; Complement Pathway, Mannose-Binding Lectin ; Cross-Linking Reagents/chemistry ; Crystallography, X-Ray ; Gene Expression ; Glutamic Acid/chemistry ; Glutamic Acid/metabolism ; Host-Pathogen Interactions ; Humans ; Lysine/chemistry ; Lysine/metabolism ; Models, Molecular ; Mutation ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Structure, Secondary ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Staphylococcus aureus/chemistry
Chemical Substances	1-ethyl-3-(3-(diethylamino)propyl)carbodiimide ; Bacterial Proteins ; Carbodiimides ; Cross-Linking Reagents ; Eap-N protein, Staphylococcus aureus ; RNA-Binding Proteins ; Recombinant Proteins ; Glutamic Acid (3KX376GY7L) ; Complement C4b (80295-50-7) ; Lysine (K3Z4F929H6) ; Alanine (OF5P57N2ZX)
Language	English
Publishing date	2017-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.3195
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 3407: 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 1: Show issues

Order via subito

Details ▾

To top

More links

Kategorien

Order via subito

More links

Kategorien

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

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

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

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