LIVIVO - Search results -

Search results

Result 1 - 10 of total 171

Search options

Article ; Online: A transplant recipient's pandemic perspective.

Frick, David N

Transplant infectious disease : an official journal of the Transplantation Society

2021 Volume 23, Issue 5, Page(s) e13738

MeSH term(s)	COVID-19 ; Humans ; Pandemics ; Transplant Recipients ; Transplants
Language	English
Publishing date	2021-10-06
Publishing country	Denmark
Document type	Letter ; Comment
ZDB-ID	1476094-0
ISSN	1399-3062 ; 1398-2273
ISSN (online)	1399-3062
ISSN	1398-2273
DOI	10.1111/tid.13738
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5100: 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 ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Fluorescent probe displacement assays reveal unique nucleic acid binding properties of human nudix enzymes.

Ray, Atreyei / Frick, David N

Analytical biochemistry

2020 Volume 595, Page(s) 113622

Abstract: Nudix proteins are members of a large family of homologous enzymes that hydrolyze nucleoside diphosphates linked to other compounds. The substrates for a subset of Nudix enzymes are all nucleotides linked to RNA, like the ... ...

Abstract	Nudix proteins are members of a large family of homologous enzymes that hydrolyze nucleoside diphosphates linked to other compounds. The substrates for a subset of Nudix enzymes are all nucleotides linked to RNA, like the m
MeSH term(s)	Binding Sites ; DNA/chemistry ; DNA Repair Enzymes/analysis ; Escherichia coli/enzymology ; Fluorescent Dyes/chemistry ; Humans ; Phosphoric Monoester Hydrolases/analysis ; Pyrophosphatases/analysis ; RNA/chemistry ; Recombinant Proteins/analysis ; Nudix Hydrolases
Chemical Substances	Fluorescent Dyes ; Recombinant Proteins ; RNA (63231-63-0) ; DNA (9007-49-2) ; Phosphoric Monoester Hydrolases (EC 3.1.3.2) ; NUDT12 protein, human (EC 3.6.1.-) ; Pyrophosphatases (EC 3.6.1.-) ; NUDT2 protein, human (EC 3.6.1.17) ; 8-oxodGTPase (EC 3.6.1.55) ; DNA Repair Enzymes (EC 6.5.1.-)
Language	English
Publishing date	2020-02-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2020.113622
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 389: 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: Fluorescent probe displacement assays reveal unique nucleic acid binding properties of human nudix enzymes

Ray, Atreyei / Frick, David N

Analytical biochemistry. 2020 Apr. 15, v. 595

2020

Abstract	Nudix proteins are members of a large family of homologous enzymes that hydrolyze nucleoside diphosphates linked to other compounds. The substrates for a subset of Nudix enzymes are all nucleotides linked to RNA, like the m7G mRNA caps and the more recently discovered NAD(H) RNA caps. However, the RNA affinity and nucleic acid specificity of Nudix proteins has not yet been explored in depth. In this study we designed new fluorescence-based assays to examine the interaction of purified recombinant E. coli NudC and human Nudt1 (aka MTH1) Nudt3, Nudt12, Nudt16, and Nudt20 (aka Dcp2). All Nudix proteins except Nudt1 and Nudt12 bound both RNA and DNA stoichiometrically with high affinity (dissociation constants in the nanomolar range) and no clear sequence specificity. In stark contrast, Nudt12 binds RNA but not similar DNA oligonucleotides. Nudt12 also bound RNAs with 5’ NAD+ caps more tightly than those with NADH or m7G cap. NudC was similarly selective against m7G caps but did not differentiate between NAD+ and NADH capped RNA. Nudt3, Nudt16, and Nudt20 bound m7G capped RNA more tightly than RNA with NADH caps.
Keywords	DNA ; Escherichia coli ; NAD (coenzyme) ; binding properties ; dissociation ; enzymes ; fluorescent dyes ; humans ; messenger RNA ; nucleosides ; oligonucleotides ; proteins
Language	English
Dates of publication	2020-0415
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2020.113622
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 70/124: 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: The BALB/c Mouse Model for the Evaluation of Therapies to Treat Infections with Aerosolized

Nelson, Michelle / Barnes, Kay B / Davies, Carwyn H / Cote, Christopher K / Meinig, J Matthew / Biryukov, Sergei S / Dyer, David N / Frick, Ondraya / Heine, Henry / Pfefferle, Denise A / Horstman-Smith, Amanda / Barbaras, Julie / Harding, Sarah V

Antibiotics (Basel, Switzerland)

2023 Volume 12, Issue 3

Abstract: Burkholderia ... ...

Abstract	Burkholderia pseudomallei
Language	English
Publishing date	2023-03-03
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2681345-2
ISSN	2079-6382
ISSN	2079-6382
DOI	10.3390/antibiotics12030506
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Entrustable professional activities for residency in general internal medicine: a systematic review.

Valding, Bastien / Monti, Matteo / Junod Perron, Noëlle / Frick, Sonia / Jaques, Cécile / Nendaz, Mathieu / Gachoud, David

Swiss medical weekly

2022 Volume 152, Page(s) 40002

Abstract: ... population (n = 103 EPAs); (2) care and management of patients with specific needs (n = 67); (3) care ... coordination and communication (n = 52); (4) management and leadership (N = 21); (5) healthcare quality ... education, and research (n = 41); and (6) miscellaneous (n = 24). The remaining 87 EPAs were disease ...

Abstract	Context: Entrustable Professional Activities (EPAs) are observable tasks that are regular parts of a physician's daily clinical work. Before being permitted to accomplish these tasks independently, trainees must gain their supervisors' trust. Defining the list of EPAs that should be mastered by the end of a residency is critical to setting clear expectations about autonomous practice. Objective: To collect all the lists of EPAs defined for residencies in general internal medicine and synthesise them into a reference work useful for developing new lists of EPAs or improving existing ones. Method: This systematic review searched five databases and relevant grey literature using keywords related to EPAs and postgraduate education, from 2005, when the first article on EPAs was published, to April 2022. Inclusion criteria were the availability of an EPAs list and a focus on general internal medicine. Two reviewers independently selected the studies, extracted data and performed a quality assessment using QATSDD and AACODS tools. Mean values and inter-rater reliability were calculated. Results: The review yielded 3292 records, with 16 articles meeting the inclusion criteria, mostly from North America. Synthesising their 16 lists generated 395 EPAs. The reviewers then inductively categoried those EPAs, 308 of which fell into 6 domains, 14 themes and 24 subthemes. The domains were: (1) care and management of the general adult population (n = 103 EPAs); (2) care and management of patients with specific needs (n = 67); (3) care coordination and communication (n = 52); (4) management and leadership (N = 21); (5) healthcare quality, education, and research (n = 41); and (6) miscellaneous (n = 24). The remaining 87 EPAs were disease-specific and did not fit into this categorisation. Conclusions: Categorising EPAs created a unique synthesis of the existing lists of EPAs for educating residents in general internal medicine. This synthesis could be used as a reference for anyone tasked with developing new lists of EPAs or improving existing ones.
MeSH term(s)	Humans ; Reproducibility of Results ; Internship and Residency ; Internal Medicine
Language	English
Publishing date	2022-11-04
Publishing country	Switzerland
Document type	Systematic Review ; Journal Article
ZDB-ID	2036179-8
ISSN	1424-3997 ; 1424-7860
ISSN (online)	1424-3997
ISSN	1424-7860
DOI	10.57187/smw.2022.40002
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ua VI Zs.152: 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: The influence of anterior cingulate GABA+ and glutamate on emotion regulation and reactivity in adolescents and adults.

Widegren, Ebba / Frick, Matilda A / Hoppe, Johanna Motilla / Weis, Jan / Möller, Stefan / Fällmar, David / Mårtensson, Johanna / Brocki, Karin / Gingnell, Malin / Frick, Andreas

Developmental psychobiology

2024 Volume 66, Issue 4, Page(s) e22492

Abstract: ... in a sample of typically developed adolescents (n = 37; 13-16 years) and adults (n = 39; 30-40 years), and ...

Abstract	During adolescence, emotion regulation and reactivity are still developing and are in many ways qualitatively different from adulthood. However, the neurobiological processes underpinning these differences remain poorly understood, including the role of maturing neurotransmitter systems. We combined magnetic resonance spectroscopy in the dorsal anterior cingulate cortex (dACC) and self-reported emotion regulation and reactivity in a sample of typically developed adolescents (n = 37; 13-16 years) and adults (n = 39; 30-40 years), and found that adolescents had higher levels of glutamate to total creatine (tCr) ratio in the dACC than adults. A glutamate Í age group interaction indicated a differential relation between dACC glutamate levels and emotion regulation in adolescents and adults, and within-group follow-up analyses showed that higher levels of glutamate/tCr were related to worse emotion regulation skills in adolescents. We found no age-group differences in gamma-aminobutyric acid+macromolecules (GABA+) levels; however, emotion reactivity was positively related to GABA+/tCr in the adult group, but not in the adolescent group. The results demonstrate that there are developmental changes in the concentration of glutamate, but not GABA+, within the dACC from adolescence to adulthood, in accordance with previous findings indicating earlier maturation of the GABA-ergic than the glutamatergic system. Functionally, glutamate and GABA+ are positively related to emotion regulation and reactivity, respectively, in the mature brain. In the adolescent brain, however, glutamate is negatively related to emotion regulation, and GABA+ is not related to emotion reactivity. The findings are consistent with synaptic pruning of glutamatergic synapses from adolescence to adulthood and highlight the importance of brain maturational processes underlying age-related differences in emotion processing.
MeSH term(s)	Adult ; Humans ; Adolescent ; Glutamic Acid ; Gyrus Cinguli/chemistry ; Gyrus Cinguli/physiology ; Emotional Regulation ; gamma-Aminobutyric Acid/analysis ; Receptors, Antigen, T-Cell/analysis
Chemical Substances	Glutamic Acid (3KX376GY7L) ; gamma-Aminobutyric Acid (56-12-2) ; Receptors, Antigen, T-Cell
Language	English
Publishing date	2024-04-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	4107-5
ISSN	1098-2302 ; 0012-1630
ISSN (online)	1098-2302
ISSN	0012-1630
DOI	10.1002/dev.22492
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 1102: 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: Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3.

Frick, David N / Virdi, Rajdeep S / Vuksanovic, Nemanja / Dahal, Narayan / Silvaggi, Nicholas R

Biochemistry

2020 Volume 59, Issue 28, Page(s) 2608–2615

Abstract: The virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymerase, helicase, and main protease, are well conserved ...

Abstract	The virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymerase, helicase, and main protease, are well conserved between SARS-CoV-2 and the original SARS virus, but several others are not. This study examines one of the proteins encoded by SARS-CoV-2 that is most different, a macrodomain of nonstructural protein 3 (nsp3). Although 26% of the amino acids in this SARS-CoV-2 macrodomain differ from those observed in other coronaviruses, biochemical and structural data reveal that the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses and a potential therapeutic target.
MeSH term(s)	Adenosine Diphosphate Ribose/metabolism ; Betacoronavirus/chemistry ; COVID-19 ; Coronavirus/chemistry ; Coronavirus Infections/drug therapy ; Coronavirus Infections/virology ; Coronavirus Papain-Like Proteases ; Crystallography, X-Ray ; Drug Delivery Systems ; Humans ; Models, Molecular ; Pandemics ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/virology ; Protein Domains ; SARS-CoV-2 ; Thermodynamics ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/metabolism
Chemical Substances	Viral Nonstructural Proteins ; Adenosine Diphosphate Ribose (20762-30-5) ; Coronavirus Papain-Like Proteases (EC 3.4.22.2) ; papain-like protease, SARS-CoV-2 (EC 3.4.22.2)
Keywords	covid19
Language	English
Publishing date	2020-07-06
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	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.0c00309
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: Role of the Conserved DECH-Box Cysteine in Coupling Hepatitis C Virus Helicase-Catalyzed ATP Hydrolysis to RNA Unwinding.

Yerukhimovich, Mark M / Marohnic, Christopher C / Frick, David N

Biochemistry

2018 Volume 57, Issue 43, Page(s) 6247–6255

Abstract: DECH-box proteins are a subset of DExH/D-box superfamily 2 helicases possessing a conserved Asp-Glu-Cys-His motif in their ATP binding site. The conserved His helps position the Asp and Glu residues, which coordinate the divalent metal cation that ... ...

Abstract	DECH-box proteins are a subset of DExH/D-box superfamily 2 helicases possessing a conserved Asp-Glu-Cys-His motif in their ATP binding site. The conserved His helps position the Asp and Glu residues, which coordinate the divalent metal cation that connects the protein to ATP and activate the water molecule needed for ATP hydrolysis, but the role of the Cys is still unclear. This study uses site-directed mutants of the model DECH-box helicase encoded by the hepatitis C virus (HCV) to examine the role of the Cys in helicase action. Proteins lacking a Cys unwound DNA less efficiently than wild-type proteins did. For example, at low protein concentrations, a helicase harboring a Gly instead of the DECH-box Cys unwound DNA more slowly than the wild-type helicase did, but at higher protein concentrations, the two proteins unwound DNA at similar rates. All HCV proteins analyzed had similar affinities for ATP and nucleic acids and hydrolyzed ATP in the presence of RNA at similar rates. However, in the absence of RNA, all proteins lacking a DECH-box cysteine hydrolyzed ATP 10-15 times faster with higher K
MeSH term(s)	Adenosine Triphosphate/metabolism ; Binding Sites ; Catalysis ; Cysteine/chemistry ; Cysteine/genetics ; Cysteine/metabolism ; DNA/chemistry ; DNA/metabolism ; Hepacivirus/enzymology ; Humans ; Hydrolysis ; Mutagenesis, Site-Directed ; Mutation ; RNA/chemistry ; RNA/metabolism ; Substrate Specificity ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism
Chemical Substances	NS3 protein, hepatitis C virus ; Viral Nonstructural Proteins ; RNA (63231-63-0) ; Adenosine Triphosphate (8L70Q75FXE) ; DNA (9007-49-2) ; Cysteine (K848JZ4886)
Language	English
Publishing date	2018-10-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.8b00796
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: New Techniques to Study Intracellular Receptors in Living Cells: Insights Into RIG-I-Like Receptor Signaling.

Corby, M J / Raicu, Valerica / Frick, David N

Advances in experimental medicine and biology

2018 Volume 1111, Page(s) 219–240

Abstract: This review discusses new developments in Förster resonance energy transfer (FRET) microscopy and its application to cellular receptors. The method is based on the kinetic theory of FRET, which can be used to predict FRET not only in dimers, but also ... ...

Abstract	This review discusses new developments in Förster resonance energy transfer (FRET) microscopy and its application to cellular receptors. The method is based on the kinetic theory of FRET, which can be used to predict FRET not only in dimers, but also higher order oligomers of donor and acceptor fluorophores. Models based on such FRET predictions can be fit to observed FRET efficiency histograms (also called FRET spectrograms) and used to estimate intracellular binding constants, free energy values, and stoichiometries. These "FRET spectrometry" methods have been used to analyze oligomers formed by various receptors in cell signaling pathways, but until recently such studies were limited to receptors residing on the cell surface. To study complexes residing inside the cell, a technique called Quantitative Micro-Spectroscopic Imaging (Q-MSI) was developed. Q-MSI combines determination of quaternary structure from pixel-level apparent FRET spectrograms with the determination of both donor and acceptor concentrations at the organelle level. This is done by resolving and analyzing the spectrum of a third fluorescent marker, which does not participate in FRET. Q-MSI was first used to study the interaction of a class of cytoplasmic receptors that bind viral RNA and signal an antiviral response via complexes formed mainly on mitochondrial membranes. Q-MSI revealed previously unknown RNA mitochondrial receptor orientations, and the interaction between the viral RNA receptor called LGP2 with the RNA helicase encoded by the hepatitis virus. The biological importance of these new observations is discussed.
MeSH term(s)	Cell Survival ; DEAD Box Protein 58/metabolism ; Fluorescence Resonance Energy Transfer ; Signal Transduction
Chemical Substances	DEAD Box Protein 58 (EC 3.6.4.13)
Language	English
Publishing date	2018-11-23
Publishing country	United States
Document type	Journal Article ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/5584_2018_297
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Molecular Basis for ADP-Ribose Binding to the Mac1 Domain of SARS-CoV-2 nsp3

Frick, David N / Virdi, Rajdeep S / Vuksanovic, Nemanja / Dahal, Narayan / Silvaggi, Nicholas R

Biochemistry. 2020 June 24, v. 59, no. 28

2020

Abstract	The virus that causes COVID-19, SARS-CoV-2, has a large RNA genome that encodes numerous proteins that might be targets for antiviral drugs. Some of these proteins, such as the RNA-dependent RNA polymerase, helicase, and main protease, are well conserved between SARS-CoV-2 and the original SARS virus, but several others are not. This study examines one of the proteins encoded by SARS-CoV-2 that is most different, a macrodomain of nonstructural protein 3 (nsp3). Although 26% of the amino acids in this SARS-CoV-2 macrodomain differ from those observed in other coronaviruses, biochemical and structural data reveal that the protein retains the ability to bind ADP-ribose, which is an important characteristic of beta coronaviruses and a potential therapeutic target.
Keywords	Coronavirus infections ; Orthocoronavirinae ; RNA ; RNA-directed RNA polymerase ; amino acids ; antiviral agents ; genome ; proteinases ; therapeutics ; viral nonstructural proteins ; viruses
Language	English
Dates of publication	2020-0624
Size	p. 2608-2615.
Publishing place	American Chemical Society
Document type	Article
Note	NAL-light
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.0c00309
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

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

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

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