LIVIVO - Search results -

Search results

Result 1 - 10 of total 188

Search options

Article: A unifying model to explain high nirmatrelvir therapeutic efficacy against SARS-CoV-2, despite low post-exposure prophylaxis efficacy and frequent viral rebound.

Esmaeili, Shadisadat / Owens, Katherine / Wagoner, Jessica / Polyak, Stephen J / White, Judith M / Schiffer, Joshua T

medRxiv : the preprint server for health sciences

2024

Abstract: In a pivotal trial (EPIC-HR), a 5-day course of oral ritonavir-boosted nirmatrelvir, given early during symptomatic SARS-CoV-2 infection (within three days of symptoms onset), decreased hospitalization and death by 89.1% and nasal viral load by 0.87 log ... ...

Abstract	In a pivotal trial (EPIC-HR), a 5-day course of oral ritonavir-boosted nirmatrelvir, given early during symptomatic SARS-CoV-2 infection (within three days of symptoms onset), decreased hospitalization and death by 89.1% and nasal viral load by 0.87 log relative to placebo in high-risk individuals. Yet, nirmatrelvir/ritonavir failed as post-exposure prophylaxis in a trial, and frequent viral rebound has been observed in subsequent cohorts. We developed a mathematical model capturing viral-immune dynamics and nirmatrelvir pharmacokinetics that recapitulated viral loads from this and another clinical trial (PLATCOV). Our results suggest that nirmatrelvir's
Language	English
Publishing date	2024-04-17
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.08.23.23294505
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: Viral Membrane Fusion: A Dance Between Proteins and Lipids.

White, Judith M / Ward, Amanda E / Odongo, Laura / Tamm, Lukas K

Annual review of virology

2023 Volume 10, Issue 1, Page(s) 139–161

Abstract: There are at least 21 families of enveloped viruses that infect mammals, and many contain members of high concern for global human health. All enveloped viruses have a dedicated fusion protein or fusion complex that enacts the critical genome-releasing ... ...

Abstract	There are at least 21 families of enveloped viruses that infect mammals, and many contain members of high concern for global human health. All enveloped viruses have a dedicated fusion protein or fusion complex that enacts the critical genome-releasing membrane fusion event that is essential before viral replication within the host cell interior can begin. Because all enveloped viruses enter cells by fusion, it behooves us to know how viral fusion proteins function. Viral fusion proteins are also major targets of neutralizing antibodies, and hence they serve as key vaccine immunogens. Here we review current concepts about viral membrane fusion proteins focusing on how they are triggered, structural intermediates between pre- and postfusion forms, and their interplay with the lipid bilayers they engage. We also discuss cellular and therapeutic interventions that thwart virus-cell membrane fusion.
MeSH term(s)	Animals ; Humans ; Virus Internalization ; Viral Fusion Proteins/chemistry ; Membrane Fusion ; Viruses/genetics ; Lipids ; Mammals/metabolism
Chemical Substances	Viral Fusion Proteins ; Lipids
Language	English
Publishing date	2023-09-29
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	2764224-0
ISSN	2327-0578 ; 2327-056X
ISSN (online)	2327-0578
ISSN	2327-056X
DOI	10.1146/annurev-virology-111821-093413
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: A novel

Odongo, Laura / Habtegebrael, Betelihem H / Kiessling, Volker / White, Judith M / Tamm, Lukas K

Microbiology spectrum

2023 , Page(s) e0190823

Abstract: Ebola virus (EBOV) causes a hemorrhagic fever with fatality rates up to 90%. The EBOV entry process is complex and incompletely understood. Following attachment to host cells, EBOV is trafficked to late endosomes/lysosomes where its glycoprotein (GP) is ... ...

Abstract	Ebola virus (EBOV) causes a hemorrhagic fever with fatality rates up to 90%. The EBOV entry process is complex and incompletely understood. Following attachment to host cells, EBOV is trafficked to late endosomes/lysosomes where its glycoprotein (GP) is processed to a 19-kDa form, which binds to the EBOV intracellular receptor Niemann-Pick type C1. We previously showed that the cathepsin protease inhibitor, E-64d, blocks infection by pseudovirus particles bearing 19-kDa GP, suggesting that further cathepsin action is needed to trigger fusion. This, however, has not been demonstrated directly. Since 19-kDa Ebola GP fusion occurs in late endosomes, we devised a system in which enriched late endosomes are used to prepare supported planar endosomal membranes (SPEMs), and fusion of fluorescent (pseudo)virus particles is monitored by total internal reflection fluorescence microscopy. We validated the system by demonstrating the pH dependencies of influenza virus hemagglutinin (HA)-mediated and Lassa virus (LASV) GP-mediated fusion. Using SPEMs, we showed that fusion mediated by 19-kDa Ebola GP is dependent on low pH, enhanced by Ca
Language	English
Publishing date	2023-09-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	2807133-5
ISSN	2165-0497 ; 2165-0497
ISSN (online)	2165-0497
ISSN	2165-0497
DOI	10.1128/spectrum.01908-23
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Endosomes supporting fusion mediated by vesicular stomatitis virus glycoprotein have distinctive motion and acidification.

Cabot, Maya / Kiessling, Volker / White, Judith M / Tamm, Lukas K

Traffic (Copenhagen, Denmark)

2022 Volume 23, Issue 4, Page(s) 221–234

Abstract: Most enveloped viruses infect cells by binding receptors at the cell surface and undergo trafficking through the endocytic pathway to a compartment with the requisite conditions to trigger fusion with a host endosomal membrane. Broad categories of ... ...

Abstract	Most enveloped viruses infect cells by binding receptors at the cell surface and undergo trafficking through the endocytic pathway to a compartment with the requisite conditions to trigger fusion with a host endosomal membrane. Broad categories of compartments in the endocytic pathway include early and late endosomes, which can be further categorized into subpopulations with differing rates of maturation and motility characteristics. Endocytic compartments have varying protein and lipid components, luminal ionic conditions and pH that provide uniquely hospitable environments for specific viruses to fuse. In order to characterize compartments that permit fusion, we studied the trafficking and fusion of viral particles pseudotyped with the vesicular stomatitis virus glycoprotein (VSV-G) on their surface and equipped with a novel pH sensor and a fluorescent content marker to measure pH, motion and fusion at the single particle level in live cells. We found that the VSV-G particles fuse predominantly from more acidic and more motile endosomes, and that a significant fraction of particles is trafficked to more static and less acidic endosomes that do not support their fusion. Moreover, the fusion-supporting endosomes undergo directed motion.
MeSH term(s)	Animals ; Endocytosis ; Endosomes/metabolism ; Glycoproteins/metabolism ; Hydrogen-Ion Concentration ; Vesicular Stomatitis/metabolism ; Virus Internalization
Chemical Substances	Glycoproteins
Language	English
Publishing date	2022-02-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1483852-7
ISSN	1600-0854 ; 1398-9219
ISSN (online)	1600-0854
ISSN	1398-9219
DOI	10.1111/tra.12836
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 5634: 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 ; Online: Two-way pharmacodynamic modeling of drug combinations and its application to pairs of repurposed Ebola and SARS-CoV-2 agents.

Xu, Shuang / Esmaeili, Shadisadat / Cardozo-Ojeda, E Fabian / Goyal, Ashish / White, Judith M / Polyak, Stephen J / Schiffer, Joshua T

Antimicrobial agents and chemotherapy

2024 Volume 68, Issue 4, Page(s) e0101523

Abstract: Existing pharmacodynamic (PD) mathematical models for drug combinations discriminate antagonistic, additive, multiplicative, and synergistic effects, but fail to consider how concentration-dependent drug interaction effects may vary across an entire dose- ...

Abstract	Existing pharmacodynamic (PD) mathematical models for drug combinations discriminate antagonistic, additive, multiplicative, and synergistic effects, but fail to consider how concentration-dependent drug interaction effects may vary across an entire dose-response matrix. We developed a two-way pharmacodynamic (TWPD) model to capture the PD of two-drug combinations. TWPD captures interactions between upstream and downstream drugs that act on different stages of viral replication, by quantifying upstream drug efficacy and concentration-dependent effects on downstream drug pharmacodynamic parameters. We applied TWPD to previously published
MeSH term(s)	Humans ; Models, Biological ; SARS-CoV-2 ; Hemorrhagic Fever, Ebola/drug therapy ; COVID-19 ; Drug Combinations
Chemical Substances	Drug Combinations
Language	English
Publishing date	2024-03-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	217602-6
ISSN	1098-6596 ; 0066-4804
ISSN (online)	1098-6596
ISSN	0066-4804
DOI	10.1128/aac.01015-23
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 809: 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)
Einzelsignatur: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Unlocking avian museum collections to enable and advance environmental change research

Norris, Ken / Bond, Alexander L. / Cooper, Joanna H. / Adams, Mark P. / van Grouw, Hein / White, Judith / Stervander, Martin / Russell, Douglas G. D. / Loader, Simon P.

Ibis. 2024 Jan., v. 166, no. 1 p.315-322

2024

Abstract: The rate and magnitude of contemporary changes in natural systems is unprecedented in the Earth's history. Studies of wild birds have been critically important in helping us understand and address these environmental changes. Avian collections provide a ... ...

Abstract	The rate and magnitude of contemporary changes in natural systems is unprecedented in the Earth's history. Studies of wild birds have been critically important in helping us understand and address these environmental changes. Avian collections provide a potentially unique perspective on change through time, but their role in environmental change research is limited by the availability of collections data. Here we describe how avian collections might be unlocked to enable environmental change research, and discuss the opportunities and constraints associated with this. We use the concept of the extended specimen to describe the types of data that could be unlocked from basic data for discoverability to enhanced data that might be directly applied to environmental change questions. We illustrate the type of environmental change research these data might support. We argue that data creation and access is currently limited by funding for digitization, a rather patchy understanding of the needs of the research community and less than adequate data‐sharing by institutions and researchers. We develop a blueprint for addressing these issues which includes (1) improvements in sharing the data we are already creating and (2) building a better case for digitization at scale. As one of the largest avian collections in the world, the Natural History Museum, UK, is committed to unlocking our collections, but we will need input and support from the avian research community to do so.
Keywords	data collection ; funding ; museums ; researchers ; type collections ; wild birds ; wills
Language	English
Dates of publication	2024-01
Size	p. 315-322.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	JOURNAL ARTICLE
ZDB-ID	2071870-6
ISSN	1474-919X ; 0019-1019
ISSN (online)	1474-919X
ISSN	0019-1019
DOI	10.1111/ibi.13271
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Implementation of high-throughput non-invasive prenatal testing for fetal RHD genotype testing in England: Results of a cross-sectional survey of maternity units and expert interviews.

Ryczek, Edyta / White, Judith / Carolan-Rees, Grace

Transfusion medicine (Oxford, England)

2020 Volume 30, Issue 4, Page(s) 287–294

Abstract: Background: Previously, routine antenatal anti-D prophylaxis (RAADP) was administered to all RhD-negative mothers to reduce the risk of sensitisation in the UK's National Health Service (NHS). If the baby is RhD-negative, RAADP is not required. In 2016, ...

Abstract	Background: Previously, routine antenatal anti-D prophylaxis (RAADP) was administered to all RhD-negative mothers to reduce the risk of sensitisation in the UK's National Health Service (NHS). If the baby is RhD-negative, RAADP is not required. In 2016, the UK National Institute for Health and Care Excellence (NICE) recommended non-invasive prenatal testing (NIPT) for fetal RHD genotype as a cost-effective option to guide RAADP. Objectives: To evaluate the implementation of high-throughput NIPT for fetal RHD genotype in maternity units in England by addressing research recommendations from the NICE. These were to reduce uncertainty around the resource use and cost of staff training, management of samples and results and record-keeping, as well as resultant changes to antenatal or post-partum care and performance of NIPT. Methods: A cross-sectional survey was developed and sent to clinicians at 39 English NHS Trusts in May 2018. Qualitative interviews with seven individuals were conducted to explore missing or contraindicatory data. Qualitative findings were supplemented with NIPT test results (April 2017 to February 2019) from English hospitals. Results: Staff reported that training took up to 30 minutes. There were no extra costs associated with sample management or additional appointments. Extra time required for record-keeping and management of test results was balanced later in the patient pathway. The antenatal pathway was not changed in the Trusts surveyed. The survey revealed that four post-partum scenarios were being used within English NHS Trusts. The frequency of inconclusive NIPT results was 4.3%. Conclusion: NIPT for fetal RHD genotype can be implemented without consuming substantial extra resources through incorporation into an existing patient pathway.
MeSH term(s)	Adult ; Cross-Sectional Studies ; England ; Female ; Genotype ; Humans ; Pregnancy ; Prenatal Diagnosis ; Rh Isoimmunization/diagnosis ; Rh Isoimmunization/genetics ; Rh-Hr Blood-Group System/genetics
Chemical Substances	Rh-Hr Blood-Group System ; Rho(D) antigen
Language	English
Publishing date	2020-06-11
Publishing country	England
Document type	Journal Article ; Observational Study
ZDB-ID	1067989-3
ISSN	1365-3148 ; 0958-7578
ISSN (online)	1365-3148
ISSN	0958-7578
DOI	10.1111/tme.12702
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 3177: 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 ; Online: Purification and structure of luminal domain C of human Niemann-Pick C1 protein.

Odongo, Laura / Zadrozny, Kaneil K / Diehl, William E / Luban, Jeremy / White, Judith M / Ganser-Pornillos, Barbie K / Tamm, Lukas K / Pornillos, Owen

Acta crystallographica. Section F, Structural biology communications

2023 Volume 79, Issue Pt 2, Page(s) 45–50

Abstract: Niemann-Pick C1 protein (NPC1) is a membrane protein that primarily resides in late endosomes and lysosomes, and plays an important role in cholesterol homeostasis in the cell. The second luminal domain of NPC1 (NPC1-C) serves as the intracellular ... ...

Abstract	Niemann-Pick C1 protein (NPC1) is a membrane protein that primarily resides in late endosomes and lysosomes, and plays an important role in cholesterol homeostasis in the cell. The second luminal domain of NPC1 (NPC1-C) serves as the intracellular receptor for Ebola and Marburg viruses. Here, the recombinant production of nonglycosylated and glycosylated NPC1-C and a new crystal form of the nonglycosylated protein are reported. The crystals belonged to space group P2
MeSH term(s)	Humans ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/metabolism ; Niemann-Pick C1 Protein/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Crystallography, X-Ray ; Glycoproteins/chemistry ; Lysosomes/metabolism
Chemical Substances	Membrane Glycoproteins ; Niemann-Pick C1 Protein ; Intracellular Signaling Peptides and Proteins ; Glycoproteins
Language	English
Publishing date	2023-02-02
Publishing country	United States
Document type	Journal Article
ISSN	2053-230X
ISSN (online)	2053-230X
DOI	10.1107/S2053230X23000705
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

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 ▾
- Full text online
- Order with fees

Article: The conundrum of an overlooked skeleton referable to Imperial Woodpecker Campephilus imperialis in the collection of the Natural History Museum at Tring

Prŷs-Jones, Robert P / Manegold, Albrecht / White, Judith

Bulletin of the British Ornithologists' Club. 2021 Mar. 9, v. 141, no. 1

2021

Abstract: The discovery of an overlooked skeleton of Imperial Woodpecker Campephilus imperialis in the bird collection of the Natural History Museum at Tring (NHMUK) is documented, one of very few known to exist worldwide of this almost certainly extinct species. ... ...

Abstract	The discovery of an overlooked skeleton of Imperial Woodpecker Campephilus imperialis in the bird collection of the Natural History Museum at Tring (NHMUK) is documented, one of very few known to exist worldwide of this almost certainly extinct species. We present evidence that, on balance of probabilities, it is one of two collected by Alphonse Forrer in 1882 near the settlement of La Ciudad in the Sierra Madre Occidental, Durango, western Mexico; the whereabouts of the other, which did not come to NHMUK, appears currently unknown. During research into the NHMUK specimen, we demonstrated that the supposed Imperial Woodpecker skull held in the collection of the Russian Academy of Sciences, St. Petersburg, must in fact be that of an Ivory-billed Woodpecker C. principalis.
Keywords	extinct species ; skeleton ; skull ; woodpeckers ; Mexico
Language	English
Dates of publication	2021-0309
Size	p. 66-74.
Publishing place	British Ornithologists’ Club
Document type	Article
Note	NAL-light
ZDB-ID	2927179-4
ISSN	2513-9894 ; 0007-1595
ISSN (online)	2513-9894
ISSN	0007-1595
DOI	10.25226/bboc.v141i1.2021.a7
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article ; Online: Discovery of host-directed modulators of virus infection by probing the SARS-CoV-2-host protein-protein interaction network.

Ravindran, Vandana / Wagoner, Jessica / Athanasiadis, Paschalis / Den Hartigh, Andreas B / Sidorova, Julia M / Ianevski, Aleksandr / Fink, Susan L / Frigessi, Arnoldo / White, Judith / Polyak, Stephen J / Aittokallio, Tero

Briefings in bioinformatics

2024 Volume 23, Issue 6

Abstract: The ongoing coronavirus disease 2019 (COVID-19) pandemic has highlighted the need to better understand virus-host interactions. We developed a network-based method that expands the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2)-host protein ...

Abstract	The ongoing coronavirus disease 2019 (COVID-19) pandemic has highlighted the need to better understand virus-host interactions. We developed a network-based method that expands the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2)-host protein interaction network and identifies host targets that modulate viral infection. To disrupt the SARS-CoV-2 interactome, we systematically probed for potent compounds that selectively target the identified host proteins with high expression in cells relevant to COVID-19. We experimentally tested seven chemical inhibitors of the identified host proteins for modulation of SARS-CoV-2 infection in human cells that express ACE2 and TMPRSS2. Inhibition of the epigenetic regulators bromodomain-containing protein 4 (BRD4) and histone deacetylase 2 (HDAC2), along with ubiquitin-specific peptidase (USP10), enhanced SARS-CoV-2 infection. Such proviral effect was observed upon treatment with compounds JQ1, vorinostat, romidepsin and spautin-1, when measured by cytopathic effect and validated by viral RNA assays, suggesting that the host proteins HDAC2, BRD4 and USP10 have antiviral functions. We observed marked differences in antiviral effects across cell lines, which may have consequences for identification of selective modulators of viral infection or potential antiviral therapeutics. While network-based approaches enable systematic identification of host targets and selective compounds that may modulate the SARS-CoV-2 interactome, further developments are warranted to increase their accuracy and cell-context specificity.
MeSH term(s)	Humans ; SARS-CoV-2 ; Protein Interaction Maps ; Nuclear Proteins ; Transcription Factors ; Antiviral Agents/pharmacology ; Ubiquitin Thiolesterase ; Cell Cycle Proteins ; COVID-19 Drug Treatment
Chemical Substances	Nuclear Proteins ; Transcription Factors ; Antiviral Agents ; USP10 protein, human ; Ubiquitin Thiolesterase (EC 3.4.19.12) ; BRD4 protein, human ; Cell Cycle Proteins
Language	English
Publishing date	2024-05-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2068142-2
ISSN	1477-4054 ; 1467-5463
ISSN (online)	1477-4054
ISSN	1467-5463
DOI	10.1093/bib/bbac456
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 6262: 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

To top

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

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

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

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