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Article: In vitro

Hoffmann, Magnus A G / Kieffer, Collin / Bjorkman, Pamela J

Molecular therapy. Methods & clinical development

2021 Volume 21, Page(s) 161–170

Abstract: Engineered red blood cells (RBCs) expressing viral receptors could be used therapeutically as viral traps, as RBCs lack nuclei and other organelles required for viral replication. However, expression of viral receptors on RBCs is difficult to achieve ... ...

Abstract	Engineered red blood cells (RBCs) expressing viral receptors could be used therapeutically as viral traps, as RBCs lack nuclei and other organelles required for viral replication. However, expression of viral receptors on RBCs is difficult to achieve since mature erythrocytes lack the cellular machinery to synthesize proteins. Herein, we show that the combination of a powerful erythroid-specific expression system and transgene codon optimization yields high expression levels of the HIV-1 receptors CD4 and CCR5, as well as a CD4-glycophorin A (CD4-GpA) fusion protein in erythroid progenitor cells, which efficiently differentiated into enucleated RBCs. HIV-1 efficiently entered RBCs that co-expressed CD4 and CCR5, but viral entry was not required for neutralization, as CD4 or CD4-GpA expression in the absence of CCR5 was sufficient to potently neutralize HIV-1 and prevent infection of CD4
Language	English
Publishing date	2021-03-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	2872938-9
ISSN	2329-0501 ; 2329-0501
ISSN (online)	2329-0501
ISSN	2329-0501
DOI	10.1016/j.omtm.2021.03.003
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Article ; Online: ESCRT recruitment to SARS-CoV-2 spike induces virus-like particles that improve mRNA vaccines.

Hoffmann, Magnus A G / Yang, Zhi / Huey-Tubman, Kathryn E / Cohen, Alexander A / Gnanapragasam, Priyanthi N P / Nakatomi, Leesa M / Storm, Kaya N / Moon, Woohyun J / Lin, Paulo J C / West, Anthony P / Bjorkman, Pamela J

Cell

2023 Volume 186, Issue 11, Page(s) 2380–2391.e9

Abstract: Prime-boost regimens for COVID-19 vaccines elicit poor antibody responses against Omicron-based variants and employ frequent boosters to maintain antibody levels. We present a natural infection-mimicking technology that combines features of mRNA- and ... ...

Abstract	Prime-boost regimens for COVID-19 vaccines elicit poor antibody responses against Omicron-based variants and employ frequent boosters to maintain antibody levels. We present a natural infection-mimicking technology that combines features of mRNA- and protein nanoparticle-based vaccines through encoding self-assembling enveloped virus-like particles (eVLPs). eVLP assembly is achieved by inserting an ESCRT- and ALIX-binding region (EABR) into the SARS-CoV-2 spike cytoplasmic tail, which recruits ESCRT proteins to induce eVLP budding from cells. Purified spike-EABR eVLPs presented densely arrayed spikes and elicited potent antibody responses in mice. Two immunizations with mRNA-LNP encoding spike-EABR elicited potent CD8
MeSH term(s)	Animals ; Humans ; Mice ; Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19/prevention & control ; COVID-19 Vaccines ; Endosomal Sorting Complexes Required for Transport ; mRNA Vaccines ; RNA, Messenger ; SARS-CoV-2
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; COVID-19 Vaccines ; Endosomal Sorting Complexes Required for Transport ; mRNA Vaccines ; RNA, Messenger
Language	English
Publishing date	2023-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2023.04.024
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Zs.A 1167: 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)
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Article ; Online: ESCRT recruitment to SARS-CoV-2 spike induces virus-like particles that improve mRNA vaccines

Hoffmann, Magnus A.G. / Yang, Zhi / Huey-Tubman, Kathryn E. / Cohen, Alexander A. / Gnanapragasam, Priyanthi N.P. / Nakatomi, Leesa M. / Storm, Kaya N. / Moon, Woohyun J. / Lin, Paulo J.C. / West, Anthony P. / Bjorkman, Pamela J.

Cell. 2023 May, v. 186, no. 11 p.2380-2391.e9

2023

Abstract	Prime-boost regimens for COVID-19 vaccines elicit poor antibody responses against Omicron-based variants and employ frequent boosters to maintain antibody levels. We present a natural infection-mimicking technology that combines features of mRNA- and protein nanoparticle-based vaccines through encoding self-assembling enveloped virus-like particles (eVLPs). eVLP assembly is achieved by inserting an ESCRT- and ALIX-binding region (EABR) into the SARS-CoV-2 spike cytoplasmic tail, which recruits ESCRT proteins to induce eVLP budding from cells. Purified spike-EABR eVLPs presented densely arrayed spikes and elicited potent antibody responses in mice. Two immunizations with mRNA-LNP encoding spike-EABR elicited potent CD8⁺ T cell responses and superior neutralizing antibody responses against original and variant SARS-CoV-2 compared with conventional spike-encoding mRNA-LNP and purified spike-EABR eVLPs, improving neutralizing titers >10-fold against Omicron-based variants for 3 months post-boost. Thus, EABR technology enhances potency and breadth of vaccine-induced responses through antigen presentation on cell surfaces and eVLPs, enabling longer-lasting protection against SARS-CoV-2 and other viruses.
Keywords	COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; T-lymphocytes ; antibodies ; antigen presentation ; nanoparticles ; mRNA vaccines ; SARS-CoV-2 ; ESCRT
Language	English
Dates of publication	2023-05
Size	p. 2380-2391.e9.
Publishing place	Elsevier Inc.
Document type	Article ; Online
Note	Pre-press version ; Use and reproduction
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2023.04.024
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Oxygenation properties of hemoglobin and the evolutionary origins of isoform multiplicity in an amphibious air-breathing fish, the blue-spotted mudskipper (

Storz, Jay F / Natarajan, Chandrasekhar / Grouleff, Magnus K / Vandewege, Michael / Hoffmann, Federico G / You, Xinxin / Venkatesh, Byrappa / Fago, Angela

The Journal of experimental biology

2020 Volume 223, Issue Pt 2

Abstract: Among the numerous lineages of teleost fish that have independently transitioned from obligate water breathing to facultative air breathing, evolved properties of hemoglobin (Hb)- ... ...

Abstract	Among the numerous lineages of teleost fish that have independently transitioned from obligate water breathing to facultative air breathing, evolved properties of hemoglobin (Hb)-O
MeSH term(s)	Animals ; Evolution, Molecular ; Fishes/physiology ; Hemoglobins/chemistry ; Protein Isoforms/chemistry ; Respiration
Chemical Substances	Hemoglobins ; Protein Isoforms
Language	English
Publishing date	2020-01-23
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	218085-6
ISSN	1477-9145 ; 0022-0949
ISSN (online)	1477-9145
ISSN	0022-0949
DOI	10.1242/jeb.217307
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Article ; Online: Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer.

Yang, Zhi / Dam, Kim-Marie A / Bridges, Michael D / Hoffmann, Magnus A G / DeLaitsch, Andrew T / Gristick, Harry B / Escolano, Amelia / Gautam, Rajeev / Martin, Malcolm A / Nussenzweig, Michel C / Hubbell, Wayne L / Bjorkman, Pamela J

Nature communications

2022 Volume 13, Issue 1, Page(s) 732

Abstract: Broadly-neutralizing antibodies (bNAbs) against HIV-1 Env can protect from infection. We characterize Ab1303 and Ab1573, heterologously-neutralizing CD4-binding site (CD4bs) antibodies, isolated from sequentially-immunized macaques. Ab1303/Ab1573 binding ...

Abstract	Broadly-neutralizing antibodies (bNAbs) against HIV-1 Env can protect from infection. We characterize Ab1303 and Ab1573, heterologously-neutralizing CD4-binding site (CD4bs) antibodies, isolated from sequentially-immunized macaques. Ab1303/Ab1573 binding is observed only when Env trimers are not constrained in the closed, prefusion conformation. Fab-Env cryo-EM structures show that both antibodies recognize the CD4bs on Env trimer with an 'occluded-open' conformation between closed, as targeted by bNAbs, and fully-open, as recognized by CD4. The occluded-open Env trimer conformation includes outwardly-rotated gp120 subunits, but unlike CD4-bound Envs, does not exhibit V1V2 displacement, 4-stranded gp120 bridging sheet, or co-receptor binding site exposure. Inter-protomer distances within trimers measured by double electron-electron resonance spectroscopy suggest an equilibrium between occluded-open and closed Env conformations, consistent with Ab1303/Ab1573 binding stabilizing an existing conformation. Studies of Ab1303/Ab1573 demonstrate that CD4bs neutralizing antibodies that bind open Env trimers can be raised by immunization, thereby informing immunogen design and antibody therapeutic efforts.
MeSH term(s)	Animals ; Antibodies, Neutralizing/isolation & purification ; Antibodies, Neutralizing/pharmacology ; Antibodies, Neutralizing/therapeutic use ; Antibodies, Neutralizing/ultrastructure ; Binding Sites ; CD4 Antigens/immunology ; CD4 Antigens/metabolism ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Drug Design ; HIV Antibodies/isolation & purification ; HIV Antibodies/pharmacology ; HIV Antibodies/therapeutic use ; HIV Antibodies/ultrastructure ; HIV Infections/drug therapy ; HIV Infections/immunology ; HIV Infections/virology ; HIV-1/immunology ; Humans ; Macaca ; Molecular Docking Simulation ; Protein Binding ; Protein Domains ; Protein Multimerization ; env Gene Products, Human Immunodeficiency Virus/immunology ; env Gene Products, Human Immunodeficiency Virus/metabolism
Chemical Substances	Antibodies, Neutralizing ; CD4 Antigens ; HIV Antibodies ; env Gene Products, Human Immunodeficiency Virus
Language	English
Publishing date	2022-02-08
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-28424-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: ESCRT recruitment to mRNA-encoded SARS-CoV-2 spike induces virus-like particles and enhanced antibody responses.

Hoffmann, Magnus A G / Yang, Zhi / Huey-Tubman, Kathryn E / Cohen, Alexander A / Gnanapragasam, Priyanthi N P / Nakatomi, Leesa M / Storm, Kaya N / Moon, Woohyun J / Lin, Paulo J C / Bjorkman, Pamela J

bioRxiv : the preprint server for biology

2022

Abstract	Prime-boost regimens for COVID-19 vaccines elicit poor antibody responses against Omicron-based variants and employ frequent boosters to maintain antibody levels. We present a natural infection-mimicking technology that combines features of mRNA- and protein nanoparticle-based vaccines through encoding self-assembling enveloped virus-like particles (eVLPs). eVLP assembly is achieved by inserting an ESCRT- and ALIX-binding region (EABR) into the SARS-CoV-2 spike cytoplasmic tail, which recruits ESCRT proteins to induce eVLP budding from cells. Purified spike-EABR eVLPs presented densely-arrayed spikes and elicited potent antibody responses in mice. Two immunizations with mRNA-LNP encoding spike-EABR elicited potent CD8+ T-cell responses and superior neutralizing antibody responses against original and variant SARS-CoV-2 compared to conventional spike-encoding mRNA-LNP and purified spike-EABR eVLPs, improving neutralizing titers >10-fold against Omicron-based variants for three months post-boost. Thus, EABR technology enhances potency and breadth of vaccine-induced responses through antigen presentation on cell surfaces and eVLPs, enabling longer-lasting protection against SARS-CoV-2 and other viruses.
Language	English
Publishing date	2022-12-27
Publishing country	United States
Document type	Preprint
DOI	10.1101/2022.12.26.521940
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer

Zhi Yang / Kim-Marie A. Dam / Michael D. Bridges / Magnus A. G. Hoffmann / Andrew T. DeLaitsch / Harry B. Gristick / Amelia Escolano / Rajeev Gautam / Malcolm A. Martin / Michel C. Nussenzweig / Wayne L. Hubbell / Pamela J. Bjorkman

Nature Communications, Vol 13, Iss 1, Pp 1-

2022 Volume 14

Abstract: Neutralizing antibodies (bNAbs) against HIV-1 are exclusively directed against the viral envelope protein (Env) and mainly target Env in a closed, prefusion state. Here, Yang et al. structurally characterize two heterologously-neutralizing CD4-binding ... ...

Abstract	Neutralizing antibodies (bNAbs) against HIV-1 are exclusively directed against the viral envelope protein (Env) and mainly target Env in a closed, prefusion state. Here, Yang et al. structurally characterize two heterologously-neutralizing CD4-binding site (CD4bs) antibodies isolated from sequentially immunized macaques, and show that these antibodies recognize the CD4bs on Env trimers in an „occluded-open‟ conformation between closed, as targeted by bNAbs, and fully-open, as recognized by CD4.
Keywords	Science ; Q
Language	English
Publishing date	2022-02-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: CD4 binding site immunogens elicit heterologous anti-HIV-1 neutralizing antibodies in transgenic and wild-type animals.

Gristick, Harry B / Hartweger, Harald / Loewe, Maximilian / van Schooten, Jelle / Ramos, Victor / Oliveira, Thiago Y / Nishimura, Yoshiaki / Koranda, Nicholas S / Wall, Abigail / Yao, Kai-Hui / Poston, Daniel / Gazumyan, Anna / Wiatr, Marie / Horning, Marcel / Keeffe, Jennifer R / Hoffmann, Magnus A G / Yang, Zhi / Abernathy, Morgan E / Dam, Kim-Marie A /

Gao, Han / Gnanapragasam, Priyanthi N P / Kakutani, Leesa M / Pavlovitch-Bedzyk, Ana Jimena / Seaman, Michael S / Howarth, Mark / McGuire, Andrew T / Stamatatos, Leonidas / Martin, Malcolm A / West, Anthony P / Nussenzweig, Michel C / Bjorkman, Pamela J

Science immunology

2023 Volume 8, Issue 80, Page(s) eade6364

Abstract: Passive transfer of broadly neutralizing anti-HIV-1 antibodies (bNAbs) protects against infection, and therefore, eliciting bNAbs by vaccination is a major goal of HIV-1 vaccine efforts. bNAbs that target the CD4 binding site (CD4bs) on HIV-1 Env are ... ...

Abstract	Passive transfer of broadly neutralizing anti-HIV-1 antibodies (bNAbs) protects against infection, and therefore, eliciting bNAbs by vaccination is a major goal of HIV-1 vaccine efforts. bNAbs that target the CD4 binding site (CD4bs) on HIV-1 Env are among the most broadly active, but to date, responses elicited against this epitope in vaccinated animals have lacked potency and breadth. We hypothesized that CD4bs bNAbs resembling the antibody IOMA might be easier to elicit than other CD4bs antibodies that exhibit higher somatic mutation rates, a difficult-to-achieve mechanism to accommodate Env's N276
MeSH term(s)	Animals ; Rabbits ; Mice ; Animals, Wild/metabolism ; Broadly Neutralizing Antibodies ; Macaca mulatta ; Antibodies, Neutralizing ; HIV Antibodies ; Binding Sites ; CD4 Antigens/metabolism ; Animals, Genetically Modified ; Epitopes ; Cell Adhesion Molecules ; HIV-1 ; Polysaccharides
Chemical Substances	Broadly Neutralizing Antibodies ; Antibodies, Neutralizing ; HIV Antibodies ; CD4 Antigens ; Epitopes ; Cell Adhesion Molecules ; Polysaccharides
Language	English
Publishing date	2023-02-10
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. ; Research Support, N.I.H., Intramural
ISSN	2470-9468
ISSN (online)	2470-9468
DOI	10.1126/sciimmunol.ade6364
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Article ; Online: ESCRT recruitment to mRNA-encoded SARS-CoV-2 spike induces virus-like particles and enhanced antibody responses

Hoffmann, Magnus A. G. / Yang, Zhi / Huey-Tubman, Kathryn E. / Cohen, Alexander A. / Gnanapragasam, Priyanthi N. P. / Nakatomi, Leesa M. / Storm, Kaya N. / Moon, Woohyun J. / Lin, Paulo J.C. / Bjorkman, Pamela J.

bioRxiv

Abstract	Prime-boost regimens for COVID-19 vaccines elicit poor antibody responses against Omicron-based variants and employ frequent boosters to maintain antibody levels. We present a natural infection-mimicking technology that combines features of mRNA- and protein nanoparticle-based vaccines through encoding self-assembling enveloped virus-like particles (eVLPs). eVLP assembly is achieved by inserting an ESCRT- and ALIX-binding region (EABR) into the SARS-CoV-2 spike cytoplasmic tail, which recruits ESCRT proteins to induce eVLP budding from cells. Purified spike-EABR eVLPs presented densely-arrayed spikes and elicited potent antibody responses in mice. Two immunizations with mRNA-LNP encoding spike-EABR elicited potent CD8+ T-cell responses and superior neutralizing antibody responses against original and variant SARS-CoV-2 compared to conventional spike-encoding mRNA-LNP and purified spike-EABR eVLPs, improving neutralizing titers >10-fold against Omicron-based variants for three months post-boost. Thus, EABR technology enhances potency and breadth of vaccine-induced responses through antigen presentation on cell surfaces and eVLPs, enabling longer-lasting protection against SARS-CoV-2 and other viruses.
Keywords	covid19
Language	English
Publishing date	2022-12-27
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2022.12.26.521940
Database	COVID19

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Article ; Online: Nanoparticles presenting clusters of CD4 expose a universal vulnerability of HIV-1 by mimicking target cells.

Hoffmann, Magnus A G / Bar-On, Yotam / Yang, Zhi / Gristick, Harry B / Gnanapragasam, Priyanthi N P / Vielmetter, Jost / Nussenzweig, Michel C / Bjorkman, Pamela J

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

2020 Volume 117, Issue 31, Page(s) 18719–18728

Abstract: CD4-based decoy approaches against HIV-1 are attractive options for long-term viral control, but initial designs, including soluble CD4 (sCD4) and CD4-Ig, were ineffective. To evaluate a therapeutic that more accurately mimics HIV-1 target cells compared ...

Abstract	CD4-based decoy approaches against HIV-1 are attractive options for long-term viral control, but initial designs, including soluble CD4 (sCD4) and CD4-Ig, were ineffective. To evaluate a therapeutic that more accurately mimics HIV-1 target cells compared with monomeric sCD4 and dimeric CD4-Ig, we generated virus-like nanoparticles that present clusters of membrane-associated CD4 (CD4-VLPs) to permit high-avidity binding of trimeric HIV-1 envelope spikes. In neutralization assays, CD4-VLPs were >12,000-fold more potent than sCD4 and CD4-Ig and >100-fold more potent than the broadly neutralizing antibody (bNAb) 3BNC117, with >12,000-fold improvements against strains poorly neutralized by 3BNC117. CD4-VLPs also neutralized patient-derived viral isolates that were resistant to 3BNC117 and other bNAbs. Intraperitoneal injections of CD4-CCR5-VLP produced only subneutralizing plasma concentrations in HIV-1-infected humanized mice but elicited CD4-binding site mutations that reduced viral fitness. All mutant viruses showed reduced sensitivity to sCD4 and CD4-Ig but remained sensitive to neutralization by CD4-VLPs in vitro. In vitro evolution studies demonstrated that CD4-VLPs effectively controlled HIV-1 replication at neutralizing concentrations, and viral escape was not observed. Moreover, CD4-VLPs potently neutralized viral swarms that were completely resistant to CD4-Ig, suggesting that escape pathways that confer resistance against conventional CD4-based inhibitors are ineffective against CD4-VLPs. These findings suggest that therapeutics that mimic HIV-1 target cells could prevent viral escape by exposing a universal vulnerability of HIV-1: the requirement to bind CD4 on a target cell. We propose that therapeutic and delivery strategies that ensure durable bioavailability need to be developed to translate this concept into a clinically feasible functional cure therapy.
MeSH term(s)	Anti-HIV Agents ; CD4 Antigens/chemistry ; CD4 Antigens/metabolism ; Cell Line ; HIV-1/chemistry ; HIV-1/genetics ; HIV-1/metabolism ; Humans ; Molecular Mimicry ; Nanomedicine/methods ; Nanoparticles/chemistry ; Nanoparticles/metabolism ; Virion/chemistry ; Virion/metabolism
Chemical Substances	Anti-HIV Agents ; CD4 Antigens
Language	English
Publishing date	2020-07-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2010320117
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