Open Access Helper

OpenAlex Citation Counts

OpenAlex Citations Logo

OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

NeutrobodyPlex—monitoring SARS‐CoV‐2 neutralizing immune responses using nanobodies
Teresa R. Wagner, E. Ostertag, Philipp D. Kaiser, et al.
EMBO Reports (2021) Vol. 22, Iss. 5
Open Access | Times Cited: 58

Showing 26-50 of 58 citing articles:

Nanobodies: COVID-19 and Future Perspectives
G Valenzuela, Zaray Miranda-Chacón, Constanza Salinas-Rebolledo, et al.
Frontiers in Drug Discovery (2022) Vol. 2
Open Access | Times Cited: 13
A Novel PNGase Rc for Improved Protein N-Deglycosylation in Bioanalytics and Hydrogen–Deuterium Exchange Coupled With Mass Spectrometry Epitope Mapping under Challenging Conditions
Marius Gramlich, Sandra Maier, Philipp D. Kaiser, et al.
Analytical Chemistry (2022) Vol. 94, Iss. 27, pp. 9863-9871
Closed Access | Times Cited: 12
Exploring the ability of the MD+FoldX method to predict SARS-CoV-2 antibody escape mutations using large-scale data
L. América, Jonathan E. Barnes, Jagdish Suresh Patel, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 2
Structural Characterization of a Neutralizing Nanobody With Broad Activity Against SARS-CoV-2 Variants
Tingting Li, Bingjie Zhou, Zhipu Luo, et al.
Frontiers in Microbiology (2022) Vol. 13
Open Access | Times Cited: 11
Poly(methyl methacrylate)-Based Nanofluidic Device for Rapid and Multiplexed Serological Antibody Detection of SARS-CoV-2
Thomas Mortelmans, Dimitrios Kazazis, Celestino Padeste, et al.
ACS Applied Nano Materials (2022) Vol. 5, Iss. 1, pp. 517-526
Closed Access | Times Cited: 10
Comparison of the Anti-SARS-CoV-2 Surrogate Neutralization Assays by TECOmedical and DiaPROPH-Med with Samples from Vaccinated and Infected Individuals
Lennart Münsterkötter, Moritz M. Hollstein, Andreas Hahn, et al.
Viruses (2022) Vol. 14, Iss. 2, pp. 315-315
Open Access | Times Cited: 10
Applications of nanobodies in the prevention, detection, and treatment of the evolving SARS-CoV-2
Wenyi Wang, Yue Hu, Bohan Li, et al.
Biochemical Pharmacology (2022) Vol. 208, pp. 115401-115401
Open Access | Times Cited: 10
“Nanobody-based immunodiagnostics: A systematic review of nanobody integration in diagnostics and deep insight into electrochemical immunoassays”
Mohammad IA. Ahmad, Célia G. Amorim, Luay F. Abu Qatouseh, et al.
Microchemical Journal (2023) Vol. 196, pp. 109628-109628
Closed Access | Times Cited: 5
SARS-CoV-2 Delta Variant Decreases Nanobody Binding and ACE2 Blocking Effectivity
Mert Gölcük, Aysima Hacisuleyman, Sema Zeynep Yilmaz, et al.
Journal of Chemical Information and Modeling (2022) Vol. 62, Iss. 10, pp. 2490-2498
Open Access | Times Cited: 9
Biparatopic nanobodies targeting the receptor binding domain efficiently neutralize SARS-CoV-2
Phillip Pymm, Samuel J. Redmond, Olan Dolezal, et al.
iScience (2022) Vol. 25, Iss. 11, pp. 105259-105259
Open Access | Times Cited: 9
A Nanobody-Based Toolset to Monitor and Modify the Mitochondrial GTPase Miro1
Funmilayo O. Fagbadebo, Philipp D. Kaiser, Katharina Zittlau, et al.
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 8
Targeting Spike Protein: Modified Antibody for Broad-Spectrum Binding to Coronaviruses: An In Silico Study
Rai RC
Virology & Immunology Journal (2023) Vol. 7, Iss. 3, pp. 1-15
Open Access | Times Cited: 4
A Naïve Phage Display Library-Derived Nanobody Neutralizes SARS-CoV-2 and Three Variants of Concern
Dandan Wu, Junxiao Cong, Jiali Wei, et al.
International Journal of Nanomedicine (2023) Vol. Volume 18, pp. 5781-5795
Open Access | Times Cited: 4
Biparatopic sybody constructs neutralize SARS-CoV-2 variants of concern and mitigate emergence of drug resistance
Justin D. Walter, Cedric A. J. Hutter, Alisa A. Garaeva, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2020)
Open Access | Times Cited: 11
Exploring the ability of the MD+FoldX method to predict SARS-CoV-2 antibody escape mutations using large-scale data
L. América, Jonathan E. Barnes, Jagdish Suresh Patel, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Making the effect visible – OX40 targeting nanobodies for in vivo imaging of activated T cells
Desiree I. Frecot, Simone Blaess, Teresa R. Wagner, et al.
Frontiers in Immunology (2024) Vol. 15
Open Access | Times Cited: 1
Nanobodies in the limelight: Multifunctional tools in the fight against viruses
Ainhoa Moliner Morro, Gerald M. McInerney, Leo Hanke
Journal of General Virology (2022) Vol. 103, Iss. 5
Closed Access | Times Cited: 4
Nanobody Technology and New Molecular Biology Methods to Advance Rapid Diagnostic Test for Neglected Tropical Diseases
Andrés Álvarez-Rodríguez, Magdalena Radwanska, Stefan Magez, et al.
IntechOpen eBooks (2023)
Open Access | Times Cited: 2
Rapid Antigen Testing
Laura Anfossi, Amira Chahinez, Ferdous Dahmani, et al.
IntechOpen eBooks (2023)
Open Access | Times Cited: 1
Characterization of a novel format scFv×VHH single‐chain biparatopic antibody against metal binding protein MtsA
R Asano, Miyu Takeuchi, Makoto Nakakido, et al.
Protein Science (2024) Vol. 33, Iss. 6
Open Access
Nanobodies as novel tools to monitor the mitochondrial fission factor Drp1
Theresa Froehlich, Andreas Jenner, Claudia Cavarischia-Rega, et al.
Life Science Alliance (2024) Vol. 7, Iss. 8, pp. e202402608-e202402608
Open Access
Making the effect visible – OX40 targeting nanobodies forin vivoimaging of activated T cells
Desiree I. Frecot, Simone Blaess, Teresa R. Wagner, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Super-immunity by broadly protective nanobodies to sarbecoviruses
Yufei Xiang, Wei Huang, Hejun Liu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2021)
Open Access | Times Cited: 3
SARS-Cov-2 Delta Variant Decreases Nanobody Binding and ACE2 Blocking Effectivity
Mert Gölcük, Aysima Hacisuleyman, Sema Zeynep Yilmaz, et al.
(2021)
Open Access | Times Cited: 2
Hetero-bivalent Nanobodies Provide Broad-spectrum Protection against SARS-CoV-2 Variants of Concern including Omicron
Huan Ma, Xinghai Zhang, Peiyi Zheng, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access | Times Cited: 1

Scroll to top