Virus Internalization

"Virus Internalization" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

The entering of cells by viruses following VIRUS ATTACHMENT. This is achieved by ENDOCYTOSIS, by direct MEMBRANE FUSION of the viral membrane with the CELL MEMBRANE, or by translocation of the whole virus across the cell membrane.

Descriptor ID	D053586
MeSH Number(s)	G06.920.881
Concept/Terms	Virus Internalization Virus Internalization Internalization, Virus Virus Entry Entry, Virus Virus Membrane Fusion Virus Membrane Fusion Viral Membrane Fusion Fusion, Viral Membrane Membrane Fusion, Viral

Below are MeSH descriptors whose meaning is more general than "Virus Internalization".

Biological Sciences [G]
Microbiological Phenomena [G06]
Virus Physiological Phenomena [G06.920]
Virus Internalization [G06.920.881]

Below are MeSH descriptors whose meaning is related to "Virus Internalization".

Below are MeSH descriptors whose meaning is more specific than "Virus Internalization".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "Virus Internalization" by people in this website by year, and whether "Virus Internalization" was a major or minor topic of these publications.

Bar chart showing 66 publications over 18 distinct years, with a maximum of 9 publications in 2020

To see the data from this visualization as text, click here.

Year	Major Topic	Minor Topic	Total
2008	5	2	7
2009	3	0	3
2010	1	1	2
2011	2	0	2
2012	2	4	6
2013	4	2	6
2014	0	3	3
2015	4	2	6
2016	3	1	4
2017	0	1	1
2018	1	1	2
2019	3	0	3
2020	5	4	9
2021	0	2	2
2022	2	3	5
2023	0	1	1
2024	1	2	3
2025	1	0	1

Below are the most recent publications written about "Virus Internalization" by people in Profiles.

Durham ND, Jain A, Howard A, Luban J, Munro JB. Molecular basis for the increased fusion activity of the Ebola virus glycoprotein epidemic variant A82V: Insights from simulations and experiments. Cell Rep. 2025 Apr 22; 44(4):115521.

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Dey S, Pahari P, Mukherjee S, Munro JB, Das DK. Conformational dynamics of SARS-CoV-2 Omicron spike trimers during fusion activation at single molecule resolution. Structure. 2024 11 07; 32(11):1910-1925.e6.

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D?az-Salinas MA, Jain A, Durham ND, Munro JB. Single-molecule imaging reveals allosteric stimulation of SARS-CoV-2 spike receptor binding domain by host sialic acid. Sci Adv. 2024 07 19; 10(29):eadk4920.

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Kushwaha N, Dwivedi A, Tiwari S, Mishra P, Verma SK. Comprehensive analytics for virus-cell and cell-cell multinucleation system. Biochem Biophys Res Commun. 2024 09 24; 726:150281.

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Vaknin A, Grossman A, Durham ND, Lupovitz I, Goren S, Golani G, Roichman Y, Munro JB, Sorkin R. Ebola Virus Glycoprotein Strongly Binds to Membranes in the Absence of Receptor Engagement. ACS Infect Dis. 2024 05 10; 10(5):1590-1601.

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Jain A, Govindan R, Berkman AR, Luban J, D?az-Salinas MA, Durham ND, Munro JB. Regulation of Ebola GP conformation and membrane binding by the chemical environment of the late endosome. PLoS Pathog. 2023 Dec; 19(12):e1011848.

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Suvarnapathaki S, Chauhan D, Nguyen A, Ramalingam M, Camci-Unal G. Advances in Targeting ACE2 for Developing COVID-19 Therapeutics. Ann Biomed Eng. 2022 Dec; 50(12):1734-1749.

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Willett BJ, Grove J, MacLean OA, Wilkie C, De Lorenzo G, Furnon W, Cantoni D, Scott S, Logan N, Ashraf S, Manali M, Szemiel A, Cowton V, Vink E, Harvey WT, Davis C, Asamaphan P, Smollett K, Tong L, Orton R, Hughes J, Holland P, Silva V, Pascall DJ, Puxty K, da Silva Filipe A, Yebra G, Shaaban S, Holden MTG, Pinto RM, Gunson R, Templeton K, Murcia PR, Patel AH, Klenerman P, Dunachie S, Haughney J, Robertson DL, Palmarini M, Ray S, Thomson EC. SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway. Nat Microbiol. 2022 08; 7(8):1161-1179.

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Favre D, Harmon JF, Zhang A, Miller MS, Kaltashov IA. Decavanadate interactions with the elements of the SARS-CoV-2 spike protein highlight the potential role of electrostatics in disrupting the infectivity cycle. J Inorg Biochem. 2022 09; 234:111899.

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Ren W, Ju X, Gong M, Lan J, Yu Y, Long Q, Kenney DJ, O'Connell AK, Zhang Y, Zhong J, Zhong G, Douam F, Wang X, Huang A, Zhang R, Ding Q. Characterization of SARS-CoV-2 Variants B.1.617.1 (Kappa), B.1.617.2 (Delta), and B.1.618 by Cell Entry and Immune Evasion. mBio. 2022 04 26; 13(2):e0009922.

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