Reference health
In situ structure of virus capsids within cell nuclei by correlative light and cryo-electron tomography
47/47 checkable references clean · checked 2026-07-23
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
3 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 47 checked references that resolve
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Electron microscopy after rapid freezing on a metal surface and substitution fixation
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Paramyxovirus Ultrastructure and Genome Packaging: Cryo-Electron Tomography of Sendai Virus
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Cryotomography of Budding Influenza A Virus Reveals Filaments with Diverse Morphologies that Mostly Do Not Bear a Genome at Their Distal End
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resolves10.1038/nmeth1014
Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy
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Correlative light and electron microscopy methods for the study of virus–cell interactions
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Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus
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Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes
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Labeling and Localization of the Herpes Simplex Virus Capsid Protein UL25 and Its Interaction with the Two Triplexes Closest to the Penton
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The Large Tegument Protein pUL36 Is Essential for Formation of the Capsid Vertex-Specific Component at the Capsid-Tegument Interface of Herpes Simplex Virus 1
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Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids
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Analysis of the Early Steps of Herpes Simplex Virus 1 Capsid Tegumentation
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Differing Roles of Inner Tegument Proteins pUL36 and pUL37 during Entry of Herpes Simplex Virus Type 1
resolves10.1016/j.virol.2014.02.003
The interaction of the HSV-1 tegument proteins pUL36 and pUL37 is essential for secondary envelopment during viral egress
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A Null Mutation in the UL36 Gene of Herpes Simplex Virus Type 1 Results in Accumulation of Unenveloped DNA-Filled Capsids in the Cytoplasm of Infected Cells
resolves10.1016/j.jviromet.2019.113792
A new inactivation method to facilitate cryo-EM of enveloped, RNA viruses requiring high containment: A case study using Venezuelan Equine Encephalitis Virus (VEEV)
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GraFix: Stabilization of Fragile Macromolecular Complexes for Single Particle Cryo-EM
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Near-atomic structure of Japanese encephalitis virus reveals critical determinants of virulence and stability
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Visualization of Tegument-Capsid Interactions and DNA in Intact Herpes Simplex Virus Type 1 Virions
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The UL36 Tegument Protein of Herpes Simplex Virus 1 Has a Composite Binding Site at the Capsid Vertices
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Residues of the UL25 Protein of Herpes Simplex Virus That Are Required for Its Stable Interaction with Capsids
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The Herpes Simplex Virus 1 UL17 Protein Is the Second Constituent of the Capsid Vertex-Specific Component Required for DNA Packaging and Retention
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Nuclear Egress of Pseudorabies Virus Capsids Is Enhanced by a Subspecies of the Large Tegument Protein That Is Lost upon Cytoplasmic Maturation
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The C Terminus of the Large Tegument Protein pUL36 Contains Multiple Capsid Binding Sites That Function Differently during Assembly and Cell Entry of Herpes Simplex Virus
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The 3 references without a DOI — listed, not checked
no DOI — not checkedMielańczyk, L., Matysiak, N., Klymenko, O. & Wojnicz, R. in Transmission Electron Microscope. (ed. M. Khan) (Intechopen-Web of Science, London, 2015).
no DOI — not checkedWhitley, R.J. in Fields’ Virology, Vol. 2. (eds. D.M. Knipe & P.M. Howley) 2461–2509 (Lippincott Williams & Wilkins, Philadelphia; 2001).
no DOI — not checkedRoizman, B., Knipe, D.M. & Whitley, R.J. in Fields Virology, Vol. 2, Edn. 6. (eds. D.M. Knipe et al.) 1824–1897 (Lippincott Williams & Wilkins, Philadelphia; 2013).
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