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Label-Free and Direct Visualization of Multivalent Binding of Bone Morphogenetic Protein-2 with Cartilage Oligomeric Matrix Protein

Autor: Eric O. Klineberg, Michael C. Fong, Weiliang Cai, Gang-yu Liu, Victoria Tran, Árpád Karsai, Jasper H.N. Yik, Dominik R. Haudenschild

Publikováno v: J Phys Chem B
The journal of physical chemistry. B, vol 123, iss 1
Tran, V; Karsai, A; Fong, MC; Cai, W; Yik, JHN; Klineberg, E; et al.(2019). Label-Free and Direct Visualization of Multivalent Binding of Bone Morphogenetic Protein-2 with Cartilage Oligomeric Matrix Protein. Journal of Physical Chemistry B, 123(1), 39-46. doi: 10.1021/acs.jpcb.8b08564. UC Davis: Retrieved from: http://www.escholarship.org/uc/item/9cm010zc

© 2018 American Chemical Society. This work presents the first direct evidence of multivalent binding between bone morphogenetic protein-2 (BMP-2) and cartilage oligomeric matrix protein (COMP) using high-resolution atomic force microscopy (AFM) ima

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a4c3dc93266b38d8796da99ae441934
https://doi.org/10.1021/acs.jpcb.8b08564

A pentameric protein ring with novel architecture is required for herpesviral packaging

Autor: Lisa M Strong, Stephanie N. Gates, Britt A. Glaunsinger, Allison L. Didychuk, Matthew R Gardner, Andreas Martin

Publikováno v: eLife
eLife, Vol 10 (2021)

Genome packaging in large double-stranded DNA viruses requires a powerful molecular motor to force the viral genome into nascent capsids. This process appears mechanistically similar in two evolutionarily distant viruses, the herpesviruses and the ta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c3bb19cd956024e837eda7a36e49dc6
http://europepmc.org/articles/PMC7889075

Lipid-anchor display on peptoid nanosheets via co-assembly for multivalent pathogen recognition

Autor: Ryan K. Spencer, Ronald N. Zuckermann, Lisa Yun, Jae Hong Kim, Elissa M. Grzincic, Mark Kline

Publikováno v: Soft matter. 16(4)

Biological systems have evolved sophisticated molecular assemblies capable of exquisite molecular recognition across length scales ranging from angstroms to microns. For instance, the self-organization of glycolipids and glycoproteins on cell membran

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6831815b11a9e5deb1d730a38d6e830e
https://pubmed.ncbi.nlm.nih.gov/31854427

Flexible Connectors between Capsomer Subunits that Regulate Capsid Assembly

Autor: Mary L. Hasek, Joshua B. Maurer, Roger W. Hendrix, Robert L. Duda

Publikováno v: Journal of Molecular Biology. 429:2474-2489

Viruses build icosahedral capsids of specific size and shape by regulating the spatial arrangement of the hexameric and pentameric protein capsomers in the growing shell during assembly. In the T = 7 capsids of Escherichia coli bacteriophage HK97 and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b5fb035f09761ebd6a048bf10164a79
https://doi.org/10.1016/j.jmb.2017.07.002