Collagen’s primary structure determines collagen:HSP47 complex stoichiometry

Autor: Philipp W. N. Schmid, Matthias Mörgelin, Jan M. Gebauer, Sinan Oecal, Ulrich Baumann, Johannes Buchner, Elena Theres Abraham

Publikováno v: The Journal of Biological Chemistry
'Journal of Biological Chemistry ', vol: 297, pages: 101169-1-101169-13 (2021)

Collagens play important roles in development and homeostasis in most higher organisms. In order to function, collagens require the specific chaperone HSP47 for proper folding and secretion. HSP47 is known to bind to the collagen triple-helix but the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69eb51ebe4691e018f5c02f8682f1e26
http://europepmc.org/articles/PMC8626583

Solution structures of human myeloma IgG3 antibody reveal extended Fab and Fc regions relative to the other IgG subclasses

Autor: James Doutch, Margaret Goodall, Stephen J. Perkins, Jayesh Gor, Robert P. Rambo, Valentina A. Spiteri

Publikováno v: The Journal of Biological Chemistry

Human immunoglobulin G subclass 3 (IgG3) possesses a uniquely long hinge region that separates its Fab antigen-binding and Fc receptor-binding regions. Owing to this hinge length, the molecular structure of full-length IgG3 remains elusive, and the r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1923da25ff4b9292e3226b329080bc5
https://pubmed.ncbi.nlm.nih.gov/34302810

Structural characterization of HIV-1 matrix mutants implicated in envelope incorporation

Autor: Ruba H. Ghanam, Gunnar N. Eastep, Jamil S. Saad, Todd Green

Publikováno v: The Journal of Biological Chemistry

During the late phase of HIV-1 infection, viral Gag polyproteins are targeted to the plasma membrane (PM) for assembly. Gag localization at the PM is a prerequisite for the incorporation of the envelope protein (Env) into budding particles. Gag assem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12dc23cc6d0b48d19655e15d1a020016
http://europepmc.org/articles/PMC7952133

The molecular basis for apolipoprotein E4 as the major risk factor for late onset Alzheimer's disease

Autor: John R. Atack, Wei-Feng Xue, Louise C. Serpell, Ana Caroline Raulin, Youssra K. Al-Hilaly, John McGeehan, Lucas Kraft

Publikováno v: Journal of Molecular Biology
Raulin, A-C, Kraft, L, Al-Hilaly, Y, Xue, W-F, McGeehan, J, Atack, J & Serpell, L C 2019, ' The molecular basis for Apolipoprotein E4 as the major risk factor for late onset Alzheimer's disease ', Journal of Molecular Biology, vol. 431, no. 12, pp. 2248-2265 . https://doi.org/10.1016/j.jmb.2019.04.019

Apolipoprotein E4 (ApoE4) is one of three (E2, E3 and E4) human isoforms of an α-helical, 299-amino-acid protein. Homozygosity for the ε4 allele is the major genetic risk factor for developing late-onset Alzheimer's disease (AD). ApoE2, ApoE3 and A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05a9d6a9f7dcb0650d86ec70dd141851
http://sro.sussex.ac.uk/id/eprint/83616/7/1-s2.0-S0022283619302268-main.pdf

Active site metals mediate an oligomeric equilibrium in Plasmodium M17 aminopeptidases

Autor: Hariprasad Venugopal, Sarah C. Atkinson, Matthew J. Belousoff, Sheena McGowan, Nyssa Drinkwater, Natalie A. Borg, Tess R. Malcolm

Publikováno v: The Journal of Biological Chemistry

M17 leucyl aminopeptidases are metal-dependent exopeptidases that rely on oligomerization to diversify their functional roles. The M17 aminopeptidases from Plasmodium falciparum (PfA-M17) and Plasmodium vivax (Pv-M17) function as catalytically active

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d502046e408696b428e9ed5010d0d4a
https://doi.org/10.1074/jbc.ra120.016313