Zobrazeno 1 - 10
of 363
pro vyhledávání: ''
Autor:
Pamela A. Naulin, Jorge E. Contreras, Nelson P. Barrera, Christian Fuentes, Benjamin Lozano, Yu Liu, Carla Schmidt
Publikováno v:
The Journal of Biological Chemistry
The Journal of biological chemistry, vol 295, iss 49
The Journal of biological chemistry, vol 295, iss 49
Connexin (Cx) protein forms hemichannels and gap junctional channels, which play diverse and profound roles in human physiology and diseases. Gap junctions are arrays of intercellular channels formed by the docking of two hemichannels from adjacent c
Publikováno v:
The Journal of Biological Chemistry
A central role for the influenza matrix protein 1 (M1) is to form a polymeric coat on the inner leaflet of the host membrane that ultimately provides shape and stability to the virion. M1 polymerizes upon binding membranes, but triggers for conversio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f2511df3f85af9fd3f946220a7f2382
https://doi.org/10.1016/j.jbc.2021.100316
https://doi.org/10.1016/j.jbc.2021.100316
Publikováno v:
The Journal of Biological Chemistry
Post-translationally modified tau is the primary component of tau neurofibrillary tangles, a pathological hallmark of Alzheimer's disease and other tauopathies. Post-translational modifications (PTMs) within the tau microtubule (MT)-binding domain (M
Publikováno v:
The Journal of Biological Chemistry
The two-pore channels (TPCs) are voltage-gated cation channels consisting of single polypeptides with two repeats of a canonical 6-transmembrane unit. TPCs are known to be regulated by various physiological signals such as membrane voltage and phosph
Publikováno v:
The Journal of Biological Chemistry
How and when disulfides form in proteins during their folding is a fundamental question in cell biology. Two models describe the relationship between disulfide formation and folding, the folded precursor model, in which formation of nascent structure
Autor:
John David Parkin, Elisavet Makou, Richard G. Bailey, Georg Hähner, Heather J. Johnston, Paul N. Barlow, Alison N. Hulme
Publikováno v:
The Journal of Biological Chemistry
Makou, E, Bailey, R G, Johnston, H, Parkin, J D, Hulme, A N, Hähner, G & Barlow, P N 2019, ' Combining SPR with atomic-force microscopy enables single-molecule insights into activation and suppression of the complement cascade ', Journal of Biological Chemistry, vol. 294, no. 52, pp. 20148-20163 . https://doi.org/10.1074/jbc.RA119.010913
Makou, E, Bailey, R G, Johnston, H, Parkin, J D, Hulme, A N, Hähner, G & Barlow, P N 2019, ' Combining SPR with atomic-force microscopy enables single-molecule insights into activation and suppression of the complement cascade ', Journal of Biological Chemistry, vol. 294, no. 52, pp. 20148-20163 . https://doi.org/10.1074/jbc.RA119.010913
This work was supported by Leverhulme Trust Grant RPG-2015-109. Activation and suppression of the complement system compete on every serum-exposed surface, host or foreign. Potentially harmful outcomes of this competition depend on surface molecules
Autor:
Christopher L.-H. Huang, Antony P. Jackson, Jonathan R. Silva, Zaki F. Habib, Samantha C. Salvage, Wandi Zhu, Jennifer R. Irons, Soyon S. Hwang
Publikováno v:
The Journal of Biological Chemistry
The auxiliary β3-subunit is an important functional regulator of the cardiac sodium channel Nav1.5, and some β3 mutations predispose individuals to cardiac arrhythmias. The β3-subunit uses its transmembrane α-helix and extracellular domain to bin
Publikováno v:
The Journal of Biological Chemistry
Huntington's disease (HD) is a neurodegenerative disorder caused by a poly-CAG expansion in the first exon of the HTT gene, resulting in an extended poly-glutamine tract in the N-terminal domain of the Huntingtin (Htt) protein product. Proteolytic fr
Autor:
Nicolas Doucet, Marianne Rooman, Gabriel Begin, Marlène Fortier, David Chatenet, Yves St-Pierre, Charles Calmettes, Myriam Létourneau, Fabrizio Pucci, Patrick Lagüe, N. T. Hang Pham, M. Sameer Al-Abdul-Wahid, Benjamin Folch
Publikováno v:
The Journal of Biological Chemistry
The design of allosteric modulators to control protein function is a key objective in drug discovery programs. Altering functionally essential allosteric residue networks provides unique protein family subtype specificity, minimizes unwanted off-targ
Publikováno v:
The Journal of Biological Chemistry
The Journal of biological chemistry, vol 297, iss 5
The Journal of biological chemistry, vol 297, iss 5
Human apoptosis-linked gene-2 interacting protein X (ALIX), a versatile adapter protein, regulates essential cellular processes by shuttling between late endosomal membranes and the cytosol, determined by its interactions with Src kinase. Here, we in