Integrin ?M?2 (Mac-1, CD11b/CD18, CR3) is an important adhesion receptor expressed on monocytes. Mac-1 is responsible for mediating cell migration, phagocytosis, degranulation as well as cell-cell fusion. It is also the most promiscuous integrin in terms of ligand specificity with over 100 ligands, most of which use the ?MI-domain as their binding site. Despite the importance of ?MI-domain in defining ligand interactions of Mac-1, structural studies of ?MI-domain's interactions with ligands are...
[NMR paper] Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant
Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant
Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders associated with the misfolding and aggregation of the human prion protein (huPrP). Despite efforts into investigating the process of huPrP aggregation, the mechanisms triggering its misfolding remain elusive. A number of TSE-associated mutations of huPrP have been identified, but their role at the onset and progression of prion diseases is unclear. Here we report the NMR assignments of...
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[NMR paper] Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
Biomol NMR Assign. 2021 Feb 15;:
Authors: Sanz-Hernández M, De Simone A
Abstract
Transmissible spongiform encephalopathies (TSEs) are fatal...
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02-18-2021 03:17 PM
[NMR paper] ?¹V NMR Crystallography of Vanadium Chloroperoxidase and Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environments of the Active Site.
?¹V NMR Crystallography of Vanadium Chloroperoxidase and Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environments of the Active Site.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles ?¹V NMR Crystallography of Vanadium Chloroperoxidase and Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environments of the Active Site.
J Am Chem Soc. 2015 Apr 29;137(16):5618-28
Authors: Gupta R, Hou G, Renirie R, Wever R, Polenova T
Abstract
...
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03-22-2016 01:46 PM
51V NMRCrystallography of Vanadium Chloroperoxidaseand Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environmentsof the Active Site
51V NMRCrystallography of Vanadium Chloroperoxidaseand Its Directed Evolution P395D/L241V/T343A Mutant: Protonation Environmentsof the Active Site
Rupal Gupta, Guangjin Hou, Rokus Renirie, Ron Wever and Tatyana Polenova
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b02635/20150420/images/medium/ja-2015-02635t_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b02635
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/wtjqPzQxjn0
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[NMR paper] NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and
NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Related Articles NMR characterization of a single-cysteine mutant of Escherichia coli thioredoxin and a covalent thioredoxin-peptide complex.
Eur J Biochem. 1998 Oct 15;257(2):299-308
Authors: Jeng MF, Reymond MT, Tennant LL, Holmgren A, Dyson HJ
The mechanism of disulfide reduction by thioredoxin in the cell is thought to occur through the formation and subsequent destruction of a mixed-disulfide intermediate between...
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11-17-2010 11:15 PM
[NMR paper] Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Eur J Biochem. 1991 Aug 15;200(1):139-48
Authors: Folkers PJ, Stassen AP, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW
Recording of good quality NMR spectra of the single-stranded DNA binding protein gene V of the...
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08-21-2010 11:12 PM
[NMR paper] Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Characterization of wild-type and mutant M13 gene V proteins by means of 1H-NMR.
Eur J Biochem. 1991 Aug 15;200(1):139-48
Authors: Folkers PJ, Stassen AP, van Duynhoven JP, Harmsen BJ, Konings RN, Hilbers CW
Recording of good quality NMR spectra of the single-stranded DNA binding protein gene V of the...