[ASAP] Protein Polymerization as a Novel Targeted Protein Degradation Mechanism
Protein Polymerization as a Novel Targeted Protein Degradation Mechanism
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00163/20210324/images/medium/bi1c00163_0002.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00163
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03-24-2021 11:20 PM
[ASAP] Staphylococcus aureus Glucose-Induced Biofilm Accessory Protein A (GbaA) Is a Monothiol-Dependent Electrophile Sensor
Staphylococcus aureus Glucose-Induced Biofilm Accessory Protein A (GbaA) Is a Monothiol-Dependent Electrophile Sensor
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00347/20200729/images/medium/bi0c00347_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00347
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07-30-2020 05:28 PM
[ASAP] Cd(II)- and Pb(II)-Induced Self-Assembly of Peripheral Membrane Domains from Protein Kinase C
Cd(II)- and Pb(II)-Induced Self-Assembly of Peripheral Membrane Domains from Protein Kinase C
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b01235/20181228/images/medium/bi-2018-01235k_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b01235
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01-07-2019 05:49 AM
[ASAP] The Role of Ionic Liquid Breakdown in the Electrochemical Metallization of VO2: An NMR Study of Gating Mechanisms and VO2 Reduction
The Role of Ionic Liquid Breakdown in the Electrochemical Metallization of VO2: An NMR Study of Gating Mechanisms and VO2 Reduction
Michael A. Hope, Kent J. Griffith, Bin Cui, Fang Gao, Siān E. Dutton, Stuart S. P. Parkin, Clare P. Grey
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b09513/20181121/images/medium/ja-2018-095138_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b09513
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http://feeds.feedburner.com/~r/acs/jacsat/~4/vBauA7yiw7s
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11-25-2018 06:02 AM
[NMR paper] Structural mechanisms for the S-nitrosylation-derived protection of mouse galectin-2 from oxidation-induced inactivation revealed by NMR.
Structural mechanisms for the S-nitrosylation-derived protection of mouse galectin-2 from oxidation-induced inactivation revealed by NMR.
Structural mechanisms for the S-nitrosylation-derived protection of mouse galectin-2 from oxidation-induced inactivation revealed by NMR.
FEBS J. 2018 Feb 02;:
Authors: Sakakura M, Tamura M, Fujii N, Takeuchi T, Hatanaka T, Kishimoto S, Arata Y, Takahashi H
Abstract
Galectin-2 (Gal-2) is a lectin thought to play protective roles in the gastrointestinal tract. Oxidation of mouse Gal-2 (mGal-2)...
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Protein revealed as glue that holds biomolecules within the nucleolus - Phys.Org
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Protein revealed as glue that holds biomolecules within the nucleolus
Phys.Org
Researchers have determined that the protein nucleophosmin (NPM1) serves as glue that holds proteins and RNA together in the nucleolus and showed how NPM1's structure makes it ideal for the job. St. Jude Children's Research Hospital scientists led the ...
Scientists Reveal Protein That Works as Glue Holding Together Biomolecules Within NucleolusScicasts (press release) (blog)
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Protein revealed as glue that holds biomolecules within the nucleolus...
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03-01-2016 05:59 PM
[NMR paper] Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.
Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Mechanisms of peptide-induced pore formation in lipid bilayers investigated by oriented 31P solid-state NMR spectroscopy.
PLoS One. 2012;7(10):e47745
Authors: Bertelsen K,...
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[NMR paper] Solid-state NMR analysis of crosslinking in mussel protein glue.
Solid-state NMR analysis of crosslinking in mussel protein glue.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solid-state NMR analysis of crosslinking in mussel protein glue.
Arch Biochem Biophys. 1993 Apr;302(1):255-8
Authors: Holl SM, Hansen D, Waite JH, Schaefer J
Solid-state 13C and 15N NMR spectra have been obtained of intact adhesive plaques from the mussel Geukensia demissa labeled by L-lysine. The plaques are rich in a polyphenolic protein glue which has 50...