[ASAP] Bacterial Model Membranes Reshape Fibrillation of a Functional Amyloid Protein
Bacterial Model Membranes Reshape Fibrillation of a Functional Amyloid Protein
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00002/20180402/images/medium/bi-2018-00002f_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00002
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04-03-2018 05:04 AM
Improved Analysis of RNA Localization by SpatiallyRestricted Oxidation of RNA–Protein Complexes
Improved Analysis of RNA Localization by SpatiallyRestricted Oxidation of RNA–Protein Complexes
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00053/20180227/images/medium/bi-2018-00053a_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00053
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02-28-2018 01:42 AM
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion
Publication date: February 2018
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes, Volume 1860, Issue 2</br>
Author(s): Mukesh Mahajan, Deepak Chatterjee, Kannaian Bhuvaneswari, Shubhadra Pillay, Surajit Bhattacharjya</br>
The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV) are serious human health hazard. A...
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11-23-2017 08:38 AM
[NMR paper] NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.
NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion.
Biochim Biophys Acta. 2017 Oct 05;:
Authors: Mahajan M, Chatterjee D, Bhuvaneswari K, Pillay S, Bhattacharjya S
Abstract
The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV)...
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10-11-2017 10:37 AM
[NMR paper] Structural insights of proteins in sub-cellular compartments: in-mitochondria NMR.
Structural insights of proteins in sub-cellular compartments: in-mitochondria NMR.
Related Articles Structural insights of proteins in sub-cellular compartments: in-mitochondria NMR.
Biochim Biophys Acta. 2014 Jun 23;
Authors: Barbieri L, Luchinat E, Banci L
Abstract
Many eukaryotic proteins exert their physiological function in specific cellular compartments. Proteins of the inter-membrane space (IMS) of mitochondria, for example, are synthesized in the cytoplasm and translocate to the IMS, where they are further processed to...
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06-29-2014 02:00 AM
Structural insights of proteins in sub-cellular compartments: in-mitochondria NMR
Structural insights of proteins in sub-cellular compartments: in-mitochondria NMR
Publication date: Available online 23 June 2014
Source:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research</br>
Author(s): Letizia Barbieri , Enrico Luchinat , Lucia Banci</br>
Many eukaryotic proteins exert their physiological function in specific cellular compartments. Proteins of the inter-membrane space (IMS) of mitochondria, for example, are synthesized in the cytoplasm and translocate to the IMS, where they are further processed to their mature form. In-cell Nuclear...
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06-24-2014 03:40 AM
[NMR paper] Quantitative NMR analysis of Erk activity and inhibition by U0126 in a panel of patient-derived colorectal cancer cell lines.
Quantitative NMR analysis of Erk activity and inhibition by U0126 in a panel of patient-derived colorectal cancer cell lines.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Quantitative NMR analysis of Erk activity and inhibition by U0126 in a panel of patient-derived colorectal cancer cell lines.
Biochim Biophys Acta. 2013 Jan 26;
Authors: Rose HM, Stuiver M, Thongwichian R, Theillet FX, Feller SM, Selenko P
Abstract
We comparatively analyzed the basal activity...
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02-03-2013 10:19 AM
[NMR paper] Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and it
Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and its application to elucidate long distance information.
Related Articles Paramagnetic NMR study of Cu(2+)-IDA complex localization on a protein surface and its application to elucidate long distance information.
FEBS Lett. 2004 May 21;566(1-3):157-61
Authors: Nomura M, Kobayashi T, Kohno T, Fujiwara K, Tenno T, Shirakawa M, Ishizaki I, Yamamoto K, Matsuyama T, Mishima M, Kojima C
The paramagnetic metal chelate complex Cu(2+)-iminodiacetic acid (Cu(2+)-IDA) was...