PyTMs: a useful PyMOL plugin for modeling common post-translational modifications. - Wikidata - wikimedia - TriplyDB

PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

http://www.wikidata.org/entity/Q35457946

about

Post-Translational Modifications of Cardiac Mitochondrial Proteins in Cardiovascular Disease: Not Lost in Translation Histone H3 Ser57 and Thr58 phosphorylation in the brain of 5XFAD mice.Structural insights into the recognition of phosphorylated FUNDC1 by LC3B in mitophagy.Phosphorylation of the phytosulfokine peptide receptor PSKR1 controls receptor activity.Proteomic analysis reveals diverse proline hydroxylation-mediated oxygen-sensing cellular pathways in cancer cells.Scavenger Receptor A Mediates the Clearance and Immunological Screening of MDA-Modified Antigen by M2-Type Macrophages.SIRT2 regulates oxidative stress-induced cell death through deacetylation of c-Jun NH2-terminal kinase.SIRT2 deacetylase regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation.

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P2860

PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

http://www.wikidata.org/entity/Q35457946

description

2014 nî lūn-bûn

@nan

2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

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PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

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PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

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PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

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PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

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PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

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PyTMs: a useful PyMOL plugin for modeling common post-translational modifications.

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Robert A Harris

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P2860

HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

Regulation of cellular metabolism by protein lysine acetylation

Electrostatics of nanosystems: application to microtubules and the ribosome

PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse

Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of MBP complexed with I-Au

Structural basis for modulation and agonist specificity of HCN pacemaker channels

A molecular basis for the association of the HLA-DRB1 locus, citrullination, and rheumatoid arthritis

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Hybrid malondialdehyde and acetaldehyde protein adducts form in the lungs of mice exposed to alcohol and cigarette smoke

The innate immune response to products of phospholipid peroxidation

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s12859-014-0370-6

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15

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Tatyana Sandalova

Andreas Warnecke

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