Exploring the sequence context of phosphorylatable amino acids: the contribution of the upgraded MAPRes tool. (Q45922474)

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scientific article published in March 2015

Language	Label	Description	Also known as
English	Exploring the sequence context of phosphorylatable amino acids: the contribution of the upgraded MAPRes tool.	scientific article published in March 2015

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

Exploring the sequence context of phosphorylatable amino acids: the contribution of the upgraded MAPRes tool. (English)

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

author name string

Zeeshan Iqbal

1

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

Daniel C Hoessli

2

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

Wajahat M Qazi

3

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

Munir Ahmad

4

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

Abdul Rauf Shakoori

5

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

Nasir-ud-Din

6

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

publication date

1 March 2015

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

Journal of Cellular Biochemistry

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

116

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

3

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

370-379

1 reference

Europe PubMed Central

PubMed publication ID

17 December 2017

http://europepmc.org/abstract/MED/25258092

MAPRes: an efficient method to analyze protein sequence around post-translational modification sites.

1 reference

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Phosphoproteome sequence analysis and significance: mining association patterns around phosphorylation sites utilizing MAPRes

1 reference

https://api.crossref.org/works/10.1002%2FJCB.24983

21 January 2018

MAPRes: Mining association patterns among preferred amino acid residues in the vicinity of amino acids targeted for post-translational modifications

1 reference

https://api.crossref.org/works/10.1002%2FJCB.24983

21 January 2018

Protein structure prediction and structural genomics

1 reference

https://api.crossref.org/works/10.1002%2FJCB.24983

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A probability-based approach for high-throughput protein phosphorylation analysis and site localization

1 reference

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21 January 2018

Sequence and structure-based prediction of eukaryotic protein phosphorylation sites

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Phospho.ELM: a database of phosphorylation sites--update 2011

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The relationship between protein structure and function: a comprehensive survey with application to the yeast genome

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Identification of phosphorylation sites in protein kinase A substrates using artificial neural networks and mass spectrometry

1 reference

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The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: from respiration to apoptosis

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The importance of intrinsic disorder for protein phosphorylation

1 reference

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NetPhosYeast: prediction of protein phosphorylation sites in yeast.

1 reference

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Influence of the sequence environment and properties of neighboring amino acids on amino-acetylation: relevance for structure-function analysis

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Moonlighting proteins.

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Charge environments around phosphorylation sites in proteins

1 reference

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Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter

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NetPhosBac - a predictor for Ser/Thr phosphorylation sites in bacterial proteins.

1 reference

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21 January 2018

CATH--a hierarchic classification of protein domain structures

1 reference

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21 January 2018

Chemical approaches to understanding O-GlcNAc glycosylation in the brain

1 reference

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21 January 2018

Proteomic analysis of human blood serum using peptide library beads

1 reference

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21 January 2018

Dynamic interplay between O-GlcNAc and O-phosphate: the sweet side of protein regulation

1 reference

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21 January 2018

SH3 domain tyrosine phosphorylation--sites, role and evolution.

1 reference

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21 January 2018

A motif-based profile scanning approach for genome-wide prediction of signaling pathways

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21 January 2018

Functional importance of polar and charged amino acid residues in transmembrane helix 14 of multidrug resistance protein 1 (MRP1/ABCC1): identification of an aspartate residue critical for conversion from a high to low affinity substrate binding sta

1 reference

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21 January 2018

Exceptional disfavor for proline at the P + 1 position among AGC and CAMK kinases establishes reciprocal specificity between them and the proline-directed kinases.

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21 January 2018

Capillary HPLC: A Method for Protein Isolation and Peptide Mapping

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Global Assessment of Regulation of Phosphorylation of Insulin Receptor Substrate-1 by Insulin In Vivo in Human Muscle

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21 January 2018

Identifiers

10.1002/JCB.24983

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