(Q24295612)

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The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6

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The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6 (English)

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Riccardo Sgarra

1

object named as

Riccardo Sgarra

author given names

Riccardo

author last names

Sgarra

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PubMed publication ID

30 October 2023

author name string

Jaeho Lee

2

author given names

Jaeho

author last names

Lee

1 reference

PubMed publication ID

30 October 2023

Michela A Tessari

3

author given names

Michela A

author last names

Tessari

1 reference

PubMed publication ID

30 October 2023

Sandro Altamura

4

author given names

Sandro

author last names

Altamura

1 reference

PubMed publication ID

30 October 2023

Barbara Spolaore

5

author given names

Barbara

author last names

Spolaore

1 reference

PubMed publication ID

30 October 2023

Vincenzo Giancotti

6

author given names

Vincenzo

author last names

Giancotti

1 reference

PubMed publication ID

30 October 2023

Mark T Bedford

7

author given names

Mark T

author last names

Bedford

1 reference

PubMed publication ID

30 October 2023

Guidalberto Manfioletti

8

author given names

Guidalberto

author last names

Manfioletti

1 reference

PubMed publication ID

30 October 2023

language of work or name

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publication date

17 February 2006

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Journal of Biological Chemistry

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281

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7

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3764-72

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Nerve growth factor-mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1

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Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)

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Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a

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Histones and histone modifications

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Arginine methylation an emerging regulator of protein function

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Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides

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Differential in vivo modifications of the HMGI(Y) nonhistone chromatin proteins modulate nucleosome and DNA interactions

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Methylation of histone H3 by coactivator-associated arginine methyltransferase 1

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During apoptosis of tumor cells HMGA1a protein undergoes methylation: identification of the modification site by mass spectrometry

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Tandem mass spectrometry for the examination of the posttranslational modifications of high-mobility group A1 proteins: symmetric and asymmetric dimethylation of Arg25 in HMGA1a protein

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In vivo posttranslational modifications of the high mobility group A1a proteins in breast cancer cells of differing metastatic potential

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Reversing histone methylation

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The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif

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Increase of HMGA1a protein methylation is a distinctive characteristic of leukaemic cells induced to undergo apoptosis

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Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)

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Phosphorylation of the DNA-binding domain of nonhistone high-mobility group I protein by cdc2 kinase: reduction of binding affinity

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Multivalent DNA-binding properties of the HMG-1 proteins

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PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation

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1 reference

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10.1074/JBC.M510231200

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release_wrpuxk3lsfgdncjog47ubfanhm

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