Institute of Biochemistry

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1,041 to 1,050 of 1,362 Results

no enzyme control CG substrate.txt Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation Plain Text - 4.5 MB - MD5: 07952c6e424db104ee99286e6731b074
no enzyme control CN substrate.txt Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation Plain Text - 6.4 MB - MD5: 0b14eacd283dd29ab8d843d61ba628d2
no enzyme control MD_221.txt Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation Plain Text - 9.6 MB - MD5: 5a8cfc627ac86e53f78624da2befaf7e
no enzyme control MD_222.txt Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation Plain Text - 11.9 MB - MD5: 072a812944c71194459bf18d03e8ba52
no enzyme control PB_954.txt Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation Plain Text - 12.2 MB - MD5: 413bc4d5f9e8a2f896b941cab31ce58f
no enzyme control PB_955.txt Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation Plain Text - 9.3 MB - MD5: 8a550e97f117c08732d08b76217ea681
no enzyme control PB_956.txt Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation Plain Text - 7.7 MB - MD5: 0001bb40f5c9c9a817db0900fad68482
readme.pdf Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation Adobe PDF - 119.2 KB - MD5: fee216cf25110a60a46f76ebb5aba084
Additional data related to Schnee et al.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide Aug 15, 2022 - MD Simulations Jeltsch, Albert; Schnee, Philipp; Pleiss, Jürgen, 2022, "Additional data related to Schnee et al.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide", https://doi.org/10.18419/DARUS-2508, DaRUS, V2 This data collection contains additional data related to Schnee et al.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide. This includes MD simulations code and analysis scripts. The usage of these Phyton scripts is further explained in the enclosed readm...
Movie1_ssK36_hairpin_formation.mp4 Aug 15, 2022 - Additional data related to Schnee et al.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide MPEG-4 Video - 7.9 MB - MD5: bc370cb514eda10a067eaff28bc80a26 Formation of hairpin conformation of ssK36 peptide. The movie shows an MD simulation of the ssK36 peptide in solution and its formation of a hairpin conformation.

no enzyme control CG substrate.txt

Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation

Plain Text - 4.5 MB -

no enzyme control CN substrate.txt

Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation

Plain Text - 6.4 MB -

no enzyme control MD_221.txt

Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation

Plain Text - 9.6 MB -

no enzyme control MD_222.txt

Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation

Plain Text - 11.9 MB -

no enzyme control PB_954.txt

Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation

Plain Text - 12.2 MB -

no enzyme control PB_955.txt

Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation

Plain Text - 9.3 MB -

no enzyme control PB_956.txt

Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation

Plain Text - 7.7 MB -

readme.pdf

Sep 27, 2022 - NGS data related to Dukatz et al.: DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation

Adobe PDF - 119.2 KB -

Additional data related to Schnee et al.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide

Aug 15, 2022 - MD Simulations

Jeltsch, Albert; Schnee, Philipp; Pleiss, Jürgen, 2022, "Additional data related to Schnee et al.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide", https://doi.org/10.18419/DARUS-2508, DaRUS, V2

This data collection contains additional data related to Schnee et al.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide. This includes MD simulations code and analysis scripts. The usage of these Phyton scripts is further explained in the enclosed readm...

Movie1_ssK36_hairpin_formation.mp4

Aug 15, 2022 - Additional data related to Schnee et al.: Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide

MPEG-4 Video - 7.9 MB -

Formation of hairpin conformation of ssK36 peptide. The movie shows an MD simulation of the ssK36 peptide in solution and its formation of a hairpin conformation.

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