Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Protein science 33 (2024), No. e4897

Event: Veröffentlichung

(where): Stuttgart

(who): Universitätsbibliothek der Universität Stuttgart

(when): 2024

Creator: Weirich, Sara
Ulu, Gizem T.
Chandrasekaran, Thyagarajan T.
Kehl, Jana
Schmid, Jasmin
Dorscht, Franziska
Kublanovsky, Margarita
Levy, Dan
Jeltsch, Albert

DOI: 10.18419/opus-14749

URN: urn:nbn:de:bsz:93-opus-ds-147689

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 25.03.2025, 1:49 PM CET

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Associated

Weirich, Sara
Ulu, Gizem T.
Chandrasekaran, Thyagarajan T.
Kehl, Jana
Schmid, Jasmin
Dorscht, Franziska
Kublanovsky, Margarita
Levy, Dan
Jeltsch, Albert
Universitätsbibliothek der Universität Stuttgart

Time of origin

2024

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Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues

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Other Objects (12)

Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase

Structure, activity and function of the NSD3 protein lysine methyltransferase

Site-specific RNA methylation by a methyltransferase ribozyme

Histone lysine methylation in the context of nuclear architecture

Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9

Lysine residues control the conformational dynamics of beta 2-glycoprotein I

Histone H3 lysine 9 methylation : a signature for chromatin function

The role of histone H3.3 lysine 4 and lysine 36 residues in mouse embryonic stem cells and neuronal development

Triple helix-targeted DNA methylation with DNA methyltransferase-oligodeoxynucleotide conjugates

Lysine methyltransferase 9 (KMT9) is an actionable target in muscle-invasive bladder cancer

Identification of protein lysine methylation readers with a yeast three-hybrid approach

Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase

Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase

Structure, activity and function of the NSD3 protein lysine methyltransferase

Site-specific RNA methylation by a methyltransferase ribozyme

Histone lysine methylation in the context of nuclear architecture

Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9

Lysine residues control the conformational dynamics of beta 2-glycoprotein I

Histone H3 lysine 9 methylation : a signature for chromatin function

The role of histone H3.3 lysine 4 and lysine 36 residues in mouse embryonic stem cells and neuronal development

Triple helix-targeted DNA methylation with DNA methyltransferase-oligodeoxynucleotide conjugates

Lysine methyltransferase 9 (KMT9) is an actionable target in muscle-invasive bladder cancer

Identification of protein lysine methylation readers with a yeast three-hybrid approach

Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase

Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase

Structure, activity and function of the NSD3 protein lysine methyltransferase

Site-specific RNA methylation by a methyltransferase ribozyme

Histone lysine methylation in the context of nuclear architecture

Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9

Lysine residues control the conformational dynamics of beta 2-glycoprotein I

Histone H3 lysine 9 methylation : a signature for chromatin function

The role of histone H3.3 lysine 4 and lysine 36 residues in mouse embryonic stem cells and neuronal development

Triple helix-targeted DNA methylation with DNA methyltransferase-oligodeoxynucleotide conjugates

Lysine methyltransferase 9 (KMT9) is an actionable target in muscle-invasive bladder cancer

Identification of protein lysine methylation readers with a yeast three-hybrid approach

Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase

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