List of works - Adam Frankel

A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism

scientific article published on 8 February 2008

Approaches to measuring the activities of protein arginine N-methyltransferases

scientific article

Arginine methylation in yeast proteins during stationary-phase growth and heat shock

scientific article published on 19 July 2015

Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

scientific article (publication date: 26 May 2000)

Context and conformation dictate function of a transcription antitermination switch ⬇️

scientific article published on September 21, 2003

Förster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization.

scientific article

In vitro selection for sense codon suppression

scientific article

Inconvenient Truths for PRMT6 Kinetic Studies ⬇️

scientific article published on March 16, 2012

Kinetic Analysis of PRMT1 Reveals Multifactorial Processivity and a Sequential Ordered Mechanism.

scientific article published on 7 November 2017

Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4

scientific article

MS³ fragmentation patterns of monomethylarginine species and the quantification of all methylarginine species in yeast using MRM³.

scientific article published on 17 January 2013

Molecular basis for class Ib anti-arrhythmic inhibition of cardiac sodium channels

scientific article published on 14 June 2011

Nη-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases.

scientific article published on November 2010

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

scientific article published in July 2017

PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain.

scientific article published on October 2000

PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins

scientific article published in Journal of Biological Chemistry

PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity

scientific article

Peptidic partial bisubstrates as inhibitors of the protein arginine N-methyltransferases

scientific article published on 10 May 2011

Protein arginine N-methyltransferase substrate preferences for different nη-substituted arginyl peptides

scientific article published on 08 July 2014

RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases.

scientific article published on June 1999

Sources of S-adenosyl-L-homocysteine background in measuring protein arginine N-methyltransferase activity using tandem mass spectrometry

scientific article published on 3 September 2009

Structural basis of arginine asymmetrical dimethylation by PRMT6.

scientific article published on August 2016

Targeting protein arginine N-methyltransferases with peptide-based inhibitors: opportunities and challenges.

scientific article published on December 2013

The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity ⬇️

scientific article published on November 27, 2001

Unnatural RNA display libraries.

scientific article

Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A.

scientific article

Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis

scientific article

List of works by Adam Frankel

A kinetic study of human protein arginine N-methyltransferase 6 reveals a distributive mechanism

Approaches to measuring the activities of protein arginine N-methyltransferases

Arginine methylation in yeast proteins during stationary-phase growth and heat shock

Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

Context and conformation dictate function of a transcription antitermination switch ⬇️

Förster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization.

In vitro selection for sense codon suppression

Inconvenient Truths for PRMT6 Kinetic Studies ⬇️

Kinetic Analysis of PRMT1 Reveals Multifactorial Processivity and a Sequential Ordered Mechanism.

Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4

MS³ fragmentation patterns of monomethylarginine species and the quantification of all methylarginine species in yeast using MRM³.

Molecular basis for class Ib anti-arrhythmic inhibition of cardiac sodium channels

Nη-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases.

PRMT2 interacts with splicing factors and regulates the alternative splicing of BCL-X.

PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain.

PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in Proteins

PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity

Peptidic partial bisubstrates as inhibitors of the protein arginine N-methyltransferases

Protein arginine N-methyltransferase substrate preferences for different nη-substituted arginyl peptides

RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases.

Sources of S-adenosyl-L-homocysteine background in measuring protein arginine N-methyltransferase activity using tandem mass spectrometry

Structural basis of arginine asymmetrical dimethylation by PRMT6.

Targeting protein arginine N-methyltransferases with peptide-based inhibitors: opportunities and challenges.

The Novel Human Protein Arginine N-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity ⬇️

Unnatural RNA display libraries.

Yeast Hsl7 (histone synthetic lethal 7) catalyses the in vitro formation of omega-N(G)-monomethylarginine in calf thymus histone H2A.

Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis