scholarly journals Covalent inhibition of cyclin dependent kinase 2 (CDK2) through modification of a non-catalytic lysine side chain

2019 ◽  
Author(s):  
Nathalie Myrthil
Keyword(s):  
Side Chain ◽  
Cyclin Dependent Kinase ◽  
Lysine Side Chain ◽  
Covalent Inhibition

Catalytic activity of CuGHK peptide-based porous material

2021 ◽  
Author(s):  
Francisco G. Cirujano ◽  
Nuria Martin ◽  
Neyvis Almora-Barrios ◽  
Carlos Martí-Gastaldo
Keyword(s):  
Catalytic Activity ◽  
Porous Material ◽  
Active Sites ◽  
Room Temperature ◽  
Side Chain ◽  
Periodic Distribution ◽  
Lysine Side Chain ◽  
One Step

Room temperature one-step synthesis of the peptide-based porous material with a periodic distribution of pockets decorated with lysine side chain active sites behaves as a heterogeneous organocatalyst. The pockets are...

L-Lysine sulphate, C6H16N2O22+.SO42−: a novel conformation of the L-lysine side chain

1983 ◽  
Vol 39 (2) ◽  
pp. 281-283 ◽  
Author(s):  
S. Capasso ◽  
C. A. Mattia ◽  
L. Mazzarella ◽  
A. Zagari
Keyword(s):  
Side Chain ◽  
Lysine Side Chain

Structure of the dipeptide L-prolyl-L-lysine acetate. A new conformation of the lysine side chain

1988 ◽  
Vol 44 (2) ◽  
pp. 281-285 ◽  
Author(s):  
L. Urpí ◽  
M. Coll ◽  
J. A. Subirana ◽  
X. Solans ◽  
M. Font-Altaba
Keyword(s):  
Side Chain ◽  
Lysine Side Chain

ChemInform Abstract: Structure of L-Lysinamide Dihydrochloride. A New Conformation of the Lysine Side Chain.

ChemInform ◽  
2010 ◽  
Vol 22 (43) ◽  
pp. no-no
Author(s):  
X. DE LA CRUZ ◽  
J. TORMO ◽  
I. FITA ◽  
J. A. SUBIRANA
Keyword(s):  
Side Chain ◽  
Lysine Side Chain ◽  
Abstract Structure

Abstract C40: Inhibition of Mcl-1 through covalent modification of a non-catalytic lysine side chain

2015 ◽  
Author(s):  
Qibin Su ◽  
Gizem Akçay ◽  
Neil Grimster ◽  
Matthew Belmonte ◽  
Philip Rawlins ◽  
...  
Keyword(s):  
Covalent Modification ◽  
Side Chain ◽  
Lysine Side Chain

N-Terminus and Lysine Side Chain pKa Values of Melittin in Aqueous Solutions and Micellar Dispersions Measured by 15N NMR

Biochemistry ◽  
1995 ◽  
Vol 34 (40) ◽  
pp. 13196-13202 ◽  
Author(s):  
Lingyang Zhu ◽  
Marvin D. Kemple ◽  
Peng Yuan ◽  
Franklyn G. Prendergast
Keyword(s):  
Aqueous Solutions ◽  
Side Chain ◽  
15N Nmr ◽  
Pka Values ◽  
Lysine Side Chain ◽  
N Terminus

Peptide Architecture: Adding an α-Helix to the PYY Lysine Side Chain Provides Nanomolar Binding and Body-Weight-Lowering Effects

ChemMedChem ◽  
2010 ◽  
Vol 5 (4) ◽  
pp. 545-551 ◽  
Author(s):  
Søren L. Pedersen ◽  
Pottayil G. Sasikumar ◽  
Niels Vrang ◽  
Knud J. Jensen
Keyword(s):  
Body Weight ◽  
Side Chain ◽  
Lysine Side Chain ◽  
Α Helix

Inhibition of Mcl-1 through covalent modification of a noncatalytic lysine side chain

2016 ◽  
Vol 12 (11) ◽  
pp. 931-936 ◽  
Author(s):  
Gizem Akçay ◽  
Matthew A Belmonte ◽  
Brian Aquila ◽  
Claudio Chuaqui ◽  
Alexander W Hird ◽  
...  
Keyword(s):  
Covalent Modification ◽  
Side Chain ◽  
Lysine Side Chain

scholarly journals Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Abbas H. K. Al Temimi ◽  
Jona Merx ◽  
Christian J. van Noortwijk ◽  
Giordano Proietti ◽  
Romano Buijs ◽  
...  
Keyword(s):  
High Specificity ◽  
Fine Tuning ◽  
Side Chain ◽  
Chemical Probes ◽  
Histone Lysine ◽  
Lysine Side Chain ◽  
Synthetic Amino Acids ◽  
Epigenetic Gene Regulation ◽  
Lysine Methyltransferases ◽  
Histone Lysine Methyltransferases

AbstractHistone lysine methyltransferases (KMTs) play an important role in epigenetic gene regulation and have emerged as promising targets for drug discovery. However, the scope and limitation of KMT catalysis on substrates possessing substituted lysine side chains remain insufficiently explored. Here, we identify new unnatural lysine analogues as substrates for human methyltransferases SETD7, SETD8, G9a and GLP. Two synthetic amino acids that possess a subtle modification on the lysine side chain, namely oxygen at the γ position (KO, oxalysine) and nitrogen at the γ position (KN, azalysine) were incorporated into histone peptides and tested as KMTs substrates. Our results demonstrate that these lysine analogues are mono-, di-, and trimethylated to a different extent by trimethyltransferases G9a and GLP. In contrast to monomethyltransferase SETD7, SETD8 exhibits high specificity for both lysine analogues. These findings are important to understand the substrate scope of KMTs and to develop new chemical probes for biomedical applications.

Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear1H−15N NMR Spectroscopy

2011 ◽  
Vol 133 (4) ◽  
pp. 909-919 ◽  
Author(s):  
Alexandre Esadze ◽  
Da-Wei Li ◽  
Tianzhi Wang ◽  
Rafael Brüschweiler ◽  
Junji Iwahara
Keyword(s):  
Nmr Spectroscopy ◽  
Side Chain ◽  
15N Nmr ◽  
Amino Groups ◽  
Lysine Side Chain ◽  
15N Nmr Spectroscopy
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