1-7 of 7
Keywords: activation loop
Close
Save search
Follow your search
Access your saved searches in your account
Would you like to receive an alert when new items match your search?
Close Modal
Sort by
Articles

A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding

Open Access
Alexander Pflug, Marianne Schimpl, J. Willem M. Nissink, Ross C. Overman, Philip B. Rawlins, Caroline Truman, Elizabeth Underwood, Juli Warwicker, Jon Winter-Holt, William McCoull
Journal: Biochemical Journal
Biochem J (2020) 477 (22): 4443–4452.
https://doi.org/10.1042/BCJ20200735
Published: 27 November 2020
...Alexander Pflug; Marianne Schimpl; J. Willem M. Nissink; Ross C. Overman; Philip B. Rawlins; Caroline Truman; Elizabeth Underwood; Juli Warwicker; Jon Winter-Holt; William McCoull The activation loop (A-loop) plays a key role in regulating the catalytic activity of protein kinases. Phosphorylation...
View articletitled, A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding
Open the PDF for A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding in another window
Includes: Supplementary data
Articles

Conserved phosphorylation sites in the activation loop of the Arabidopsis phytosulfokine receptor PSKR1 differentially affect kinase and receptor activity

Open Access
Jens Hartmann, Dennis Linke, Christine Bönniger, Andreas Tholey, Margret Sauter
Journal: Biochemical Journal
Biochem J (2015) 472 (3): 379–391.
https://doi.org/10.1042/BJ20150147
Published: 27 November 2015
... 696 and Ser 698 in the JM (juxtamembrane) region and probably Ser 886 and/or Ser 893 in the AL (activation loop) as in planta phosphorylation sites. In vitro -expressed kinase was autophosphorylated at Ser 717 in the JM, and at Ser 733 , Thr 752 , Ser 783 , Ser 864 , Ser 911 , Ser 958 and Thr 998...
View articletitled, Conserved phosphorylation sites in the activation loop of the Arabidopsis phytosulfokine receptor PSKR1 differentially affect kinase and receptor activity
Open the PDF for Conserved phosphorylation sites in the activation loop of the Arabidopsis phytosulfokine receptor PSKR1 differentially affect kinase and receptor activity in another window
Includes: Supplementary data
Articles

Structure of cyclin G-associated kinase (GAK) trapped in different conformations using nanobodies

Open Access
Apirat Chaikuad, Tracy Keates, Cécile Vincke, Melanie Kaufholz, Michael Zenn, Bastian Zimmermann, Carlos Gutiérrez, Rong-guang Zhang, Catherine Hatzos-Skintges, Andrzej Joachimiak, Serge Muyldermans, Friedrich W. Herberg, Stefan Knapp, Susanne Müller
Journal: Biochemical Journal
Biochem J (2014) 459 (1): 59–69.
https://doi.org/10.1042/BJ20131399
Published: 14 March 2014
...-coated vesicle trafficking. The determined crystal structures of GAK in complex with specific single chain antibodies (nanobodies) revealed the domain plasticity of this kinase and unusual activation segment architecture. activation loop cyclin G-associated kinase drug side effect kinase...
View articletitled, Structure of cyclin G-associated kinase (GAK) trapped in different conformations using nanobodies
Open the PDF for Structure of cyclin G-associated kinase (GAK) trapped in different conformations using nanobodies in another window
Includes: Supplementary data
Articles

Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif

Available to Purchase
Jianchuan Wang, Chen Zhong, Fang Wang, Fangfang Qu, Jianping Ding
Journal: Biochemical Journal
Biochem J (2013) 454 (1): 39–47.
https://doi.org/10.1042/BJ20121863
Published: 26 July 2013
... of the activation loop. S6K1 has an array of substrates and is involved in many physiological processes. It plays an important role in gene transcription and mRNA processing, through phosphorylation of eEF2K (eukaryotic elongation factor-2 kinase) which is a negative regulator of transcription [ 4 , 5...
View articletitled, Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif
Open the PDF for Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif in another window
Includes: Supplementary data
Articles

The ubiquitin-associated domain of AMPK-related protein kinases allows LKB1-induced phosphorylation and activation

Available to Purchase
Mark H. Rider
Journal: Biochemical Journal
Biochem J (2006) 394 (3): e7.
https://doi.org/10.1042/BJ20060184
Published: 24 February 2006
... in mammalian cells Cell Metab. 2005 1 21 33 A common feature of the AMPK-related kinases is conservation of the activation loop (T-loop) threonine residue (Thr-172 in α1/α2-AMPK) located in a distinct motif between subdomains VII and VIII of the kinase domain. AMPK Thr-172 phosphorylation...
View articletitled, The ubiquitin-associated domain of AMPK-related protein kinases allows LKB1-induced phosphorylation and activation
Open the PDF for The ubiquitin-associated domain of AMPK-related protein kinases allows LKB1-induced phosphorylation and activation in another window
Articles

Identification of the autophosphorylation sites and characterization of their effects in the protein kinase DYRK1A

Available to Purchase
Sunke HIMPEL, Pascal PANZER, Klaus EIRMBTER, Hanna CZAJKOWSKA, Muhammed SAYED, Len C. PACKMAN, Tom BLUNDELL, Heiner KENTRUP, Joachim GRÖTZINGER, Hans-G. JOOST, Walter BECKER
Journal: Biochemical Journal
Biochem J (2001) 359 (3): 497–505.
https://doi.org/10.1042/bj3590497
Published: 25 October 2001
... of DYRK1A is dependent on the autophosphorylation of a conserved tyrosine residue in the activation loop. 8 5 2001 6 7 2001 31 8 2001 The Biochemical Society, London ©2001 2001 activation loop molecular model signal transduction tyrosine phosphorylation Abbreviations...
View articletitled, Identification of the autophosphorylation sites and characterization of their effects in the protein kinase DYRK1A
Open the PDF for Identification of the autophosphorylation sites and characterization of their effects in the protein kinase DYRK1A in another window
Articles

LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505

Available to Purchase
Toru AMANO, Kazuyo TANABE, Tomonori ETO, Shuh NARUMIYA, Kensaku MIZUNO
Journal: Biochemical Journal
Biochem J (2001) 354 (1): 149–159.
https://doi.org/10.1042/bj3540149
Published: 08 February 2001
... as substrates. We also show that LIMK2 is activated by ROCK by phosphorylation at Thr-505 within the activation loop. Wild-type LIMK2, but not its mutant (T505V) with replacement of Thr-505 by Val, was activated by ROCK in vitro and in vivo . LIMK2 mutants with replacement of Thr-505 by one or two Glu residues...
View articletitled, LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505
Open the PDF for LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505 in another window