AMPK in health and disease

GR Steinberg, BE Kemp - Physiological reviews, 2009 - journals.physiology.org
The function and survival of all organisms is dependent on the dynamic control of energy
metabolism, when energy demand is matched to energy supply. The AMP-activated protein …

The conformational plasticity of protein kinases

M Huse, J Kuriyan - Cell, 2002 - cell.com
Protein kinases operate in a large number of distinct signaling pathways, where the tight
regulation of their catalytic activity is crucial to the development and maintenance of …

DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation

CJ Bakkenist, MB Kastan - Nature, 2003 - nature.com
The ATM protein kinase, mutations of which are associated with the human disease ataxia–
telangiectasia, mediates responses to ionizing radiation in mammalian cells. Here we show …

The CLAVATA1gene encodes a putative receptor kinase that controls shoot and floral meristem size in Arabidopsis

SE Clark, RW Williams, EM Meyerowitz - Cell, 1997 - cell.com
The shoot apical meristem is responsible for above-ground organ initiation in higher plants,
accomplishing continuous organogenesis by maintaining a pool of undifferentiated cells and …

Active and inactive protein kinases: structural basis for regulation

LN Johnson, MEM Noble, DJ Owen - Cell, 1996 - cell.com
Active and Inactive Protein Kinases: Structural Basis for Regulation: Cell Skip to Main
Content Advertisement Cell This journal offers authors two options (open access or …

Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

PD Jeffrey, AA Russo, K Polyak, E Gibbs, J Hurwitz… - Nature, 1995 - nature.com
The crystal structure of the human cyclinA-cyclin-dependent kinase2 (CDK2)-ATP complex
has been determined at 2.3 A resolution. CyclinA binds to one side of CDK2's catalytic cleft …

Structural basis for control by phosphorylation

LN Johnson, RJ Lewis - Chemical reviews, 2001 - ACS Publications
Posttranslational modification by phosphorylation is a ubiquitous regulatory mechanism in
both eukaryotes and prokaryotes. Intracellular phosphorylation by protein kinases, triggered …

Crystal structure of the tyrosine kinase domain of the human insulin receptor

SR Hubbard, L Wei, WA Hendrickson - Nature, 1994 - nature.com
The X-ray crystal structure of the tyrosine kinase domain of the human insulin receptor has
been determined by multiwavelength anomalous diffraction phasing and refined to 2.1 Å …

A critical evaluation of protein kinase regulation by activation loop autophosphorylation

R Reinhardt, TA Leonard - Elife, 2023 - elifesciences.org
Phosphorylation of proteins is a ubiquitous mechanism of regulating their function,
localization, or activity. Protein kinases, enzymes that use ATP to phosphorylate protein …

[HTML][HTML] Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

BJ Canagarajah, A Khokhlatchev, MH Cobb… - Cell, 1997 - cell.com
The structure of the active form of the MAP kinase ERK2 has been solved, phosphorylated
on a threonine and a tyrosine residue within the phosphorylation lip. The lip is refolded …