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 …
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 …
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 …
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 …
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 …
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 …
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 …
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 …
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 …