✦ LIBER ✦

Regulation of the Wild-Type and Y1235D Mutant Met Kinase Activation

✍ Scribed by Cristiani, Cinzia; Rusconi, Luisa; Perego, Rita; Schiering, Nikolaus; Kalisz, Henryk M.; Knapp, Stefan; Isacchi, Antonella

Book ID: 126115488
Publisher: American Chemical Society
Year: 2005
Tongue: English
Weight: 227 KB
Volume: 44
Category: Article
ISSN: 0006-2960
DOI: 10.1021/bi051242k

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Regulation of wild-type and mutant KCNQ1

Regulation of wild-type and mutant KCNQ1/KCNE1 channels by tyrosine kinase

✍ Sergey Missan; Jiansong Qi; Julie Crack; Terence F. McDonald; Paul Linsdell 📂 Article 📅 2009 🏛 Springer 🌐 English ⚖ 306 KB

Regulation of c-Src activity by the expr

Regulation of c-Src activity by the expression of wild-type v-Src and its kinase-dead double Y416F-K295N mutant

✍ Martina Vojtěchová; Filip Šenigl; Eva Šloncová; Zdena Tuháčková 📂 Article 📅 2006 🏛 Elsevier Science 🌐 English ⚖ 802 KB

Deuterium Exchange Mass Spectrometry as

Deuterium Exchange Mass Spectrometry as a Probe of Protein Kinase Activation. Analysis of Wild-Type and Constitutively Active Mutants of MAP Kinase Kinase-1 †

✍ Resing, Katheryn A.; Ahn, Natalie G. 📂 Article 📅 1998 🏛 American Chemical Society 🌐 English ⚖ 180 KB

Differential activation of yeast adenyla

Differential activation of yeast adenylate cyclase by wild type and mutant RAS proteins

✍ Broek, Daniel; Samiy, Nasrollah; Fasano, Ottavio; Fujiyama, Asao; Tamanoi, Fuyuh 📂 Article 📅 1985 🏛 Elsevier Science 🌐 English ⚖ 813 KB

Regulation of the neutral phosphatase in

Regulation of the neutral phosphatase inChlamydomonas reinhardi:An immunogenetic study of wild-type and mutant strains

✍ R. Loppes; J. Braipson; R. F. Matagne; A. Sassen; L. Ledoux 📂 Article 📅 1977 🏛 Springer 🌐 English ⚖ 600 KB

In Chlamydomonas reinhardi, the activity of the neutral phosphatase considerably increases when the cells are grown in the absence of inorganic phosphate (Pi). A comparative immunological study of cells grown on media containing Pi or not indicated that the neutral phosphatase was synthesized de nov

Potentiating AZT activation: structures

Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants’ improved kinetics with the HIV prodrug metabolite AZTMP

✍ Nils Ostermann; Arnon Lavie; Sreekanta Padiyar; Ralf Brundiers; Thomas Veit; Joc 📂 Article 📅 2000 🏛 Elsevier Science 🌐 English ⚖ 429 KB