scispace - formally typeset
H

Harry Charbonneau

Researcher at Purdue University

Publications -  72
Citations -  8179

Harry Charbonneau is an academic researcher from Purdue University. The author has contributed to research in topics: Peptide sequence & Phosphatase. The author has an hindex of 42, co-authored 72 publications receiving 8052 citations. Previous affiliations of Harry Charbonneau include University of Washington.

Papers
More filters
Journal ArticleDOI

Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes

TL;DR: A hypothesis is proposed explaining how phosphatases might act synergistically with the kinases to elicit a full physiological response, without regard to the state of phosphorylation of the target proteins.
Journal ArticleDOI

Exit from Mitosis Is Triggered by Tem1-Dependent Release of the Protein Phosphatase Cdc14 from Nucleolar RENT Complex

TL;DR: A mutation is identified, net1-1, that bypasses the lethality of tem1 delta and is a key component of a multifunctional complex, denoted RENT (for regulator of nucleolar silencing and telophase), that also contains Cdc14 and the silencing regulator Sir2.
Journal ArticleDOI

Primary structure and functional expression of the beta 1 subunit of the rat brain sodium channel

TL;DR: Results indicate that the beta 1 subunit is crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the rat brain sodium channel.
Journal ArticleDOI

The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase

TL;DR: A major protein tyrosine phosphatase (PTPase 1B) has been isolated in essentially homogeneous form from the soluble and particulate fractions of human placenta, and the sequence is strikingly similar to the tandem C-terminal homologous domains of the leukocyte common antigen (CD45).
Journal ArticleDOI

A calcium-dependent protein kinase with a regulatory domain similar to calmodulin.

TL;DR: A protein kinase that requires calcium but not calmodulin or phospholipids for activity has been purified from soybean and is established as a prototype for a new family of calcium-regulated protein kinases.