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Do protein motifs read the histone code?

Article Abstract:

The existence of different patterns of chemical modifications like acetylation, methylation and others of the histone tails led to the histone code hypothesis some years ago. According to this hypothesis, these modifications would provide binding sites for proteins that can change the chromatin state to either active or repressed.

Author: Cruz, Xavier de la, Lois, Sergio, Sanchez-Molina, Sara, Martinez-Balbas, Marian A.
Publisher: John Wiley & Sons, Inc.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 2005
Histones

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Protein-interaction mapping in search of effective drug targets

Article Abstract:

The signaling complexes, their organization into a higher order networks and the discovery of drug targets through protein-interaction mapping is presented. Protein-interaction mapping is a vital discovery tool in systems biology approach of understanding diseases and creating novel strategies of human disease management.

Author: Chaudhuri, Amitabha, Chant, John
Publisher: John Wiley & Sons, Inc.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 2005
Protein research

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PAD: The smoking gun behind arginine methylation signaling?

Article Abstract:

Protein arginine methylation represents a unique signaling system that is considered to be long-term and irreversible. The discovery of a means for eucaryotic cells to remove pot-transitional methyl marks on proteins brings arginine methylation into the mainstream of cell signaling.

Author: Denman, Robert B.
Publisher: John Wiley & Sons, Inc.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 2005
Arginine, Genetic code

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Subjects list: Research, United States, Protein binding, Methylation
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