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January 24, 2010 | History

Functional characterization of PRDM12, a gene recurrently deleted during t(9;22) rearrangements in chronic myeloid leukemia patients 1 edition

Functional characterization of PRDM12, a gene recurrently deleted duri ...
Stefanie A. Turley

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Functional characterization of PRDM12, a gene recurrently deleted during t(9;22) rearrangements in chronic myeloid leukemia patients.

Published 2006 .
Written in English.

About the Book

Constitutive activation of BCR-ABL tyrosine kinase is the hallmark of CML in 95% of patients. The reciprocal fusion product, ABL-BCR, is deleted in 20% of patients. Studies have revealed a 120 kb deletion centromeric of ABL encompassing: PRDM12, a putative histone methyltransferase, and EXOSC2, a 3'-5' exoribonuclease.PRDM12 is one of 16 PR family members. PRDM12 consists of a PR domain and 3 zinc fingers. PR domains are thought to function as histone methyltransferases (HMT) as they share sequence similarity to the SET domain, known histone methyltransferases. The zinc fingers are important in DNA binding and protein-protein interactions. The PR domain of PRDM12 does not possess intrinsic HMT activity. Interestingly, PRDM12 is found associated with chromatin, suggesting it may be important in recruiting a complex of proteins involved in repression of transcription, as does another PR family member, PRDM1/PRDI-BF1/BLIMP-1. The involvement of PRDM12 with chromatin suggests a possible role in transcription regulation. This may reveal its importance in a more aggressive form of CML.

Edition Notes

Source: Masters Abstracts International, Volume: 44-06, page: 2727.

Thesis (M.Sc.)--University of Toronto, 2006.

Electronic version licensed for access by U. of T. users.

ROBARTS MICROTEXT copy on microfiche.

The Physical Object

Pagination
101 leaves.
Number of pages
101

ID Numbers

Open Library
OL19215107M
ISBN 13
9780494161593

History Created December 11, 2009 · 2 revisions Download catalog record: RDF / JSON

January 24, 2010 Edited by WorkBot add more information to works
December 11, 2009 Created by WorkBot add works page