User:Niallg: Difference between revisions

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Welcome to the newly established Howlett Laboratory at the University of Rhode Island in Kingston. We are interested in understanding the etiology of the rare recessive disease Fanconi anemia (FA). FA is characterized by developmental defects, bone marrow failure, and an increased susceptibility to cancer.
='''Niall G. Howlett'''=


=Fanconi Anemia=
==Contact Information==
RI-INBRE Assistant Professor<br>
Department of Cell and Molecular Biology<br>
University of Rhode Island<br>
113 Morrill Science Bldg.<br>
45 Lower College Road<br>
Kingston, Rhode Island 02881<br>
Phone. 401-874-4306<br>
Fax. 401-874-2202<br>
Email. nhowlett@mail.uri.edu, niall@howlett.com


FA is a rare hereditary disease characterized by developmental defects, hematological deficiencies and increased susceptibility to cancer, including acute myelogenous leukemia (AML) and solid tumors of the head and neck and gynecological regions. FA is a rare, predominantly autosomal recessive disorder (FA-B is caused by mutation in the X-linked FANCB gene), with a prevalence of approximately 1-5 affected individuals per million. There are currently approximately 300 known affected individuals in the US. FA patient derived cells are hypersensitive to DNA cross-linking agents such as mitomycin C and cisplatin.
==Education==
1990-1994 B.Sc. Industrial Biochemistry, University of Limerick, Limerick, Ireland<br>
1995-1999 Ph.D. Biological & Molecular Sciences, Oxford Brookes University, Oxford, U.K.  


There are currently thirteen defined FA complementation groups (A, B, C, D1/BRCA2, D2, E, F, G, I, J/BRIP1, L, M, and N/PALB2) and the genes underlying twelve of these complementation groups have been cloned. The FA proteins and the BReast Cancer-Associated proteins BRCA1 and BRCA2 interact in a common pathway essential in the cellular DNA damage response. The FA proteins A, B, C, E, F, G, L, and M assemble in a multi-subunit nuclear complex. Following exposure to DNA damaging agents, and also during S phase of the cell cycle, the core FA complex activates the mono-ubiquitination of lysine 561 of the FANCD2 protein, signaling its activation and translocation to discrete nuclear foci where it co-localizes with the key DNA repair proteins BRCA1 and RAD51. Mono-ubiquitination of FANCD2 promotes loading of the BRCA2 protein into chromatin complexes, and facilitates the assembly of DNA damage inducible RAD51 nuclear foci. However, the exact biochemical function of chromatin-associated mono-ubiquitinated FANCD2 protein remains unclear.
==Training==
1998-2001 Research Fellow in Cancer Cell Biology, Harvard School of Public Health, Boston, MA<br>
2001-2003 Research Fellow in Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA<br>
2003-2006 Research Fellow in Human Genetics, University of Michigan, Ann Arbor, MI<br>
2006-2007      Research Investigator in Human Genetics, University of Michigan, Ann Arbor, MI
 
==Lab Page==
[[Howlett Laboratory]] at the University of Rhode Island

Latest revision as of 12:30, 4 April 2007

Niall G. Howlett

Contact Information

RI-INBRE Assistant Professor
Department of Cell and Molecular Biology
University of Rhode Island
113 Morrill Science Bldg.
45 Lower College Road
Kingston, Rhode Island 02881
Phone. 401-874-4306
Fax. 401-874-2202
Email. nhowlett@mail.uri.edu, niall@howlett.com

Education

1990-1994 B.Sc. Industrial Biochemistry, University of Limerick, Limerick, Ireland
1995-1999 Ph.D. Biological & Molecular Sciences, Oxford Brookes University, Oxford, U.K.

Training

1998-2001 Research Fellow in Cancer Cell Biology, Harvard School of Public Health, Boston, MA
2001-2003 Research Fellow in Pediatric Oncology, Dana-Farber Cancer Institute, Boston, MA
2003-2006 Research Fellow in Human Genetics, University of Michigan, Ann Arbor, MI
2006-2007 Research Investigator in Human Genetics, University of Michigan, Ann Arbor, MI

Lab Page

Howlett Laboratory at the University of Rhode Island

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