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23 results on '"McCann, Kathleen L."'

14. When Good Ribosomes Go Bad

Author

Baserga, Susan J., primary, McCann, Kathleen L., additional, Teramoto, Takamasa, additional, Zhang, Jun, additional, and Tanaka Hall, Traci M., additional

Published
2016
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15. Automated colitis detection from endoscopic biopsies as a tissue screening tool in diagnostic pathology

Author

McCann, Michael T., McCann, Kathleen L., Ramamurthy Bhagavatula, Fickus, Matthew, Ozolek, John A., and Kovacevic, Jelena

Subjects
90699 Electrical and Electronic Engineering not elsewhere classified, FOS: Electrical engineering, electronic engineering, information engineering, Computer Engineering
Abstract

We present a method for identifying colitis in colon biopsies as an extension of our framework for the automated identification of tissues in histology images. Histology is a critical tool in both clinical and research applications, yet even mundane histological analysis, such as the screening of colon biopsies, must be carried out by highly-trained pathologists at a high cost per hour, indicating a niche for potential automation. To this end, we build upon our previous work by extending the histopathology vocabulary (a set of features based on visual cues used by pathologists) with new features driven by the colitis application. We use the multiple-instance learning framework to allow our pixel-level classifier to learn from image-level training labels. The new system achieves accuracy comparable to state-of-the-art biological image classifiers with fewer and more intuitive features.

Published
2012
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17. Tissue specific roles for the Ribosome Biogenesis Factor Wdr43 in zebrafish development

Author

Zhao, Chengtian, Andreeva, Viktoria, Gibert, Yann, LaBonty, Melissa, Lattanzi, Victoria, Prabhudesai, Shubhangi, Zhou, Yi, Zon, Leonard, McCann, Kathleen L., Baserga, Susan, Yelick, Pamela C., Zhao, Chengtian, Andreeva, Viktoria, Gibert, Yann, LaBonty, Melissa, Lattanzi, Victoria, Prabhudesai, Shubhangi, Zhou, Yi, Zon, Leonard, McCann, Kathleen L., Baserga, Susan, and Yelick, Pamela C.

Abstract

During vertebrate craniofacial development, neural crest cells (NCCs) contribute to most of the craniofacial pharyngeal skeleton. Defects in NCC specification, migration and differentiation resulting in malformations in the craniofacial complex are associated with human craniofacial disorders including Treacher-Collins Syndrome, caused by mutations in TCOF1. It has been hypothesized that perturbed ribosome biogenesis and resulting p53 mediated neuroepithelial apoptosis results in NCC hypoplasia in mouse Tcof1 mutants. However, the underlying mechanisms linking ribosome biogenesis and NCC development remain poorly understood. Here we report a new zebrafish mutant, fantome (fan), which harbors a point mutation and predicted premature stop codon in zebrafish wdr43, the ortholog to yeast UTP5. Although wdr43 mRNA is widely expressed during early zebrafish development, and its deficiency triggers early neural, eye, heart and pharyngeal arch defects, later defects appear fairly restricted to NCC derived craniofacial cartilages. Here we show that the C-terminus of Wdr43, which is absent in fan mutant protein, is both necessary and sufficient to mediate its nucleolar localization and protein interactions in metazoans. We demonstrate that Wdr43 functions in ribosome biogenesis, and that defects observed in fan mutants are mediated by a p53 dependent pathway. Finally, we show that proper localization of a variety of nucleolar proteins, including TCOF1, is dependent on that of WDR43. Together, our findings provide new insight into roles for Wdr43 in development, ribosome biogenesis, and also ribosomopathy-induced craniofacial phenotypes including Treacher-Collins Syndrome.

Published
2014

21. Fine-mapping reveals novel alternative splicing of the dopamine transporter

Author

Talkowski, Michael E., primary, McCann, Kathleen L., additional, Chen, Michael, additional, McClain, Lora, additional, Bamne, Mikhil, additional, Wood, Joel, additional, Chowdari, Kodavali V., additional, Watson, Annie, additional, Prasad, Konasale M., additional, Kirov, George, additional, Georgieva, Lyudmilla, additional, Toncheva, Draga, additional, Mansour, Hader, additional, Lewis, David A., additional, Owen, Michael, additional, O'Donovan, Michael, additional, Papasaikas, Panagiotis, additional, Sullivan, Patrick, additional, Ruderfer, Douglas, additional, Yao, Jeffrey K, additional, Leonard, Sherry, additional, Thomas, Pramod, additional, Miyajima, Fabio, additional, Quinn, John, additional, Lopez, A. Javier, additional, and Nimgaonkar, Vishwajit L., additional

Published
2010
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22. A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization.

Author

Chen Qiu, McCann, Kathleen L., Wine, Robert N., Baserga, Susan J., and Tanaka Hall, Traci M.

Subjects
*MESSENGER RNA, *RIBOSOMAL RNA, *DEVELOPMENTAL neurobiology, *CRYSTAL structure, *HISTOCOMPATIBILITY antigens, *ELECTRON density, *SMALL-angle X-ray scattering
Abstract

Pumilio/feminization of XX and XO animals (fem)-3 mRNA-binding factor (PUF) proteins bind sequence specifically to mRNA targets using a single-stranded RNA-binding domain comprising eight Pumilio (PUM) repeats. PUM repeats have now been identified in proteins that function in pre-rRNA processing, including human Puf-A and yeast Puf6. This is a role not previously ascribed to PUF proteins. Here we present crystal structures of human Puf-A that reveal a class of nucleic acid-binding proteins with 11 PUM repeats arranged in an "L"-like shape. In contrast to classical PUF proteins, Puf-A forms sequence-independent interactions with DNA or RNA, mediated by conserved basic residues. We demonstrate that equivalent basic residues in yeast Puf6 are important for RNA binding, pre-rRNA processing, and mRNA localization. Thus, PUM repeats can be assembled into alternative folds that bind to structured nucleic acids in addition to forming canonical eight-repeat crescent-shaped RNA-binding domains found in classical PUF proteins. [ABSTRACT FROM AUTHOR]

Published
2014
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23. Driving nucleolar assembly.

Author

McCann KL and Baserga SJ

Subjects
Animals, Humans, Artificial Cells metabolism, Cell Division physiology, Cell Nucleolus metabolism
Abstract

In this issue of Genes & Development, Grob and colleagues (pp. 220-230) identify the minimal molecular requirements to assemble a fully functional nucleolus in human cells and demonstrate the importance of the nucleolar transcription factor upstream binding factor (UBF) as a mitotic bookmark at the ribosomal DNA (rDNA).

Published
2014
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