C. Bancroft

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Identification by cell fusion of gene sequences that interact with positive trans-acting factors.

T. Lufkin, C. Bancroft, 1987, Science.

4 – RNA Dot and Blot Hybridization: Selected Procedures for Endocrine and Neuroendocrine Studies

T. Lufkin, B. White, G. Preston, 1989 .

RNA dot and blot hybridization: selected procedures for endocrine and neuroendocrine studies.

T. Lufkin, B. White, G. Preston, 1986, Methods in enzymology.

CHAPTER 6 – Regulation of Growth Hormone and Prolactin Gene Expression by Hormones and Calcium*

B. White, C. Bancroft, G. Gick, 1985 .

Growth hormone-releasing factor regulates growth hormone mRNA in primary cultures of rat pituitary cells.

N. Ling, F. Zeytin, P. Brazeau, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Growth hormone (GH)-releasing factor does not regulate GH release or GH mRNA levels in GH3 cells.

N. Ling, F. Zeytin, P. Brazeau, 1984, Endocrinology.

Glucocorticoid stimulation of growth hormone messenger ribonucleic acid levels in GH3 cells is inhibited by calcium but not by somatostatin.

C. Bancroft, G. Gick, 1987, Endocrinology.

An alternatively spliced Pit-1 isoform altered in its ability to trans-activate.

L. Chasin, B. Kloss, A. Morris, 1992, Nucleic acids research.

Regulation by calcium of prolactin and growth hormone mRNA sequences in primary cultures of rat pituitary cells.

C. Bancroft, G. Gick, 1985, The Journal of biological chemistry.

Mediation by calcium of thyrotropin--releasing hormone action on the prolactin promoter via transcription factor pit-1.

C. Bancroft, G. Yan, Guo-zai Yan, 1991, Molecular endocrinology.

Constitutively active G(S) alpha-subunits stimulate Pit-1 promoter activity via a protein kinase A-mediated pathway acting through deoxyribonucleic acid binding sites both for Pit-1 and for adenosine 3',5'-monophosphate response element-binding protein.

J. Loeffler, C. Gaiddon, C. Bancroft, 1996, Endocrinology.

A constitutively active form of CREB can activate expression of the rat prolactin promoter in non-pituitary cells

C. Bancroft, G. Yan, Xiao-huai Chen, 1994, Molecular and Cellular Endocrinology.

Transcriptional effects in GH3 cells of Gs alpha mutants associated with human pituitary tumors: stimulation of adenosine 3',5'-monophosphate response element-binding protein-mediated transcription and of prolactin and growth hormone promoter activity via protein kinase A.

J. Loeffler, C. Gaiddon, L. Mercken, 1995, Endocrinology.

Use of a selectable reporter for the isolation of mammalian regulatory genes.

L. Chasin, Y. Jiang, A. Morris, 1990, Gene.

Proximal rat prolactin promoter sequences direct optimal, pituitary cell-specific transcription.

T. Lufkin, W. Pan, C. Bancroft, 1989, Molecular endocrinology.

Detection of two chromatin proteins which bind specifically to the 5'-flanking region of the rat prolactin gene

T. Lufkin, B. White, G. Preston, 1985, Molecular and cellular biology.

Mapping and developmental expression analysis of the WD-repeat gene Preb.

T. Lufkin, C. Bancroft, L. Craciun, 2000, Genomics.

Proximal upstream flanking sequences direct calcium regulation of the rat prolactin gene.

C. Bancroft, A. E. Jackson, 1988, Molecular endocrinology.

Calcium channel agonists and antagonists: effects of chronic treatment on pituitary prolactin synthesis and intracellular calcium.

A. Zavacki, P. M. Hinkle, C. Bancroft, 1988, Molecular endocrinology.

Identification of a growth hormone gene promoter repressor element and its cognate double- and single-stranded DNA-binding proteins.

W. Pan, Q R Liu, C. Bancroft, 1990, The Journal of biological chemistry.

Pituitary adenylate cyclase-activating polypeptide regulates prolactin promoter activity via a protein kinase A-mediated pathway that is independent of the transcriptional pathway employed by thyrotropin-releasing hormone.

M. Sassaroli, X. Chen, C. Bancroft, 1996, Endocrinology.

Calcium induction of the mRNAs for prolactin and c-fos is independent of protein kinase C activity.

S. Bandyopadhyay, C. Bancroft, 1989, The Journal of biological chemistry.

The D2 receptor: blocked transcription in GH3 cells and cellular pathways employed by D2A to regulate prolactin promoter activity

C. Bancroft, D. Fischberg, 1995, Molecular and Cellular Endocrinology.

Cloning and characterization of human PREB; a gene that maps to a genomic region associated with trisomy 2p syndrome

K. Hirschhorn, B. Levy, C. Bancroft, 2000, Mammalian Genome.

Expression cloning and characterization of PREB (prolactin regulatory element binding), a novel WD motif DNA-binding protein with a capacity to regulate prolactin promoter activity.

P. M. Hinkle, M. Fliss, C. Bancroft, 1999, Molecular endocrinology.

Constitutively active Gq-α stimulates prolactin promoter activity via a pathway involving Raf activity

Jun Tian, C. Bancroft, Hai-Wen Ma, 1995, Molecular and Cellular Endocrinology.

Expression of constitutively active Gs alpha-subunits in GH3 pituitary cells stimulates prolactin promoter activity.

J. Chen, C. Bancroft, J. Tian, 1994, The Journal of biological chemistry.

Utilization of Never-Medicated Bipolar Disorder Patients towards Development and Validation of a Peripheral Biomarker Profile

Carter Bancroft, Laura J. Panek, C. Clelland, 2013, PloS one.

Thyrotropin-releasing hormone action on the prolactin promoter is mediated by the POU protein pit-1.

C Bancroft, W. Pan, G Z Yan, 1991, Molecular endocrinology.

Pituitary adenylate cyclase-activating polypeptide stimulates prolactin gene expression in a rat pituitary cell line.

C. Bancroft, D. T. Coleman, 1993, Endocrinology.

A Pit-1 phosphorylation mutant can mediate both basal and induced prolactin and growth hormone promoter activity.

C. Bancroft, X. H. Chen, D. Fischberg, 1994, Molecular endocrinology.

[49] Ca2+/Calmodulin regulation of prolactin gene expression

B. White, C. Bancroft, 1987 .

Epidermal growth factor and phorbol ester regulate prolactin gene expression via distinct pathways

S. Bandyopadhyay, C. Bancroft, A. E. Jackson, 1990, Molecular and Cellular Endocrinology.

Prolactin regulatory element binding protein as a potential transcriptional factor for the insulin gene in response to glucose stimulation

N. Wong, H. Iwama, H. Imachi, 2006, Diabetologia.

Either isoform of the dopamine D2 receptor can mediate dopaminergic repression of the rat prolactin promoter

S. Sealfon, K. Dong, C. Bancroft, 1991, Molecular and Cellular Endocrinology.

Nicotine Acts Directly on Pituitary GH3 Cells to Inhibit Prolactin Promoter Activity

C. Bancroft, Daniel T. Coleman, Carter Bancroft, 1995, Journal of neuroendocrinology.

Detection ofTwoChromatin Proteins WhichBindSpecifically tothe 5'-Flanking Region oftheRatProlactin Gene

G. Preston, C. Bancroft, 1985 .