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7. Precise genetic mapping and haplotype analysis of the familial dysautonomia gene on human chromosome 9q31

Author

Blumenfeld, Anat, Slaugenhaupt, Susan A., Liebert, Christopher B., Temper, Violeta, Maayan, Channa, Gill, Sandra, Lucente, Diane E., Idelson, Maria, MacCormack, Kathy, Monahan, Mary Anne, Mull, James, Leyne, Maire, Mendillo, Marc, Schiripo, Taryn, Mishori, Esther, Breakefield, Xandra, Axelrod, Felicia B., and Gusella, James F.

Subjects
Dysautonomia -- Genetic aspects, Nervous system diseases -- Genetic aspects, Genetic disorders -- Research, Biological sciences
Abstract

Findings have enabled researchers to develop accurate genetic testing for familial dysautonomia in both families who exhibit the disease and carriers of the disease. Genetic mapping has provided a narrower location of the defective gene, confirmed by haplotype analysis. This process revealed a prominent haplotype found in 435 of 441 familial dysautonomia chromosomes.

Published
1999

10. Tissue-Specific Expression of a Splicing Mutation in the IKBKAP Gene Causes Familial Dysautonomia

Author

Slaugenhaupt, Susan A., Blumenfeld, Anat, Gill, Sandra P., Leyne, Maire, Mull, James, Cuajungco, Math P., Liebert, Christopher B., Chadwick, Brian, Idelson, Maria, Reznik, Luba, Robbins, Christiane M., Makalowska, Izabela, Brownstein, Michael J., Krappmann, Daniel, Scheidereit, Claus, Maayan, Channa, Axelrod, Felicia B., and Gusella, James F.

Subjects
Dysautonomia -- Genetic aspects, Ashkenazim -- Diseases, Gene mutations -- Research, Human genetics -- Research, Biological sciences
Published
2001

18. Tissue-Specific Expression of a Splicing Mutation in the Gene Causes Familial Dysautonomia

Author

Slaugenhaupt, Susan A., primary, Blumenfeld, Anat, additional, Gill, Sandra P., additional, Leyne, Maire, additional, Mull, James, additional, Cuajungco, Math P., additional, Liebert, Christopher B., additional, Chadwick, Brian, additional, Idelson, Maria, additional, Reznik, Luba, additional, Robbins, Christiane M., additional, Makalowska, Izabela, additional, Brownstein, Michael J., additional, Krappmann, Daniel, additional, Scheidereit, Claus, additional, Maayan, Channa, additional, Axelrod, Felicia B., additional, and Gusella, James F., additional

Published
2001
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19. Cloning, genomic organization and expression of a putative human transmembrane protein related to the Caenorhabditis elegans M01F1.4 gene

Author

Chadwick, Brian P, primary, Gill, Sandra, additional, Leyne, Maire, additional, Mull, James, additional, Liebert, Christopher B, additional, Robbins, Christiane M, additional, Pinkett, Heather W, additional, Makalowska, Izabela, additional, Maayan, Channa, additional, Blumenfeld, Anat, additional, Axelrod, Felicia B, additional, Brownstein, Mike, additional, and Slaugenhaupt, Susan A, additional

Published
1999
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20. Cloning, Mapping, and Expression of Two Novel Actin Genes, Actin-like-7A (ACTL7A) and Actin-like-7B (ACTL7B), from the Familial Dysautonomia Candidate Region on 9q31

Author

Chadwick, Brian P., primary, Mull, James, additional, Helbling, Lisa A., additional, Gill, Sandra, additional, Leyne, Maire, additional, Robbins, Christiane M., additional, Pinkett, Heather W., additional, Makalowska, Izabela, additional, Maayan, Channa, additional, Blumenfeld, Anat, additional, Axelrod, Felicia B., additional, Brownstein, Mike, additional, Gusella, James F., additional, and Slaugenhaupt, Susan A., additional

Published
1999
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21. The human gene for neurotrophic tyrosine kinase receptor type 2 (NTRK2) is located on chromosome 9 but is not the familial dysautonomia gene

Author

Slaugenhaupt, Susan A., primary, Blumenfeld, Anat, additional, Liebert, Christopher B., additional, Mull, James, additional, Lucente, Diane E., additional, Monahan, Marianne, additional, Breakefield, Xandra O., additional, Maayan, Channa, additional, Parada, Luis, additional, Axelrod, Felicia B., additional, and Gusella, James F., additional

Published
1995
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22. Loss of Mouse Ikbkap, a Subunit of Elongator, Leads to Transcriptional Deficits and Embryonic Lethality That Can Be Rescued by Human IKBKAP.

Author

Yei-Tsung Chen, Hims, Matthew M., Shetty, Ranjit S., Mull, James, Lijuan Liu, Leyne, Maire, and Slaugenhaupt, Susan A.

Subjects
DYSAUTONOMIA, GENETIC disorders, NERVOUS system, EMBRYOLOGY, NEUROPATHY, MESSENGER RNA, MORPHOLOGY
Abstract

Familial dysautonomia (FD), a devastating hereditary sensory and autonomic neuropathy, results from an intronic mutation in the IKBKAP gene that disrupts normal mRNA splicing and leads to tissue-specific reduction of IKBKAP protein (IKAP) in the nervous system. To better understand the roles of IKAP in vivo, an Ikbkap knockout mouse model was created. Results from our study show that ablating Ikbkap leads to embryonic lethality, with no homozygous Ikbkap knockout (Ikbkap-/-) embryos surviving beyond 12.5 days postcoitum. Morphological analyses of the Ikbkap-/- conceptus at different stages revealed abnormalities in both the visceral yolk sac and the embryo, including stunted extraembryonic blood vessel formation, delayed entry into midgastrulation, disoriented dorsal primitive neural alignment, and failure to establish the embryonic vascular system. Further, we demonstrate downregulation of several genes that are important for neurulation and vascular development in the Ikbkap-/- embryos and show that this correlates with a defect in transcriptional elongation-coupled histone acetylation. Finally, we show that the embryonic lethality resulting from Ikbkap ablation can be rescued by a human IKBKAP transgene. For the first time, we demonstrate that IKAP is crucial for both vascular and neural development during embryogenesis and that protein function is conserved between mouse and human. [ABSTRACT FROM AUTHOR]

Published
2009
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23. Kinetin Improves IKBKAPmRNA Splicing in Patients With Familial Dysautonomia

Author

AXELROD, FELICIA B., LIEBES, LEONARD, SIMSON, GABRIELLE GOLD-VON, MENDOZA, SANDRA, MULL, JAMES, LEYNE, MAIRE, NORCLIFFE-KAUFMANN, LUCY, KAUFMANN, HORACIO, and SLAUGENHAUPT, SUSAN A.

Abstract

Familial dysautonomia (FD) is caused by an intronic splice mutation in the IKBKAPgene that leads to partial skipping of exon 20 and tissue-specific reduction in I--B kinase complex-associated protein/elongation protein 1 (IKAP/ELP-1) expression. Kinetin (6-furfurylaminopurine) has been shown to improve splicing and increase WT IKBKAPmRNA and IKAP protein expression in FD cell lines and carriers. To determine whether oral kinetin treatment could alter mRNA splicing in FD subjects and was tolerable, we administered kinetin to eight FD individuals homozygous for the splice mutation. Subjects received 23.5 mg/Kg/d for 28 d. An increase in WT IKBKAPmRNA expression in leukocytes was noted after 8 d in six of eight individuals; after 28 d, the mean increase compared with baseline was significant (p0.002). We have demonstrated that kinetin is tolerable in this medically fragile population. Not only did kinetin produce the desired effect on splicing in FD patients but also that effect seems to improve with time despite lack of dose change. This is the first report of a drug that produces in vivomRNA splicing changes in individuals with FD and supports future long-term trials to determine whether kinetin will prove therapeutic in FD patients.

Published
2011
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25. Interview with Lydia Groves

Author

Walker, William K., Walker, William K., Wilford, Craig W., Mull, James R., Groves, Lydia Dillon, Walker, William K., Walker, William K., Wilford, Craig W., Mull, James R., and Groves, Lydia Dillon

Abstract

An interview with Lydia Groves regarding her experiences in a one-room school house.

Published
1986

29. Determination of Small Amounts of Morphine in Blood

Author

Mull, James W.

Abstract

The fate of morphine in the animal body is a question that has stimulated much excellent work and the development of many methods for the determination of the drug. We do not have space to enumerate, much less to discuss, these methods, 2 of the more recent examples of which are those described by Wolff, Riegel, and Fry1and by Abe and Uchida.2Most of these methods were unsuited to our purpose since they were not designed for use with blood, and the others required more material or a more elaborate procedure than we wished to employ.The method herein described has the advantage of simplicity, takes but a few hours to complete, and gives quantitative results with small amounts of blood. It is based on that of Sanchez,3which was designed for the determination of morphine in pure solution. We have modified it for use with blood filtrates, deproteinized by the method of Somogyi,4introducing scopolamine to bring down the precipitate and permit the removal of the reacting solutions. The method in detail is as follows: A 1-to-10 filtrate is prepared by laking 1 part of blood with 7 parts of water. To this is added with constant stirring 1 part 10% zinc sulphate and 1 part 0.5 N sodium hydroxide.∗After standing 10 minutes the precipitate is centrifuged down and the supernatant liquid filtered through No. 2 Whatman paper. Treated in this manner 5 cc. blood yield over 30 cc. filtrate.To 20 cc. of the filtrate, equivalent to 2 cc. blood, is added 2.5 mg. of scopolamine hydrobromide, from a solution containing 1 mg. per 1 cc. (Proportionally smaller amounts may be used if the concentration of morphine is high.) The morphine is then precipitated by 0.4 cc. of Wavelet's solution.†The material is thoroughly mixed by stirring or shaking, and set in a cold place for about an hour.

Published
1937
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30. Peters plus syndrome mutations affect the function and stability of human ß1,3-glucosyltransferase.

Author

Ao Zhang, Venkat, Aarya, Taujale, Rahil, Mull, James L., Atsuko Ito, Kannan, Natarajan, and Haltiwanger, Robert S.

Subjects
*SHORT stature, *CONGENITAL disorders, *DEVELOPMENTAL delay, *FUCOSE, *PHENOTYPES
Abstract

Peters Plus Syndrome (PTRPLS OMIM #261540) is a severe congenital disorder of glycosylation where patients have multiple structural anomalies, including Peters anomaly of the eye (anterior segment dysgenesis), disproportionate short stature, brachydactyly, dysmorphic facial features, developmental delay, and variable additional abnormalities. PTRPLS patients and some Peters Plus-like (PTRPLS-like) patients (who only have a subset of PTRPLS phenotypes) have mutations in the gene encoding ß1,3-glucosyltransferase (B3GLCT). B3GLCT catalyzes the transfer of glucose to O-linked fucose on thrombospondin type-1 repeats. Most B3GLCT substrate proteins belong to the ADAMTS superfamily and play critical roles in extracellular matrix. We sought to determine whether the PTRPLS or PTRPLS-like mutations abrogated B3GLCT activity. B3GLCT has two putative active sites, one in the N-terminal region and the other in the C-terminal glycosyltransferase domain. Using sequence analysis and in vitro activity assays, we demonstrated that the C-terminal domain catalyzes transfer of glucose to O-linked fucose. We also generated a homology model of B3GLCT and identified D421 as the catalytic base. PTRPLS and PTRPLS-like mutations were individually introduced into B3GLCT, and the mutated enzymes were evaluated using in vitro enzyme assays and cellbased functional assays. Our results demonstrated that PTRPLS mutations caused loss of B3GLCT enzymatic activity and/or significantly reduced protein stability. In contrast, B3GLCT with PTRPLS-like mutations retained enzymatic activity, although some showed a minor destabilizing effect. Overall, our data supports the hypothesis that loss of glucose from B3GLCT substrate proteins is responsible for the defects observed in PTRPLS patients, but not for those observed in PTRPLS-like patients. [ABSTRACT FROM AUTHOR]

Published
2021
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