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Biomedical subjects

C Hodgman

Publications and source records attributed to C Hodgman.

6 recordsLinked to original sources
PubMed1999

INTERACT: an object oriented protein-protein interaction database.

MOTIVATION: Protein-protein interactions provide vital information concerning the function of proteins, complexes and networks. Currently there is no widely accepted repository of this interaction information. Our aim is to provide a single database with the necessary architecture to fully store, query and analyse interaction data. RESULTS: An object oriented database has been created which provides scientists with a resource for examining existing protein-protein interactions and inferring possible interactions from the data stored. It also provides a basis for examining networks of interacting proteins, via analysis of the data stored. The database contains over a thousand interactions. CONTACT: k.eilbeck@stud.man.ac.uk

Computational Biology↗
PubMed1996

Identification of the homologous beige and Chediak-Higashi syndrome genes.

Vesicular transport to and from the lysosome and late endosome is defective in patients with Chediak-Higashi syndrome (CHS) and in mutant beige (bg) mice. CHS and bg cells have giant, perinuclear vesicles with characteristics of late endosomes and lysosomes that arise from dysregulated homotypic fusion. CHS and bg lysosomes also exhibit compartmental missorting of proteins, such as elastase, glucuronidase and cathepsin G. Lyst, a candidate gene for bg, was identified by direct complementary DNA selection from a yeast artificial chromosome (YAC) clone containing a 650-kilobase segment of the bg-critical region on mouse chromosome 13. Lyst is disrupted by a 5-kilobase deletion in bg mice, and Lyst messenger RNA is markedly reduced in bg homozygotes. The homologous human gene, LYST, is highly conserved with mouse Lyst, and contains a frame-shift mutation at nucleotides 117-118 of the coding domain in a CHS patient. Thus bg mice and human CHS patients have homologous disorders associated with Lyst mutations. Lyst encodes a protein with a carboxy-terminal prenylation motif and multiple potential phosphorylation sites. Lyst protein is predicted to form extended helical domains, and has a region of sequence similar to stathmin, a coiled-coil phosphoprotein thought to act as a relay integrating cellular signal response coupling.

Amino Acid Sequence↗
PubMed1988

Hormonal aspects of normal and abnormal behavior in adolescents. Study group report.

As stated initially, a significant proportion of health problems of youths have genetic predispositions and potentially identifiable antecedents of disease during childhood and adolescence. Until there is advancement in delineating the multiple dimensions and relationships of a psychobiologic developmental framework, interventions may fall short of their potential to either prevent or ameliorate these problems. To date, research has been limited by narrow definitions, lack of uniformity among measures, small samples, and homogenous populations. As a forward step, longitudinal investigations of subpopulations of youths may provide an opportunity for definitive study of the basic processes of puberty and be fruitful in evaluating the deleterious effects that stresses of contemporary life place on children and adolescents. In addition, efforts to communicate existing knowledge across disciplines and to approach psychobiologic research from an interdisciplinary perspective will enhance an understanding of the interplay of social, biologic, and environmental factors that are essential in the maturational process. This multidimensional approach with newer, broader perspectives is critical to advancing the development of a psychobiologic framework that will shed further light on the mechanisms of maturation and the interferences of this pubertal process that is the hallmark of adolescence.

Adolescent↗
PubMed1986

Identification of a new glycoprotein of herpes simplex virus type 1 and genetic mapping of the gene that codes for it.

A type-specific monoclonal antibody, LP10, precipitated a glycoprotein with a molecular weight of approximately 59,000 from purified herpes simplex virus type 1. Although this glycoprotein was similar in size to glycoprotein D (gD), it was shown to be less abundant in both virions and infected cells, to migrate more rapidly in its precursor form, to incorporate glucosamine but not mannose, and to have a more stable precursor in tunicamycin-treated cells than the gD precursor (pgD). Immunoassays of cells infected with insertion recombinants and intertypic recombinants localized the gene coding for the target antigen of LP10 to the unique short (Us) region at map units 0.892 to 0.924 excluding gD. The target antigen of LP10 was then definitively mapped to the Us4 open reading frame by immunoprecipitation of a polypeptide synthesized by in vitro translation of a Us4-specific transcript prepared by using an SP6 cloning This newly identified glycoprotein product of the Us4 gene of herpes simplex virus type 1 is distinct from the previously identified gB1, gC1, gE1, and gH1.

Antibodies, Monoclonal↗