Biomedical subjects

L Wills

Publications and source records attributed to L Wills.

9 recordsLinked to original sources

PubMed2001

Phenotype of FAECB (Facility for Automated Experiments in Cell Biology) Chinese hamster ovary mutants with minimal UV-sensitivity.

The Facility for Automated Experiments in Cell Biology (FAECB) collection of over 200 lines of ultraviolet (UV)-sensitive mutant Chinese hamster ovary (CHO) cells has previously been studied for complementation group assignment (CG), with representatives of rodent UV CGs 1-6 (ERCC1-6) and the new rodent XRCC9/FANCG group identified. Ten mutants from the collection, including a further six derived from wildtype AA8, three UV-sensitive double-mutants of CHO ERCC1 cell line UV4, and a UV-sensitive mutant of CHO XRCC1 cell line EM9, had not been assigned or characterized in these previous studies. These 10 mutants include 8 with approximately 1.5-fold the UV-sensitivity of the parental line (AA8, EM9, or UV4), and 2 with about 2-fold the UV-sensitivity of AA8. The present study reports the partial characterization of these 10 mutants in terms of sensitivity to UV (with and without caffeine), ionizing radiation, mitomycin C (MMC) and ethyl methanesulfonate (EMS); proficiency in DNA repair (unscheduled DNA synthesis (UDS)); and UV-mutability. The phenotypes of the 10 cell lines were heterogeneous, a number showed reduced UDS or UV-sensitization by caffeine, whilst others showed marked sensitivity to EMS or MMC, and they may have mutations in different genes involved in nucleotide excision repair, post-replicational repair, base excision repair or recombinational repair. Previous mutants isolated as part of the FAECB collection have proved to be extremely important in characterizing mammalian DNA repair processes and cloning human repair genes and these current mutants, whilst not as hypersensitive to UV, may still have the potential to make further contributions.

Animals↗

PubMed2000

Sleep disorders in children and teens. Helping patients and their families get some rest.

Diagnosing sleep disorders in children and adolescents is challenging and rewarding and requires integration of medical, neurodevelopmental, and behavioral histories. Most patients can be successfully treated once a thorough evaluation has been completed and age-appropriate differential diagnosis of common sleep disorders has been considered. With appropriate knowledge and tools, physicians may find that pediatric sleep disorders are some of the most treatable problems in medicine.

Adolescent↗

PubMed1998

Mutational analysis of the N-linked glycans on Autographa californica nucleopolyhedrovirus gp64.

gp64 is the major envelope glycoprotein in the budded form of Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV). gp64 is essential for AcMNPV infection, as it mediates penetration of budded virus into host cells via the endocytic pathway. In this study, we used site-directed mutagenesis to map the positions of the N-linked glycans on AcMNPV gp64, characterize their structures, and evaluate their influence on gp64 function. We found that four of the five consensus N-glycosylation sites in gp64 are used, and we mapped the positions of those sites to amino acids 198, 355, 385, and 426 in the polypeptide chain. Endoglycosidase H sensitivity assays showed that N-linked glycans located at different positions are processed to various degrees. Lectin blotting analyses showed that each N-linked glycan on gp64 contains alpha-linked mannose, all but one contains alpha-linked fucose, and none contains detectable beta-linked galactose or alpha2,6-linked sialic acid. The amounts of infectious progeny produced by AcMNPV mutants lacking one, two, or three N-linked glycans on gp64 were about 10- to 100-fold lower than wild-type levels. This reduction did not correlate with reductions in the expression, transport, or inherent fusogenic activity of the mutant gp64s or in the gp64 content of mutant budded virus particles. However, all of the mutant viruses bound more slowly than the wild type. Therefore, elimination of one or more N-glycosylation sites in AcMNPV gp64 impairs binding of budded virus to the cell, which explains why viruses containing these mutant forms of gp64 produce less infectious progeny.

Animals↗

PubMed1986