L
Larry D. Ward
Researcher at Walter and Eliza Hall Institute of Medical Research
Publications - 54
Citations - 2356
Larry D. Ward is an academic researcher from Walter and Eliza Hall Institute of Medical Research. The author has contributed to research in topics: Peptide sequence & Gel electrophoresis. The author has an hindex of 26, co-authored 54 publications receiving 2302 citations. Previous affiliations of Larry D. Ward include Australian National University & Royal Melbourne Hospital.
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Journal ArticleDOI
Interleukin-6: Structure-function relationships
TL;DR: A tentative model for the IL‐6 hexameric receptor ligand complex is presented and discussed with respect to the mechanism of action of the other members of theIL‐6 family of cytokines.
Journal ArticleDOI
High affinity interleukin-6 receptor is a hexameric complex consisting of two molecules each of interleukin-6, interleukin-6 receptor, and gp-130.
Larry D. Ward,Geoffrey J. Howlett,G. Discolo,Kiyoshi Yasukawa,Annet Hammacher,Robert L. Moritz,Richard J. Simpson +6 more
TL;DR: Using a combination of size-exclusion chromatography and analytical ultracentrifugation analysis, in the low affinity receptor complex, IL-6 was shown to bind sIL-6R in a stoichiometric ratio of 1:1, whereas the high affinity ternary complex is hexameric consisting of two molecules each of IL- 6, sIL -6R, and sgp-130.
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A major binding protein for leukemia inhibitory factor in normal mouse serum: identification as a soluble form of the cellular receptor.
Meredith J. Layton,Bronwyn A. Cross,Donald Metcalf,Larry D. Ward,Richard J. Simpson,Nicos A. Nicola +5 more
TL;DR: The purified LIF-binding protein (LBP) is a glycoprotein with an apparent molecular mass of 90 kDa that specifically binds 125I-labeled murine LIF with an affinity comparable to that of the low-affinity cellular LIF receptor (Kd = 600 pM).
Journal Article
The group III allergen from the house dust mite Dermatophagoides pteronyssinus is a trypsin-like enzyme.
TL;DR: Mite trypsin underwent autolysis and the N-terminal sequences of two fragments were found to be ALAGEXPYQI and NNQVXGI respectively, which indicate that mitetrypsin is a major allergen corresponding to the previously describedAllergen, Der p III.
Journal ArticleDOI
Cloning sequencing of Lol pI, the major allergenic protein of rye‐grass pollen
Irwin J. Griffith,Penelope M. C. Smith,Joanne Pollock,Piyada Theerakulpisut,A. Avjioglu,Sean Davies,Terryn Hough,Mohan Singh,Richard J. Simpson,Larry D. Ward,R. Bruce Knox +10 more
TL;DR: Molecular cloning of Lol pI provides a molecular genetic approach to study the structure—function relationship of allergens and shows recognition by specific IgE antibodies present in sera of grass pollen‐allergic subjects.