J
John E. Donelson
Researcher at Howard Hughes Medical Institute
Publications - 38
Citations - 1609
John E. Donelson is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Gene & Complementary DNA. The author has an hindex of 23, co-authored 38 publications receiving 1587 citations. Previous affiliations of John E. Donelson include University of Iowa Hospitals and Clinics & University of Iowa.
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Journal ArticleDOI
The African trypanosome genome.
TL;DR: Analysis of a test microarray of 400 cDNAs and small random genomic DNA fragments probed with RNAs from two developmental stages of T. brucei demonstrates that the microarray technology can be used to identify batteries of genes differentially expressed during the various life cycle stages of this parasite.
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cDNA expressed sequence tags of Trypanosoma brucei rhodesiense provide new insights into the biology of the parasite.
Najib M. El-Sayed,Clara M. Alarcon,John S. Beck,Val C. Sheffield,John E. Donelson,John E. Donelson +5 more
TL;DR: These cDNA ESTs provide new avenues of research for exploring both the novel trypanosome-specific genes and the genome organization of this parasite, as well as a resource for identifying trypanOSome homologs to genes expressed in other organisms.
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Multiple mechanisms of immune evasion by African trypanosomes
TL;DR: Evidence is found for trypansome protein similar to a surface protease of Leishmania that plays a role in resistance to complement-mediated lysis in African trypanosomes.
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A differentially expressed gene family encoding "amastin," a surface protein of Trypanosoma cruzi amastigotes.
TL;DR: A new family of closely related glycoproteins, collectively called amastins, has been found on the surface of the amastigote form of Trypanosoma cruzi, indicating that the stage-specific amastin mRNA levels are determined by a post-transcriptional mechanism.
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A novel flagellar Ca2+-binding protein in trypanosomes.
TL;DR: A 24-kDa protein of Trypanosoma cruzi, the protozoan parasite that causes Chagas' disease, is recognized by antisera from both humans and experimental animals infected with this organism and suggests that it participates in molecular processes associated with the high motility of the parasite.