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Russell J. Howard

Researcher at Maxygen

Publications -  127
Citations -  10053

Russell J. Howard is an academic researcher from Maxygen. The author has contributed to research in topics: Plasmodium falciparum & Antigen. The author has an hindex of 53, co-authored 127 publications receiving 9855 citations. Previous affiliations of Russell J. Howard include Albert Einstein College of Medicine & National Institutes of Health.

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Journal ArticleDOI

Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes

Dror I. Baruch, +7 more
- 14 Jul 1995 - 
TL;DR: The cloning of two related PfEMP1 genes from the Malayan Camp parasite strain are described and the molecular basis for antigenic variation in malaria and adherence of infected erythrocytes to host cells can now be pursued.
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Applications of DNA shuffling to pharmaceuticals and vaccines.

Phillip A. Patten, +2 more
- 01 Dec 1997 - 
TL;DR: DNA shuffling technology has been significantly enhanced in the past year, extending its range of applications to small molecule pharmaceuticals, pharmaceutical proteins, gene therapy vehicles and transgenes, vaccines and evolved viruses for vaccines, and laboratory animal models.
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Identification of a strain-specific malarial antigen exposed on the surface of Plasmodium falciparum-infected erythrocytes.

J H Leech, +3 more
- 01 Jun 1984 - 
TL;DR: Strain-specific antigens identified with Camp and St. Lucia strains of P. falciparum were metabolically labeled with radioactive amino acids, indicating that they were of parasite origin rather than altered host components.
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Plasmodium falciparum erythrocyte membrane protein 1 is a parasitized erythrocyte receptor for adherence to CD36, thrombospondin, and intercellular adhesion molecule 1.

Dror I. Baruch, +4 more
- 16 Apr 1996 - 
TL;DR: A therapeutic approach to block or reverse adherence of PRBCs to host cell receptors can now be pursued with the identification of PfEMP1 as a malarial receptor for PRBC adherence to host proteins.
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Thrombospondin binds falciparum malaria parasitized erythrocytes and may mediate cytoadherence.

David D. Roberts, +8 more
- 01 Nov 1985 - 
TL;DR: Evidence is presented that the receptor for cytoadherence is the glycoprotein, thrombospondin, which may protect the parasite from splenic destruction and play a role in the pathogenesis of cerebral malaria.