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Edgar P. Heimer

Researcher at Hoffmann-La Roche

Publications -  67
Citations -  2538

Edgar P. Heimer is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Peptide & Peptide synthesis. The author has an hindex of 24, co-authored 67 publications receiving 2508 citations. Previous affiliations of Edgar P. Heimer include University of Maryland, Baltimore.

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Safety and immunogenicity in man of a synthetic peptide malaria vaccine against plasmodium falciparum sporozoites

TL;DR: This first synthetic peptide parenteral vaccine against a communicable disease tested in man is safe and stimulates biologically active antibodies, which encourage the development of improved vaccine formulations which, by enhancing immunogenicity, may lead to practical vaccines to assist in the control of falciparum malaria.
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Solid phase synthesis without repetitive acidolysis. Preparation of leucyl-alanyl-glycyl-valine using 9-fluorenylmethyloxycarbonylamino acids.

TL;DR: The utility of repetitive nonhydrolytic base cleavage of alpha-amino protective groups in solid phase peptide synthesis is shown by a preparation of the model tetrapeptide leucyl-alanyl-glycyl-valine on a p-benZyloxybenzyl ester polystyrene--1% divinylbenzene resin support.
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Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding

TL;DR: It is concluded that the CSVTCG repeat sequence is a crucial determinant of CD36 thrombospondin binding.
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Synthesis, biological activity and conformational analysis of cyclic GRF analogs.

TL;DR: Conformational analysis (circular dichroism and molecular dynamics calculations based on NOE-derived distance constraints) demonstrated that cyclo8,12[Asp8,Ala15]-GRF(1-29)-NH2 contains a long alpha-helical segment even in aqueous solution.
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Applications of BOP reagent in solid phase synthesis. II: Solid phase side-chain to side-chain cyclizations using BOP reagent

TL;DR: In this article, a kinetic study was carried out to evaluate the rate of solid phase side-chain to sidechain cyclization of Asp3 to Lys12 in the model peptide-resin.