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Andréa Dessen

Researcher at University of Grenoble

Publications -  125
Citations -  9716

Andréa Dessen is an academic researcher from University of Grenoble. The author has contributed to research in topics: Peptidoglycan & Penicillin binding proteins. The author has an hindex of 47, co-authored 120 publications receiving 9040 citations. Previous affiliations of Andréa Dessen include University of Washington & French Alternative Energies and Atomic Energy Commission.

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Atomic structure of the ectodomain from HIV-1 gp41

TL;DR: X-ray crystallography determines the structure of the protease-resistant part of a gp41 ectodomain solubilized with a trimeric GCN4 coiled coil in place of the amino-terminal fusion peptide, and suggests a common mechanism for initiating fusion.
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Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis.

TL;DR: The three-dimensional structures of wild-type and mutant InhA revealed that drug resistance is directly related to a perturbation in the hydrogen-bonding network that stabilizes NADH binding.
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Penicillin Binding Proteins: key players in bacterial cell cycle and drug resistance processes

TL;DR: Structural, functional and biological features of penicillin-binding proteins, albeit having initially been identified several decades ago, are now being aggressively pursued as highly attractive targets for the development of novel antibiotherapies.
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Structural basis for membrane fusion by enveloped viruses

TL;DR: This review focuses on the HIV-1 gp41 membrane fusion protein and discusses the structural similarities of viral membrane fusion proteins from diverse families, suggesting that they have all evolved to use a similar strategy to promote fusion of viral and cellular membranes.
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X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II.

TL;DR: Details of a predicted salt bridge between lysine DRbeta71 and aspartic acid at the P4 peptide position suggest how it may participate in both antigen binding and TCR activation.