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Loïc Martin

Researcher at Scripps Research Institute

Publications -  44
Citations -  1961

Loïc Martin is an academic researcher from Scripps Research Institute. The author has contributed to research in topics: Epitope & Chemokine. The author has an hindex of 25, co-authored 39 publications receiving 1857 citations. Previous affiliations of Loïc Martin include Peking University.

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Rational design of a CD4 mimic that inhibits HIV-1 entry and exposes cryptic neutralization epitopes

TL;DR: A 27-amino acid CD4 mimic, CD4M33, is designed that presents optimal interactions with gp120 and binds to viral particles and diverse HIV-1 envelopes with CD4-like affinity and possesses functional properties of CD4, including the ability to unmask conserved neutralization epitopes of gp120 that are cryptic on the unbound glycoprotein.
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Rational engineering of a miniprotein that reproduces the core of the CD4 site interacting with HIV-1 envelope glycoprotein.

TL;DR: In this article, the side chains of nine residues of CD4, central in the binding to HIV-1 envelope glycoprotein (gp120), were transferred to a structurally homologous region of the scorpion toxin scaffold.
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Purification, Characterization, and Immunogenicity of a Soluble Trimeric Envelope Protein Containing a Partial Deletion of the V2 Loop Derived from SF162, an R5-Tropic Human Immunodeficiency Virus Type 1 Isolate

TL;DR: The purification of this protein to homogeneity, its characterization as trimer, and its ability to induce primary isolate-neutralizing responses in rhesus macaques highlight a potential role for the trimeric o-gp140SF162ΔV2 Env immunogen in a successful HIV vaccine.
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Scorpion-Toxin Mimics of CD4 in Complex with Human Immunodeficiency Virus gp120: Crystal Structures,Molecular Mimicry, and Neutralization Breadth

TL;DR: X-ray crystallography is used to characterize atomic-level details of gp120 with this transplant, CD4M33, and define measures that quantify molecular mimicry as a function of evolutionary distance, and suggest how such evaluations might be useful in developing mimetic antagonists with increased neutralization breadth.
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A global benchmark study using affinity-based biosensors

Rebecca L. Rich, +150 more
TL;DR: To explore the variability in biosensor studies, 150 participants from 20 countries were given the same protein samples and asked to determine kinetic rate constants, demonstrating that when this biosensor assay was designed and executed appropriately, the reported rate constants were consistent, and independent of which protein was immobilized and which biosensor was used.