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Jean-Philippe Julien

Jean-Philippe Julien

D-Index & Metrics

Microbiology

D-Index
57
Citations
17704
World Ranking
3527
National Ranking
100

Overview

Jean-Philippe Julien is affiliated with the University of Toronto in Canada and specializes in fields related to Medicine, Immunology and Microbiology, and Biochemistry, Genetics and Molecular Biology. Their research spans multiple subfields including Public Health, Environmental and Occupational Health, Immunology, Molecular Biology, Infectious Diseases, and Radiology, Nuclear Medicine and Imaging.

The scientist's work focuses on several specific topics, such as Malaria Research and Control, Monoclonal and Polyclonal Antibodies Research, HIV Research and Treatment, SARS-CoV-2 and COVID-19 Research, Trypanosoma species research and implications, vaccines and immunoinformatics approaches, and Mosquito-borne diseases and control.

Among their recent published papers are the following:

  • De novo protein design enables the precise induction of RSV-neutralizing antibodies (2020, Science)
  • GPC2-CAR T cells tuned for low antigen density mediate potent activity against neuroblastoma without toxicity (2021, Cancer Cell)
  • Evolution of protective human antibodies against Plasmodium falciparum circumsporozoite protein repeat motifs (2020, Nature Medicine)
  • A versatile soluble siglec scaffold for sensitive and quantitative detection of glycan ligands (2020, Nature Communications)
  • Multivalency transforms SARS-CoV-2 antibodies into ultrapotent neutralizers (2021, Nature Communications)

The scientist frequently publishes in venues including bioRxiv (Cold Spring Harbor Laboratory), Immunity, eLife, Zenodo (CERN European Organization for Nuclear Research), and Nature Communications.

Frequent co-authors in their work include Iga Kucharska, John L. Rubinstein, Katherine Prieto, Danton Ivanochko, and Edurne Rujas.

Best Publications

  • Broad neutralization coverage of HIV by multiple highly potent antibodies

    Laura M. Walker;Michael Huber;Michael Huber;Katie J. Doores;Katie J. Doores;Emilia Falkowska;Emilia Falkowska

  • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9

    Jason S. McLellan;Marie Pancera;Chris Carrico;Jason Gorman

  • A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but Not Non-Neutralizing Antibodies

    Rogier W. Sanders;Rogier W. Sanders;Ronald Derking;Albert Cupo;Jean-Philippe Julien

  • Crystal structure of a soluble cleaved HIV-1 envelope trimer.

    Jean-Philippe Julien;Jean-Philippe Julien;Albert Cupo;Devin Sok;Devin Sok;Robyn L. Stanfield;Robyn L. Stanfield

  • Rational HIV immunogen design to target specific germline B cell receptors

    Joseph Jardine;Jean Philippe Julien;Jean Philippe Julien;Sergey Menis;Takayuki Ota

  • A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield

    Robert Pejchal;Katie J. Doores;Katie J. Doores;Laura M. Walker;Reza Khayat

  • Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer

    Dmitry Lyumkis;Jean-Philippe Julien;Natalia de Val;Albert Cupo

  • HIV-1 neutralizing antibodies induced by native-like envelope trimers

    Rogier W. Sanders;Rogier W. Sanders;Marit J. Van Gils;Ronald Derking;Devin Sok;Devin Sok

  • HIV-1 broadly neutralizing antibody precursor B cells revealed by germline-targeting immunogen.

    Joseph G. Jardine;Daniel W. Kulp;Colin Havenar-Daughton;Anita Sarkar

  • Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120

    Leopold Kong;Jeong Hyun Lee;Katie J Doores;Katie J Doores;Katie J Doores;Charles D Murin

  • Recombinant HIV envelope trimer selects for quaternary-dependent antibodies targeting the trimer apex.

    Devin Sok;Marit J. van Gils;Matthias Pauthner;Jean-Philippe Julien

  • Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans.

    Jean-Philippe Julien;Devin Sok;Reza Khayat;Jeong Hyun Lee

  • Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers.

    Claudia Blattner;Jeong Hyun Lee;Kwinten Sliepen;Ronald Derking

  • Immunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-neutralizing Epitopes

    Steven W. de Taeye;Gabriel Ozorowski;Alba Torrents de la Peña;Miklos Guttman

  • Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9.

    Jean-Philippe Julien;Jeong Hyun Lee;Albert Cupo;Charles D. Murin

  • A Native-Like SOSIP.664 Trimer Based on an HIV-1 Subtype B env Gene

    Pavel Pugach;Gabriel Ozorowski;Albert Cupo;Rajesh Ringe

  • The structural basis of modified nucleosome recognition by 53BP1

    Marcus D Wilson;Samir Benlekbir;Amélie Fradet-Turcotte;Amélie Fradet-Turcotte;Alana Sherker;Alana Sherker

  • A Broadly Neutralizing Antibody Targets the Dynamic HIV Envelope Trimer Apex via a Long, Rigidified, and Anionic β-Hairpin Structure

    Jeong Hyun Lee;Jeong Hyun Lee;Raiees Andrabi;Raiees Andrabi;Ching Yao Su;Anila Yasmeen

  • Structural Evolution of Glycan Recognition by a Family of Potent HIV Antibodies

    Fernando Garces;Devin Sok;Leopold Kong;Leopold Kong;Ryan McBride

  • The Effects of Somatic Hypermutation on Neutralization and Binding in the PGT121 Family of Broadly Neutralizing HIV Antibodies

    Devin Sok;Uri Laserson;Uri Laserson;Jonathan Laserson;Yi-Ping Liu

Frequent Co-Authors

Ian A. Wilson
Ian A. Wilson Scripps Research Institute
Rogier W. Sanders
Rogier W. Sanders University of Amsterdam
Andrew B. Ward
Andrew B. Ward Scripps Research Institute
Dennis R. Burton
Dennis R. Burton Scripps Research Institute
John P. Moore
John P. Moore Cornell University
Devin Sok
Devin Sok Scripps Research Institute
William R. Schief
William R. Schief Scripps Research Institute
Emil F. Pai
Emil F. Pai University of Toronto
Per Johan Klasse
Per Johan Klasse Cornell University
Robyn L. Stanfield
Robyn L. Stanfield Scripps Research Institute

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