Jason Gorman

National Institutes of Health - Vaccine Research Center

Bethesda, MD 20892-9806

United States

SCHOLARLY PAPERS

5

DOWNLOADS

140

TOTAL CITATIONS

7

Scholarly Papers (5)

1.

Structure-Based Design with Tag-Based Purification and In-Process Biotinylation Enable Streamlined Development of SARS-CoV-2 Spike Molecular Probes

Number of pages: 51 Posted: 21 Jul 2020
National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, Columbia University - Department of Biochemistry and Molecular Biophysics, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, Frederick National Laboratory for Cancer Research - Electron Microscopy Laboratory, National Institutes of Health (NIH) - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, Columbia University - Department of Biochemistry and Molecular Biophysics, National Institutes of Health - Vaccine Research Center, University of Kansas - Bioengineering Graduate Program, University of Kansas - Department of Pharmaceutical Chemistry, Columbia University - Aaron Diamond AIDS Research Center, University of Kansas - Department of Pharmaceutical Chemistry, University of Kansas - Department of Pharmaceutical Chemistry, University of Kansas - Department of Pharmaceutical Chemistry, University of Kansas - Department of Pharmaceutical Chemistry, Columbia University - Aaron Diamond AIDS Research Center, University of Kansas - Department of Pharmaceutical Chemistry, Columbia University - Aaron Diamond AIDS Research Center, Columbia University - Aaron Diamond AIDS Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, University of Kansas - Bioengineering Graduate Program, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center and National Institutes of Health - Vaccine Research Center
Downloads 43 (914,165)
Citation 3

Abstract:

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antibody, biotinylated probe, COVID-19, HRV3C protease, single-chain Fc, structurebased design

2.

Cryo-EM Structures Delineate a pH-Dependent Switch that Mediates Endosomal Positioning of SARS-CoV-2 Spike Receptor-Binding Domains

Number of pages: 65 Posted: 26 Oct 2020
National Institutes of Health - Vaccine Research Center, Frederick National Laboratory for Cancer Research - Electron Microscopy Laboratory, National Institutes of Health - Vaccine Research Center, Columbia University - Department of Biochemistry and Molecular Biophysics, Columbia University - Department of Biochemistry and Molecular Biophysics, National Institutes of Health - Vaccine Research Center, Columbia University - Department of Biochemistry and Molecular Biophysics, Columbia University - Department of Biochemistry and Molecular Biophysics, Johns Hopkins University - Department of Biology, Columbia University - Department of Biochemistry and Molecular Biophysics, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, Frederick National Laboratory for Cancer Research - Electron Microscopy Laboratory, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, Columbia University - Aaron Diamond AIDS Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, Columbia University - Department of Chemistry, Columbia University - Aaron Diamond AIDS Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center and National Institutes of Health - Vaccine Research Center
Downloads 31 (1,035,187)
Citation 2

Abstract:

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ACE2 receptor, endosomal entry, pH-dependent switch, receptor-binding domain (RBD), structural rearrangement, type 1 fusion machine

3.

Structure of Antibody CAP256-VRC26.25 in Complex with HIV-1 Envelope Reveals a Combined Mode of Trimer-Apex Recognition

Number of pages: 43 Posted: 05 Aug 2019
National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - Vaccine Research Center, Government of the United States of America - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Health Laboratory Services (NHLS) - Centre for HIV and STIs, University of the Witwatersrand, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - Vaccine Research Center and National Institutes of Health - Vaccine Research Center
Downloads 30 (1,046,374)
Citation 1

Abstract:

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broadly neutralizing antibody, HIV-1 envelope trimer, multidonor antibody class, PCT64, PG9, PGDM1400, PGT145, tyrosine sulfation, V1V2-apex recognition

4.

Anti-V2 Antibodies Virus Vulnerability Revealed by Envelope V1 Deletion in HIV Vaccine Candidates

Number of pages: 87 Posted: 21 Oct 2020
National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Immune Biology of Retroviral Infection Section, National Institutes of Health (NIH) - Section on Intercellular Interactions, Advanced Bioscience Laboratories, Advanced Bioscience Laboratories, New York University (NYU) - NYU Langone Health, New York University (NYU) - NYU Langone Health, Government of the United States of America - Henry M. Jackson Foundation for the Advancement of Military Medicine, Government of the United States of America - Henry M. Jackson Foundation for the Advancement of Military Medicine, Walter Reed Army Institute of Research - U.S. Military HIV Research Program, National Institutes of Health (NIH) - Laboratory of Immunoregulation, National Institutes of Health (NIH) - Laboratory of Immunoregulation, Walter Reed Army Institute of Research - U.S. Military HIV Research Program, Government of the United States of America - Henry M. Jackson Foundation for the Advancement of Military Medicine, Duke University - Division of Surgical Sciences, Duke University - Division of Surgical Sciences, National Institutes of Health (NIH) - Structural Biology Section, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - ImmunoTechnology Section, National Institutes of Health (NIH) - ImmunoTechnology Section, National Institutes of Health (NIH) - ImmunoTechnology Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Institutes of Health (NIH) - Laboratory of Immunoregulation, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, National Cancer Institute - Animal Models and Retroviral Vaccines Section, Duke University - Department of Surgery, Duke University - Division of Surgical Sciences, Duke University - Medical Center, Duke University - Duke Human Vaccine Institute, National Cancer Institute at Frederick - Human Retrovirus Section, National Cancer Institute at Frederick - Human Retrovirus Pathogenesis Section, National Cancer Institute at Frederick - Human Retrovirus Section, National Cancer Institute - Biostatistics and Data Management Section, Frederick National Laboratory - AIDS and Cancer Virus Program, Frederick National Laboratory - AIDS and Cancer Virus Program, Frederick National Laboratory - AIDS and Cancer Virus Program, Frederick National Laboratory for Cancer Research - AIDS and Cancer Virus Program, Walter Reed Army Institute of Research - U.S. Military HIV Research Program, National Institutes of Health (NIH) - Laboratory of Immunoregulation, National Institutes of Health (NIH) - Laboratory of Immunoregulation, Duke University - Division of Surgical Sciences, National Institutes of Health (NIH) - Section on Intercellular Interactions, National Cancer Institute - Immune Biology of Retroviral Infection Section, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - ImmunoTechnology Section, Walter Reed Army Institute of Research - U.S. Military HIV Research Program, New York University (NYU) - NYU Langone Health and Medical University of Bialystok - Centre for Bioinformatics and Data Analysis
Downloads 20 (1,167,001)

Abstract:

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HIV, SIV, V1/V2, V1, ALVAC

5.

A Structure-Based Matrix Approach Yields Improved VRC01-Class Antibodies for HIV-1 Therapy and Prevention

Number of pages: 41 Posted: 05 Oct 2020
National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - Laboratory of Immunoregulation, National Institutes of Health (NIH) - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, Government of the United States of America - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - Vaccine Research Center, Independent, National Institutes of Health - Vaccine Research Center, National Institutes of Health (NIH) - Vaccine Research Center, National Institutes of Health - Viral Pathogenesis Section, National Institutes of Health - Vaccine Research Center and National Institutes of Health - Vaccine Research Center
Downloads 16 (1,215,873)
Citation 1

Abstract:

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antibody VRC01, broadly neutralizing antibody, HIV-1 envelope trimer, polyreactivity, prophylaxis, treatment