John C. Kappes

Performance of Rilpivirine-Based Hydrophobic Tags and PROTACs Directed Against HIV-1 Reverse Transcriptase

The paper evaluates rilpivirine-based hydrophobic tags and PROTACs for HIV-1 RT degradation, finding that PEG4-Ad shows low nanomolar potency but limited efficacy against resistance mutations.

Characterization of full-length and cytoplasmic tail-truncated envelope glycoproteins incorporated into human immunodeficiency virus (HIV-1) virions and virus-like particles

This study investigates how truncations of the HIV-1 Env cytoplasmic tail affect Env cleavage, incorporation into virions, and antibody neutralization.

Correcting mutant CFTR with a stabilizing nanobody reveals a novel active conformation of the channel

This study uses a nanobody to stabilize mutant CFTR, revealing a novel active conformation and improving its function in cystic fibrosis.

Analysis of glycosylation and disulfide bonding of wild-type SARS-CoV-2 spike glycoprotein

The paper analyzes glycosylation and disulfide bonding of wild-type SARS-CoV-2 spike glycoprotein, finding that Golgi processing leads to complex N-glycans and partial infectivity in a Cys15Phe mutant.

Functional and Highly Crosslinkable HIV-1 Envelope Glycoproteins Enriched in a Pretriggered Conformation

The paper describes the engineering of HIV-1 Env variants enriched in a pretriggered conformation, which are more stable and crosslinkable, aiding in structural and immunogenic studies.

Asymmetric structures and conformational plasticity of the uncleaved full-length human immunodeficiency virus (HIV-1) envelope glycoprotein trimer

This study investigates the conformational plasticity of the uncleaved HIV-1 Env trimer and its implications for antibody recognition and Env cleavage.

Structural insights into the conformational plasticity of the full-length trimeric HIV-1 envelope glycoprotein precursor

This study uses cryo-EM to reveal two conformational states of the HIV-1 Env precursor, explaining its plasticity and implications for immune response.