Site-specific crosslinking reveals Phosphofructokinase-L inhibition drives self-assembly and attenuation of protein interactions.

Sivadas, Athira; McDonald, Eli Fritz; Shuster, Sydney O; Davis, Caitlin M; Plate, Lars

Sivadas, Athira; McDonald, Eli Fritz; Shuster, Sydney O; Davis, Caitlin M; Plate, Lars.

Afiliación

Sivadas A; Department of Chemistry, Vanderbilt University, Nashville, TN, USA.
McDonald EF; Department of Chemistry, Vanderbilt University, Nashville, TN, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA.
Shuster SO; Department of Chemistry, Yale University, New Haven, CT, USA.
Davis CM; Department of Chemistry, Yale University, New Haven, CT, USA.
Plate L; Department of Chemistry, Vanderbilt University, Nashville, TN, USA; Department of Biological Sciences, Vanderbilt University, Nashville, TN, USA; Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN, USA. Electronic address: lars.plate@vanderbilt.

Adv Biol Regul ; 90: 100987, 2023 Dec.

Article en En | MEDLINE | ID: mdl-37806136

Asunto(s)

Fosfofructoquinasa-1; Fosfofructoquinasas; Humanos; Fosfofructoquinasa-1/genética; Fosfofructoquinasa-1/metabolismo; Hígado/metabolismo; Citratos; Ácido Cítrico

Texto completo

Imprimir

XML

PubMed Links

Buscar en Google

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Fosfofructoquinasa-1 / Fosfofructoquinasas Límite: Humans Idioma: En Revista: Adv Biol Regul Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo

Imprimir

XML

PubMed Links

Buscar en Google