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A spectrum of clinically-identified cysteine mutations in fibulin-3 (EFEMP1) highlight its disulfide bonding complexity and potential to induce stress response activation.

Autor: Collier GE; Department of Ophthalmology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, Texas, 75390, United States., Hulleman JD; Department of Ophthalmology and Visual Neurosciences, University of Minnesota, 2001 6 St. SE, Minneapolis, Minnesota, 55455, United States.

Publikováno v: BioRxiv : the preprint server for biology [bioRxiv] 2024 Jul 23. Date of Electronic Publication: 2024 Jul 23.

The Fifth Epidermal Growth Factor-Like Domain of Thrombomodulin does not have an Epidermal Growth Factor-Like Disulfide Bonding Pattern

Autor: White, Christopher E., Hunter, Michael J., Meininger, David P., Garrod, Siv, Komives, Elizabeth A.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 1996 Sep . 93(19), 10177-10182.

Externí odkaz: https://www.jstor.org/stable/40358

DR5 disulfide bonding as a sensor and effector of protein folding stress.

Autor: Law ME, Dulloo ZM, Eggleston SR, Takacs GP, Alexandrow GM, Wang M, Su H, Forsyth B, Chiang CW, Sharma A, Kanumuri SRR, Guryanova OA, Harrison JK, Tirosh B, Castellano RK, Law BK

Publikováno v: BioRxiv : the preprint server for biology [bioRxiv] 2024 Mar 07. Date of Electronic Publication: 2024 Mar 07.

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