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FEBS Open Bio|June 12, 2014
Changed membrane integration and catalytic site conformation are two mechanisms behind the increased Aβ42/Aβ40 ratio by presenilin 1 familial Alzheimer-linked mutationsJohanna Wanngren, Patricia Lara, Karin Ojemalm, et al.
European Journal of Pediatrics|November 7, 2019
Celiac disease and complement activation in response to Streptococcus pneumoniaeAnna Röckert Tjernberg, Hanna Woksepp, Kerstin Sandholm, et al.
The FEBS Journal|January 1, 2020
Glycan biomarkers for Alzheimer disease correlate with T-tau and P-tau in cerebrospinal fluid in subjective cognitive impairmentSophia Schedin-Weiss, Stefan Gaunitz, Ping Sui, et al.
Progress in Neuro-Psychopharmacology & Biological Psychiatry|August 29, 2025
A plasma protein profile of antidepressant response to omega-3 fatty acidsJesper Lindahl, Miranda Stiernborg, Filip Ventorp, et al.
The Journal of Biological Chemistry|May 29, 1999
Endogenous proteins controlling amyloid beta-peptide polymerization. Possible implications for beta-amyloid formation in the central nervous system and in peripheral tissuesB Bohrmann, L Tjernberg, P Kuner, et al.
Journal of Alzheimer'S Disease : JAD|April 14, 2020
Proteomics Time-Course Study of App Knock-In Mice Reveals Novel Presymptomatic Aβ42-Induced Pathways to Alzheimer's Disease PathologySophia Schedin-Weiss, Per Nilsson, Anna Sandebring-Matton, et al.
Molecular and Cellular Biology|September 21, 2001
Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivoE Martinez, V B Palhan, A Tjernberg, et al.
The Journal of Biological Chemistry|July 20, 2006
Degradation of the amyloid beta-protein by the novel mitochondrial peptidasome, PrePAnnelie Falkevall, Nyosha Alikhani, Shashi Bhushan, et al.
Brain, Behavior, and Immunity|March 3, 2024
Omega-3 fatty acids for inflamed depression - A match/mismatch studyKlara Suneson, Gustav Söderberg Veibäck, Jesper Lindahl, et al.
Thrombosis and Haemostasis|December 2, 2006
Differential effects of the loss of intrachain- versus interchain-disulfide bonds in the cystine-knot domain of von Willebrand factor on the clinical phenotype of von Willebrand diseasePernilla Tjernberg, Hans L Vos, Caroline C Spaargaren-van Riel, et al.
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