{"entity": "researcher", "timestamp": "2026-07-22T17:16:37.282Z", "family": "Haytural", "given": "Hazal", "initials": "H", "orcid": "0000-0002-6805-6989", "affiliations": [], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/863ccd2db6794dff8e36a313075e4ea2.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/863ccd2db6794dff8e36a313075e4ea2"}}, "publications": [{"entity": "publication", "iuid": "1d95029adc794903bf11503ddeab9127", "links": {"self": {"href": "https://publications.scilifelab.se/publication/1d95029adc794903bf11503ddeab9127.json"}, "display": {"href": "https://publications.scilifelab.se/publication/1d95029adc794903bf11503ddeab9127"}}, "title": "Insights into the changes in the proteome of Alzheimer disease elucidated by a meta-analysis.", "authors": [{"family": "Haytural", "given": "Hazal", "initials": "H", "orcid": "0000-0002-6805-6989", "researcher": {"href": "https://publications.scilifelab.se/researcher/863ccd2db6794dff8e36a313075e4ea2.json"}}, {"family": "Benfeitas", "given": "Rui", "initials": "R"}, {"family": "Schedin-Weiss", "given": "Sophia", "initials": "S"}, {"family": "Bereczki", "given": "Erika", "initials": "E"}, {"family": "Rezeli", "given": "Melinda", "initials": "M"}, {"family": "Unwin", "given": "Richard D", "initials": "RD"}, {"family": "Wang", "given": "Xusheng", "initials": "X"}, {"family": "Dammer", "given": "Eric B", "initials": "EB", "orcid": "0000-0003-2947-7606", "researcher": {"href": "https://publications.scilifelab.se/researcher/026547f280c8451586bf92ab028090f7.json"}}, {"family": "Johnson", "given": "Erik C B", "initials": "ECB"}, {"family": "Seyfried", "given": "Nicholas T", "initials": "NT", "orcid": "0000-0002-4507-624X", "researcher": {"href": "https://publications.scilifelab.se/researcher/9c940f8678724c38b1c6e98ea1b335e4.json"}}, {"family": "Winblad", "given": "Bengt", "initials": "B", "orcid": "0000-0002-0011-1179", "researcher": {"href": "https://publications.scilifelab.se/researcher/73185a13ca474153b66415e6a2dfff0f.json"}}, {"family": "Tijms", "given": "Betty M", "initials": "BM", "orcid": "0000-0002-2612-1797", "researcher": {"href": "https://publications.scilifelab.se/researcher/74734f1c78e840b0aaadd74cc2c1ae9f.json"}}, {"family": "Visser", "given": "Pieter Jelle", "initials": "PJ"}, {"family": "Frykman", "given": "Susanne", "initials": "S"}, {"family": "Tjernberg", "given": "Lars O", "initials": "LO", "orcid": "0000-0001-6889-4950", "researcher": {"href": "https://publications.scilifelab.se/researcher/35d7bd25361f4e08a7223926311b399a.json"}}], "type": "journal article", "published": "2021-12-03", "journal": {"title": "Sci Data", "issn": "2052-4463", "volume": "8", "issue": "1", "pages": "312", "issn-l": "2052-4463"}, "abstract": "Mass spectrometry (MS)-based proteomics is a powerful tool to explore pathogenic changes of a disease in an unbiased manner and has been used extensively in Alzheimer disease (AD) research. Here, by performing a meta-analysis of high-quality proteomic studies, we address which pathological changes are observed consistently and therefore most likely are of great importance for AD pathogenesis. We retrieved datasets, comprising a total of 21,588 distinct proteins identified across 857 postmortem human samples, from ten studies using labeled or label-free MS approaches. Our meta-analysis findings showed significant alterations of 757 and 1,195 proteins in AD in the labeled and label-free datasets, respectively. Only 33 proteins, some of which were associated with synaptic signaling, had the same directional change across the individual studies. However, despite alterations in individual proteins being different between the labeled and the label-free datasets, several pathways related to synaptic signaling, oxidative phosphorylation, immune response and extracellular matrix were commonly dysregulated in AD. These pathways represent robust changes in the human AD brain and warrant further investigation.", "doi": "10.1038/s41597-021-01090-8", "pmid": "34862388", "labels": {"Bioinformatics Support, Infrastructure and Training": "Collaborative", "Bioinformatics Support and Infrastructure": "Collaborative", "Bioinformatics Support for Computational Resources": "Service", "Bioinformatics (NBIS)": "Collaborative"}, "xrefs": [{"db": "pii", "key": "10.1038/s41597-021-01090-8"}, {"db": "pmc", "key": "PMC8642431"}], "notes": [], "created": "2021-12-06T08:17:14.664Z", "modified": "2024-01-16T13:48:38.002Z"}, {"entity": "publication", "iuid": "55f4ed329d83487cb94e14dbd80050fc", "links": {"self": {"href": "https://publications.scilifelab.se/publication/55f4ed329d83487cb94e14dbd80050fc.json"}, "display": {"href": "https://publications.scilifelab.se/publication/55f4ed329d83487cb94e14dbd80050fc"}}, "title": "The Proteome of the Dentate Terminal Zone of the Perforant Path Indicates Presynaptic Impairment in Alzheimer Disease.", "authors": [{"family": "Haytural", "given": "Hazal", "initials": "H", "orcid": "0000-0002-6805-6989", "researcher": {"href": "https://publications.scilifelab.se/researcher/863ccd2db6794dff8e36a313075e4ea2.json"}}, {"family": "Mermelekas", "given": "Georgios", "initials": "G"}, {"family": "Emre", "given": "Ceren", "initials": "C"}, {"family": "Nigam", "given": "Saket Milind", "initials": "SM"}, {"family": "Carroll", "given": "Steven L", "initials": "SL"}, {"family": "Winblad", "given": "Bengt", "initials": "B"}, {"family": "Bogdanovic", "given": "Nenad", "initials": "N"}, {"family": "Barthet", "given": "Ga\u00ebl", "initials": "G", "orcid": "0000-0003-4025-1616", "researcher": {"href": "https://publications.scilifelab.se/researcher/405b338627c64906b897ff3b394ce531.json"}}, {"family": "Granholm", "given": "Ann-Charlotte", "initials": "AC"}, {"family": "Orre", "given": "Lukas M", "initials": "LM", "orcid": "0000-0002-0384-1003", "researcher": {"href": "https://publications.scilifelab.se/researcher/7b4e49a93b0143db88059c4d1e9fdc59.json"}}, {"family": "Tjernberg", "given": "Lars O", "initials": "LO"}, {"family": "Frykman", "given": "Susanne", "initials": "S"}], "type": "journal article", "published": "2020-01-00", "journal": {"volume": "19", "issn": "1535-9484", "issue": "1", "pages": "128-141", "title": "Mol. Cell Proteomics", "issn-l": "1535-9476"}, "abstract": "Synaptic dysfunction is an early pathogenic event in Alzheimer disease (AD) that contributes to network disturbances and cognitive decline. Some synapses are more vulnerable than others, including the synapses of the perforant path, which provides the main excitatory input to the hippocampus. To elucidate the molecular mechanisms underlying the dysfunction of these synapses, we performed an explorative proteomic study of the dentate terminal zone of the perforant path. The outer two-thirds of the molecular layer of the dentate gyrus, where the perforant path synapses are located, was microdissected from five subjects with AD and five controls. The microdissected tissues were dissolved and digested by trypsin. Peptides from each sample were labeled with different isobaric tags, pooled together and pre-fractionated into 72 fractions by high-resolution isoelectric focusing. Each fraction was then analyzed by liquid chromatography-mass spectrometry. We quantified the relative expression levels of 7322 proteins, whereof 724 showed significantly altered levels in AD. Our comprehensive data analysis using enrichment and pathway analyses strongly indicated that presynaptic signaling, such as exocytosis and synaptic vesicle cycle processes, is severely disturbed in this area in AD, whereas postsynaptic proteins remained unchanged. Among the significantly altered proteins, we selected three of the most downregulated synaptic proteins; complexin-1, complexin-2 and synaptogyrin-1, for further validation, using a new cohort consisting of six AD and eight control cases. Semi-quantitative analysis of immunohistochemical staining confirmed decreased levels of complexin-1, complexin-2 and synaptogyrin-1 in the outer two-thirds of the molecular layer of the dentate gyrus in AD. Our in-depth proteomic analysis provides extensive knowledge on the potential molecular mechanism underlying synaptic dysfunction related to AD and supports that presynaptic alterations are more important than postsynaptic changes in early stages of the disease. The specific synaptic proteins identified could potentially be targeted to halt synaptic dysfunction in AD.", "doi": "10.1074/mcp.RA119.001737", "pmid": "31699905", "labels": {"Global Proteomics and Proteogenomics": "Collaborative", "Bioinformatics Support for Computational Resources": "Service"}, "xrefs": [{"db": "pii", "key": "S1535-9476(20)30010-4"}, {"db": "pmc", "key": "PMC6944231"}], "notes": [], "created": "2020-01-07T09:41:41.259Z", "modified": "2024-01-16T13:48:43.135Z"}]}