{"entity": "researcher", "timestamp": "2026-07-19T06:22:01.100Z", "family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "affiliations": [], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56"}}, "publications": [{"entity": "publication", "iuid": "81a8ff1347b741339d840038298a8e71", "links": {"self": {"href": "https://publications.scilifelab.se/publication/81a8ff1347b741339d840038298a8e71.json"}, "display": {"href": "https://publications.scilifelab.se/publication/81a8ff1347b741339d840038298a8e71"}}, "title": "Seal milk oligosaccharides rival human milk complexity and exhibit functional dynamics during lactation.", "authors": [{"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Lundstr\u00f8m", "given": "Jon", "initials": "J", "orcid": "0000-0003-2733-7124", "researcher": {"href": "https://publications.scilifelab.se/researcher/1e9b642f0bae4a19ba21ed3db3e14d85.json"}}, {"family": "Cori", "given": "Carmen R", "initials": "CR"}, {"family": "Guu", "given": "Shih-Yun", "initials": "SY"}, {"family": "Bennett", "given": "Alexander R", "initials": "AR", "orcid": "0000-0003-4869-9132", "researcher": {"href": "https://publications.scilifelab.se/researcher/becd350a3553463bb37530cc639f281d.json"}}, {"family": "Dannborg", "given": "Mirjam", "initials": "M"}, {"family": "Pomeroy", "given": "Patrick P", "initials": "PP", "orcid": "0000-0003-1603-5630", "researcher": {"href": "https://publications.scilifelab.se/researcher/834269bd43b74cd8bc42aaa3600de72b.json"}}, {"family": "Kennedy", "given": "Malcolm W", "initials": "MW", "orcid": "0000-0002-0970-5264", "researcher": {"href": "https://publications.scilifelab.se/researcher/6f1fc8fbe5d748c78ab9fdd182796176.json"}}, {"family": "Bengtsson-Palme", "given": "Johan", "initials": "J", "orcid": "0000-0002-6528-3158", "researcher": {"href": "https://publications.scilifelab.se/researcher/267ff77d11e04a30bacdd0ae7492bea8.json"}}, {"family": "Hevey", "given": "Rachel", "initials": "R", "orcid": "0000-0002-2649-3427", "researcher": {"href": "https://publications.scilifelab.se/researcher/020432b915a84ec7a643efdfc8ec9e95.json"}}, {"family": "Khoo", "given": "Kay-Hooi", "initials": "KH"}, {"family": "Bojar", "given": "Daniel", "initials": "D", "orcid": "0000-0002-3008-7851", "researcher": {"href": "https://publications.scilifelab.se/researcher/f2a9b04a70e34849b1a54b8db3252807.json"}}], "type": "journal article", "published": "2025-11-25", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "16", "issue": "1", "pages": "10067", "issn-l": "2041-1723"}, "abstract": "Milk oligosaccharides are crucial for neonatal development and health in mammals. Yet most milk research focuses on humans, or on domesticated mammals that are poor in milk oligosaccharide complexity. Here, we perform an exhaustive mass spectrometry-driven structural characterization of milk oligosaccharides in a wild mammal, female Atlantic grey seals (Halichoerus grypus), throughout their lactation period. Characterizing and quantifying 332 milk oligosaccharides, including 166 unreported structures, we reveal seals to rival human milk in complexity. We report seal free oligosaccharides to reach up to 28 monosaccharides in size. Paired glycomics and metabolomics time course analysis establishes a concerted regulatory process reshaping the seal milk glycome throughout lactation, similar to human milk. Functional analysis of the structures we here characterized reveals anti-biofilm effects and immunomodulatory functions of seal milk oligosaccharides. Our findings challenge long-held assumptions about milk complexity of non-human mammals and enable insights into the functional relevance of complex carbohydrates in milk.", "doi": "10.1038/s41467-025-66075-2", "pmid": "41290693", "labels": {"Glycoproteomics and MS Proteomics": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC12647773"}, {"db": "pii", "key": "10.1038/s41467-025-66075-2"}], "notes": [], "created": "2026-01-27T13:07:39.913Z", "modified": "2026-01-27T13:07:41.170Z"}, {"entity": "publication", "iuid": "7a2b558ac01544798bc900cf393eb3bf", "links": {"self": {"href": "https://publications.scilifelab.se/publication/7a2b558ac01544798bc900cf393eb3bf.json"}, "display": {"href": "https://publications.scilifelab.se/publication/7a2b558ac01544798bc900cf393eb3bf"}}, "title": "A monoallelic UXS1 variant associated with short-limbed short stature.", "authors": [{"family": "Rustad", "given": "Cecilie F", "initials": "CF", "orcid": "0000-0001-7903-9087", "researcher": {"href": "https://publications.scilifelab.se/researcher/6a07a4976faf41e0a32c6f6183b2c4b0.json"}}, {"family": "Backe", "given": "Paul Hoff", "initials": "PH", "orcid": "0000-0003-4860-4615", "researcher": {"href": "https://publications.scilifelab.se/researcher/2b90a596052141538a2292581533775a.json"}}, {"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Merckoll", "given": "Else", "initials": "E"}, {"family": "Tveten", "given": "Kristian", "initials": "K"}, {"family": "Maciej-Hulme", "given": "Marissa Lucy", "initials": "ML"}, {"family": "Karlsson", "given": "Niclas", "initials": "N"}, {"family": "Prescott", "given": "Trine", "initials": "T", "orcid": "0000-0002-9490-3141", "researcher": {"href": "https://publications.scilifelab.se/researcher/6c1f7636c7e3471bbed443133cb51259.json"}}, {"family": "Sand", "given": "Elise Sand\u00e5s", "initials": "ES"}, {"family": "Woldseth", "given": "Berit", "initials": "B"}, {"family": "Elgst\u00f8en", "given": "Katja Benedikte Prest\u00f8", "initials": "KBP"}, {"family": "Holla", "given": "\u00d8ystein L", "initials": "\u00d8L", "orcid": "0000-0002-7697-857X", "researcher": {"href": "https://publications.scilifelab.se/researcher/eef78b38c6684b8a9211b1a5d8f1e62a.json"}}], "type": "journal article", "published": "2024-06-00", "journal": {"title": "Mol Genet Genomic Med", "issn": "2324-9269", "volume": "12", "issue": "6", "pages": "e2472", "issn-l": "2324-9269"}, "abstract": "Serine residues in the protein backbone of heavily glycosylated proteoglycans are bound to glycosaminoglycans through a tetrasaccharide linker. UXS1 encodes UDP-glucuronate decarboxylase 1, which catalyzes synthesis of UDP-xylose, the donor of the first building block in the linker. Defects in other enzymes involved in formation of the tetrasaccharide linker cause so-called linkeropathies, characterized by short stature, radio-ulnar synostosis, decreased bone density, congenital contractures, dislocations, and more.\n\nWhole exome sequencing was performed in a father and son who presented with a mild skeletal dysplasia, as well as the father's unaffected parents. Wild-type and mutant UXS1 were recombinantly expressed in Escherichia coli and purified. Enzyme activity was evaluated by LC-MS/MS. In vivo effects were studied using HeparinRed assay and metabolomics.\n\nThe son had short long bones, normal epiphysis, and subtle metaphyseal changes especially in his legs. The likely pathogenic heterozygous variant NM_001253875.1(UXS1):c.557T>A p.(Ile186Asn) detected in the son was de novo in the father. Purified Ile186Asn-UXS1, in contrast to the wild-type, was not able to convert UDP-glucuronic acid to UDP-xylose. Plasma glycosaminoglycan levels were decreased in both son and father.\n\nThis is the first report linking UXS1 to short-limbed short stature in humans.", "doi": "10.1002/mgg3.2472", "pmid": "38860481", "labels": {"Glycoproteomics and MS Proteomics": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC11165340"}], "notes": [], "created": "2024-11-27T14:01:50.567Z", "modified": "2024-11-27T15:35:29.966Z"}, {"entity": "publication", "iuid": "74bf3dccedb8436ea8a05bef8c89d201", "links": {"self": {"href": "https://publications.scilifelab.se/publication/74bf3dccedb8436ea8a05bef8c89d201.json"}, "display": {"href": "https://publications.scilifelab.se/publication/74bf3dccedb8436ea8a05bef8c89d201"}}, "title": "Ion mobility-tandem mass spectrometry of mucin-type O-glycans.", "authors": [{"family": "Bechtella", "given": "Le\u00efla", "initials": "L", "orcid": "0000-0002-7354-3108", "researcher": {"href": "https://publications.scilifelab.se/researcher/3bd4eb095d624ac1959d8dc16150ab8c.json"}}, {"family": "Chunsheng", "given": "Jin", "initials": "J", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Fentker", "given": "Kerstin", "initials": "K", "orcid": "0009-0005-0437-1049", "researcher": {"href": "https://publications.scilifelab.se/researcher/991a0c7c9fdf4187835f12fb4c68bdf0.json"}}, {"family": "Ert\u00fcrk", "given": "G\u00fcney R", "initials": "GR"}, {"family": "Safferthal", "given": "Marc", "initials": "M", "orcid": "0009-0006-9267-3940", "researcher": {"href": "https://publications.scilifelab.se/researcher/f6e1dbee77d342be876a1d7fba2732e0.json"}}, {"family": "Polewski", "given": "\u0141ukasz", "initials": "\u0141", "orcid": "0009-0001-9802-2528", "researcher": {"href": "https://publications.scilifelab.se/researcher/f4d3ffc3ab2345478fad082496479704.json"}}, {"family": "G\u00f6tze", "given": "Michael", "initials": "M", "orcid": "0000-0003-4001-2324", "researcher": {"href": "https://publications.scilifelab.se/researcher/f049e7388fe7421099b5f38c675d3962.json"}}, {"family": "Graeber", "given": "Simon Y", "initials": "SY", "orcid": "0000-0002-1666-8924", "researcher": {"href": "https://publications.scilifelab.se/researcher/f803b57dfcbb4f3b9b60ae9947e10930.json"}}, {"family": "Vos", "given": "Ga\u00ebl M", "initials": "GM"}, {"family": "Struwe", "given": "Weston B", "initials": "WB", "orcid": "0000-0003-0594-226X", "researcher": {"href": "https://publications.scilifelab.se/researcher/193bc52c108c43d6aed7a796261202a9.json"}}, {"family": "Mall", "given": "Marcus A", "initials": "MA", "orcid": "0000-0002-4057-2199", "researcher": {"href": "https://publications.scilifelab.se/researcher/1a5827fb0517424b974964081ea15d19.json"}}, {"family": "Mertins", "given": "Philipp", "initials": "P", "orcid": "0000-0002-2245-528X", "researcher": {"href": "https://publications.scilifelab.se/researcher/83ca1dab03d24278ae7cddad4944f830.json"}}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG"}, {"family": "Pagel", "given": "Kevin", "initials": "K", "orcid": "0000-0001-8054-4718", "researcher": {"href": "https://publications.scilifelab.se/researcher/398849274b4e45f6a6c6997026f7c5a1.json"}}], "type": "journal article", "published": "2024-03-23", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "2611", "issn-l": "2041-1723"}, "abstract": "The dense O-glycosylation of mucins plays an important role in the defensive properties of the mucus hydrogel. Aberrant glycosylation is often correlated with inflammation and pathology such as COPD, cancer, and Crohn's disease. The inherent complexity of glycans and the diversity in the O-core structure constitute fundamental challenges for the analysis of mucin-type O-glycans. Due to coexistence of multiple isomers, multidimensional workflows such as LC-MS are required. To separate the highly polar carbohydrates, porous graphitized carbon is often used as a stationary phase. However, LC-MS workflows are time-consuming and lack reproducibility. Here we present a rapid alternative for separating and identifying O-glycans released from mucins based on trapped ion mobility mass spectrometry. Compared to established LC-MS, the acquisition time is reduced from an hour to two minutes. To test the validity, the developed workflow was applied to sputum samples from cystic fibrosis patients to map O-glycosylation features associated with disease.", "doi": "10.1038/s41467-024-46825-4", "pmid": "38521783", "labels": {"Glycoproteomics and MS Proteomics": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC10960840"}, {"db": "pii", "key": "10.1038/s41467-024-46825-4"}], "notes": [], "created": "2024-11-27T15:32:35.327Z", "modified": "2024-11-27T15:35:26.455Z"}, {"entity": "publication", "iuid": "937420beed3f45248f9e846261358e94", "links": {"self": {"href": "https://publications.scilifelab.se/publication/937420beed3f45248f9e846261358e94.json"}, "display": {"href": "https://publications.scilifelab.se/publication/937420beed3f45248f9e846261358e94"}}, "title": "Sialidases and fucosidases of Akkermansia muciniphila are crucial for growth on mucin and nutrient sharing with mucus-associated gut bacteria.", "authors": [{"family": "Shuoker", "given": "Bashar", "initials": "B"}, {"family": "Pichler", "given": "Michael J", "initials": "MJ", "orcid": "0000-0003-3408-652X", "researcher": {"href": "https://publications.scilifelab.se/researcher/89029dfd93c148a0b9c16a66edecf0fb.json"}}, {"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Sakanaka", "given": "Hiroka", "initials": "H"}, {"family": "Wu", "given": "Haiyang", "initials": "H"}, {"family": "Gascue\u00f1a", "given": "Ana Mart\u00ednez", "initials": "AM", "orcid": "0000-0002-6245-5823", "researcher": {"href": "https://publications.scilifelab.se/researcher/77cdc688e98a4bf1a7590ea86d644b62.json"}}, {"family": "Liu", "given": "Jining", "initials": "J"}, {"family": "Nielsen", "given": "Tine Sofie", "initials": "TS"}, {"family": "Holgersson", "given": "Jan", "initials": "J"}, {"family": "Nordberg Karlsson", "given": "Eva", "initials": "E", "orcid": "0000-0002-8597-7050", "researcher": {"href": "https://publications.scilifelab.se/researcher/ddb4af1ad5f344eebef11432ed7ee4df.json"}}, {"family": "Juge", "given": "Nathalie", "initials": "N", "orcid": "0000-0001-8515-1315", "researcher": {"href": "https://publications.scilifelab.se/researcher/a155db7bbffc48429fb2e68ab7b0c306.json"}}, {"family": "Meier", "given": "Sebastian", "initials": "S", "orcid": "0000-0003-3761-3217", "researcher": {"href": "https://publications.scilifelab.se/researcher/4d38fd89c1be4714b927c7c10a2117a5.json"}}, {"family": "Morth", "given": "Jens Preben", "initials": "JP", "orcid": "0000-0003-4077-0192", "researcher": {"href": "https://publications.scilifelab.se/researcher/d16ea8a43be84cdba3e41cbaec91940e.json"}}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG", "orcid": "0000-0002-3045-2628", "researcher": {"href": "https://publications.scilifelab.se/researcher/62e0b7440ff1447c9611d938d185fbc7.json"}}, {"family": "Abou Hachem", "given": "Maher", "initials": "M", "orcid": "0000-0001-8250-1842", "researcher": {"href": "https://publications.scilifelab.se/researcher/c422215c0fb242f08e9b101521ba8f64.json"}}], "type": "journal article", "published": "2023-04-01", "journal": {"title": "Nat Commun", "issn": "2041-1723", "issn-l": "2041-1723", "volume": "14", "issue": "1", "pages": "1833"}, "abstract": "The mucolytic human gut microbiota specialist Akkermansia muciniphila is proposed to boost mucin-secretion by the host, thereby being a key player in mucus turnover. Mucin glycan utilization requires the removal of protective caps, notably fucose and sialic acid, but the enzymatic details of this process remain largely unknown. Here, we describe the specificities of ten A. muciniphila glycoside hydrolases, which collectively remove all known sialyl and fucosyl mucin caps including those on double-sulfated epitopes. Structural analyses revealed an unprecedented fucosidase modular arrangement and explained the sialyl T-antigen specificity of a sialidase of a previously unknown family. Cell-attached sialidases and fucosidases displayed mucin-binding and their inhibition abolished growth of A. muciniphila on mucin. Remarkably, neither the sialic acid nor fucose contributed to A. muciniphila growth, but instead promoted butyrate production by co-cultured Clostridia. This study brings unprecedented mechanistic insight into the initiation of mucin O-glycan degradation by A. muciniphila and nutrient sharing between mucus-associated bacteria.", "doi": "10.1038/s41467-023-37533-6", "pmid": "37005422", "labels": {"Glycoproteomics and MS Proteomics": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC10067855"}, {"db": "pii", "key": "10.1038/s41467-023-37533-6"}], "notes": [], "created": "2023-12-04T10:22:14.448Z", "modified": "2024-01-16T13:46:27.512Z"}, {"entity": "publication", "iuid": "bad5b686c16e48c0a5d5984892016a93", "links": {"self": {"href": "https://publications.scilifelab.se/publication/bad5b686c16e48c0a5d5984892016a93.json"}, "display": {"href": "https://publications.scilifelab.se/publication/bad5b686c16e48c0a5d5984892016a93"}}, "title": "Reproducing extracellular matrix adverse remodelling of non-ST myocardial infarction in a large animal model.", "authors": [{"family": "Contessotto", "given": "Paolo", "initials": "P", "orcid": "0000-0002-6990-9883", "researcher": {"href": "https://publications.scilifelab.se/researcher/cd9eff0e573f4f7097fb575bf6479f8e.json"}}, {"family": "Spelat", "given": "Renza", "initials": "R", "orcid": "0000-0001-5794-8976", "researcher": {"href": "https://publications.scilifelab.se/researcher/c7974e486fb24bbf979eb920f9d49380.json"}}, {"family": "Ferro", "given": "Federico", "initials": "F", "orcid": "0000-0002-6023-8227", "researcher": {"href": "https://publications.scilifelab.se/researcher/27810903638948feb4391fa537a7eda3.json"}}, {"family": "Vysockas", "given": "Vaidas", "initials": "V", "orcid": "0000-0002-2179-2348", "researcher": {"href": "https://publications.scilifelab.se/researcher/0c01194476544942a0fd0c153a44487e.json"}}, {"family": "Krivickien\u0117", "given": "Au\u0161ra", "initials": "A", "orcid": "0000-0003-4978-2915", "researcher": {"href": "https://publications.scilifelab.se/researcher/29901a96314b4fc489e3aa1712004ae7.json"}}, {"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Chantepie", "given": "Sandrine", "initials": "S"}, {"family": "Chinello", "given": "Clizia", "initials": "C"}, {"family": "Pauza", "given": "Audrys G", "initials": "AG", "orcid": "0000-0001-9635-8872", "researcher": {"href": "https://publications.scilifelab.se/researcher/cb08209745534c21878f607cc414aab8.json"}}, {"family": "Valente", "given": "Camilla", "initials": "C", "orcid": "0000-0003-3084-1102", "researcher": {"href": "https://publications.scilifelab.se/researcher/7cf678853015478daf234ab0f854584e.json"}}, {"family": "Rackauskas", "given": "Mindaugas", "initials": "M", "orcid": "0000-0002-2503-3437", "researcher": {"href": "https://publications.scilifelab.se/researcher/d2edbecde7f94bcfbea7f0776b69bbb2.json"}}, {"family": "Casara", "given": "Alvise", "initials": "A", "orcid": "0000-0002-5056-8732", "researcher": {"href": "https://publications.scilifelab.se/researcher/b3bfb0f2394e44cda5c96d23c6c3b32e.json"}}, {"family": "Zigmantait\u0117", "given": "Vilma", "initials": "V", "orcid": "0000-0002-0410-1533", "researcher": {"href": "https://publications.scilifelab.se/researcher/baa4c86fec6e4f0bbdd6e980a9796ff6.json"}}, {"family": "Magni", "given": "Fulvio", "initials": "F", "orcid": "0000-0002-8663-0374", "researcher": {"href": "https://publications.scilifelab.se/researcher/3d2bb884997b4437924cc2659b823637.json"}}, {"family": "Papy-Garcia", "given": "Dulce", "initials": "D", "orcid": "0000-0003-2225-9331", "researcher": {"href": "https://publications.scilifelab.se/researcher/697039fd70604a79804beb2e8179d9cf.json"}}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG", "orcid": "0000-0002-3045-2628", "researcher": {"href": "https://publications.scilifelab.se/researcher/62e0b7440ff1447c9611d938d185fbc7.json"}}, {"family": "Ereminien\u0117", "given": "Egl\u0117", "initials": "E", "orcid": "0000-0002-8332-788X", "researcher": {"href": "https://publications.scilifelab.se/researcher/8ab7bba2798e40f3b67a791e6be512bc.json"}}, {"family": "Pandit", "given": "Abhay", "initials": "A"}, {"family": "Da Costa", "given": "Mark", "initials": "M", "orcid": "0000-0001-7713-2608", "researcher": {"href": "https://publications.scilifelab.se/researcher/a18320fbed7b43299aedc829736f4eb9.json"}}], "type": "journal article", "published": "2023-02-22", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "14", "issue": "1", "pages": "995", "issn-l": "2041-1723"}, "abstract": "The rising incidence of non-ST-segment elevation myocardial infarction (NSTEMI) and associated long-term high mortality constitutes an urgent clinical issue. Unfortunately, the study of possible interventions to treat this pathology lacks a reproducible pre-clinical model. Indeed, currently adopted small and large animal models of MI mimic only full-thickness, ST-segment-elevation (STEMI) infarcts, and hence cater only for an investigation into therapeutics and interventions directed at this subset of MI. Thus, we develop an ovine model of NSTEMI by ligating the myocardial muscle at precise intervals parallel to the left anterior descending coronary artery. Upon histological and functional investigation to validate the proposed model and comparison with STEMI full ligation model, RNA-seq and proteomics show the distinctive features of post-NSTEMI tissue remodelling. Transcriptome and proteome-derived pathway analyses at acute (7 days) and late (28 days) post-NSTEMI pinpoint specific alterations in cardiac post-ischaemic extracellular matrix. Together with the rise of well-known markers of inflammation and fibrosis, NSTEMI ischaemic regions show distinctive patterns of complex galactosylated and sialylated N-glycans in cellular membranes and extracellular matrix. Identifying such changes in molecular moieties accessible to infusible and intra-myocardial injectable drugs sheds light on developing targeted pharmacological solutions to contrast adverse fibrotic remodelling.", "doi": "10.1038/s41467-023-36350-1", "pmid": "36813782", "labels": {"Glycoproteomics and MS Proteomics": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC9945840"}, {"db": "pii", "key": "10.1038/s41467-023-36350-1"}], "notes": [], "created": "2023-12-04T10:23:03.795Z", "modified": "2024-01-16T13:46:27.924Z"}, {"entity": "publication", "iuid": "b6538257193e4bda9387d19ec84faaa0", "links": {"self": {"href": "https://publications.scilifelab.se/publication/b6538257193e4bda9387d19ec84faaa0.json"}, "display": {"href": "https://publications.scilifelab.se/publication/b6538257193e4bda9387d19ec84faaa0"}}, "title": "Metabolic reprogramming and membrane glycan remodeling as potential drivers of zebrafish heart regeneration.", "authors": [{"family": "Spelat", "given": "Renza", "initials": "R", "orcid": "0000-0001-5794-8976", "researcher": {"href": "https://publications.scilifelab.se/researcher/c7974e486fb24bbf979eb920f9d49380.json"}}, {"family": "Ferro", "given": "Federico", "initials": "F", "orcid": "0000-0002-6023-8227", "researcher": {"href": "https://publications.scilifelab.se/researcher/27810903638948feb4391fa537a7eda3.json"}}, {"family": "Contessotto", "given": "Paolo", "initials": "P"}, {"family": "Aljaabary", "given": "Amal", "initials": "A", "orcid": "0000-0003-0361-166X", "researcher": {"href": "https://publications.scilifelab.se/researcher/af820e3a3c8f441c9ed519c8849f163d.json"}}, {"family": "Martin-Salda\u00f1a", "given": "Sergio", "initials": "S", "orcid": "0000-0002-9506-8483", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7a4a6088c0a4597b6c18c2a48c74b7a.json"}}, {"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG", "orcid": "0000-0002-3045-2628", "researcher": {"href": "https://publications.scilifelab.se/researcher/62e0b7440ff1447c9611d938d185fbc7.json"}}, {"family": "Grealy", "given": "Maura", "initials": "M"}, {"family": "Hilscher", "given": "Markus M", "initials": "MM", "orcid": "0000-0001-7782-0830", "researcher": {"href": "https://publications.scilifelab.se/researcher/1de5317c53f34bc89dabfddb0be44983.json"}}, {"family": "Magni", "given": "Fulvio", "initials": "F"}, {"family": "Chinello", "given": "Clizia", "initials": "C"}, {"family": "Kilcoyne", "given": "Michelle", "initials": "M", "orcid": "0000-0002-8870-1308", "researcher": {"href": "https://publications.scilifelab.se/researcher/d1d1606f98e540fbb09f7251adf921a2.json"}}, {"family": "Pandit", "given": "Abhay", "initials": "A", "orcid": "0000-0002-6292-4933", "researcher": {"href": "https://publications.scilifelab.se/researcher/b4611c209a394949bd971c8b12692fac.json"}}], "type": "journal article", "published": "2022-12-13", "journal": {"title": "Commun Biol", "issn": "2399-3642", "volume": "5", "issue": "1", "pages": "1365", "issn-l": "2399-3642"}, "abstract": "The ability of the zebrafish heart to regenerate following injury makes it a valuable model to deduce why this capability in mammals is limited to early neonatal stages. Although metabolic reprogramming and glycosylation remodeling have emerged as key aspects in many biological processes, how they may trigger a cardiac regenerative response in zebrafish is still a crucial question. Here, by using an up-to-date panel of transcriptomic, proteomic and glycomic approaches, we identify a metabolic switch from mitochondrial oxidative phosphorylation to glycolysis associated with membrane glycosylation remodeling during heart regeneration. Importantly, we establish the N- and O-linked glycan structural repertoire of the regenerating zebrafish heart, and link alterations in both sialylation and high mannose structures across the phases of regeneration. Our results show that metabolic reprogramming and glycan structural remodeling are potential drivers of tissue regeneration after cardiac injury, providing the biological rationale to develop novel therapeutics to elicit heart regeneration in mammals.", "doi": "10.1038/s42003-022-04328-2", "pmid": "36509839", "labels": {"In Situ Sequencing": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC9744865"}, {"db": "pii", "key": "10.1038/s42003-022-04328-2"}], "notes": [], "created": "2023-05-31T10:56:03.689Z", "modified": "2025-10-17T13:02:17.158Z"}, {"entity": "publication", "iuid": "5159a6336f114c1ea1325d93eb727d4b", "links": {"self": {"href": "https://publications.scilifelab.se/publication/5159a6336f114c1ea1325d93eb727d4b.json"}, "display": {"href": "https://publications.scilifelab.se/publication/5159a6336f114c1ea1325d93eb727d4b"}}, "title": "Computational Modeling of O-Linked Glycan Biosynthesis in CHO Cells.", "authors": [{"family": "Kouka", "given": "Thukaa", "initials": "T", "orcid": "0000-0002-4442-2294", "researcher": {"href": "https://publications.scilifelab.se/researcher/024a23bc99524cf3aa6cf6658f36037d.json"}}, {"family": "Akase", "given": "Sachiko", "initials": "S"}, {"family": "Sogabe", "given": "Isami", "initials": "I"}, {"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG"}, {"family": "Aoki-Kinoshita", "given": "Kiyoko F", "initials": "KF", "orcid": "0000-0002-6662-8015", "researcher": {"href": "https://publications.scilifelab.se/researcher/a619a1b021b347fe8dd951606fbfd8f4.json"}}], "type": "journal article", "published": "2022-03-08", "journal": {"title": "Molecules", "issn": "1420-3049", "issn-l": "1420-3049", "volume": "27", "issue": "6", "pages": null}, "abstract": "Glycan biosynthesis simulation research has progressed remarkably since 1997, when the first mathematical model for N-glycan biosynthesis was proposed. An O-glycan model has also been developed to predict O-glycan biosynthesis pathways in both forward and reverse directions. In this work, we started with a set of O-glycan profiles of CHO cells transiently transfected with various combinations of glycosyltransferases. The aim was to develop a model that encapsulated all the enzymes in the CHO transfected cell lines. Due to computational power restrictions, we were forced to focus on a smaller set of glycan profiles, where we were able to propose an optimized set of kinetics parameters for each enzyme in the model. Using this optimized model we showed that the abundance of more processed glycans could be simulated compared to observed abundance, while predicting the abundance of glycans earlier in the pathway was less accurate. The data generated show that for the accurate prediction of O-linked glycosylation, additional factors need to be incorporated into the model to better reflect the experimental conditions.", "doi": "10.3390/molecules27061766", "pmid": "35335136", "labels": {"Glycoproteomics and MS Proteomics": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC8950484"}, {"db": "pii", "key": "molecules27061766"}], "notes": [], "created": "2022-11-30T11:59:57.558Z", "modified": "2024-01-16T13:46:29.485Z"}, {"entity": "publication", "iuid": "16a9bb7483ba4829a975ba9c67cf1cbe", "links": {"self": {"href": "https://publications.scilifelab.se/publication/16a9bb7483ba4829a975ba9c67cf1cbe.json"}, "display": {"href": "https://publications.scilifelab.se/publication/16a9bb7483ba4829a975ba9c67cf1cbe"}}, "title": "A single sulfatase is required to access colonic mucin by a gut bacterium.", "authors": [{"family": "Luis", "given": "Ana S", "initials": "AS"}, {"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Pereira", "given": "Gabriel Vasconcelos", "initials": "GV", "orcid": "0000-0001-7937-474X", "researcher": {"href": "https://publications.scilifelab.se/researcher/18369e4fc4d64ae3a25f1f36a8ba9a06.json"}}, {"family": "Glowacki", "given": "Robert W P", "initials": "RWP"}, {"family": "Gugel", "given": "Sadie R", "initials": "SR"}, {"family": "Singh", "given": "Shaleni", "initials": "S"}, {"family": "Byrne", "given": "Dominic P", "initials": "DP"}, {"family": "Pudlo", "given": "Nicholas A", "initials": "NA"}, {"family": "London", "given": "James A", "initials": "JA"}, {"family": "Basl\u00e9", "given": "Arnaud", "initials": "A"}, {"family": "Reihill", "given": "Mark", "initials": "M", "orcid": "0000-0003-3896-9346", "researcher": {"href": "https://publications.scilifelab.se/researcher/3263be5c55014c929d3b7723f677f248.json"}}, {"family": "Oscarson", "given": "Stefan", "initials": "S", "orcid": "0000-0002-8273-4918", "researcher": {"href": "https://publications.scilifelab.se/researcher/709f6e69c27e4dc48d60502e32ee5702.json"}}, {"family": "Eyers", "given": "Patrick A", "initials": "PA", "orcid": "0000-0002-9220-2966", "researcher": {"href": "https://publications.scilifelab.se/researcher/07f88ed1e8ab4f978f801a0d304419c1.json"}}, {"family": "Czjzek", "given": "Mirjam", "initials": "M", "orcid": "0000-0002-7483-2841", "researcher": {"href": "https://publications.scilifelab.se/researcher/732f891072f4492584b366085a4b71fd.json"}}, {"family": "Michel", "given": "Gurvan", "initials": "G"}, {"family": "Barbeyron", "given": "Tristan", "initials": "T"}, {"family": "Yates", "given": "Edwin A", "initials": "EA"}, {"family": "Hansson", "given": "Gunnar C", "initials": "GC", "orcid": "0000-0002-1900-1869", "researcher": {"href": "https://publications.scilifelab.se/researcher/44b3815603154322a6dac16f2fc1c1e9.json"}}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG", "orcid": "0000-0002-3045-2628", "researcher": {"href": "https://publications.scilifelab.se/researcher/62e0b7440ff1447c9611d938d185fbc7.json"}}, {"family": "Cartmell", "given": "Alan", "initials": "A", "orcid": "0000-0002-5512-249X", "researcher": {"href": "https://publications.scilifelab.se/researcher/f80d10a6ee1547febcf53093c2b884ab.json"}}, {"family": "Martens", "given": "Eric C", "initials": "EC", "orcid": "0000-0001-6681-2990", "researcher": {"href": "https://publications.scilifelab.se/researcher/55bba05b4f76442aacb21dfaf01c0b98.json"}}], "type": "journal article", "published": "2021-10-00", "journal": {"title": "Nature", "issn": "1476-4687", "volume": "598", "issue": "7880", "pages": "332-337", "issn-l": "0028-0836"}, "abstract": "Humans have co-evolved with a dense community of microbial symbionts that inhabit the lower intestine. In the colon, secreted mucus creates a barrier that separates these microorganisms from the intestinal epithelium1. Some gut bacteria are able to utilize mucin glycoproteins, the main mucus component, as a nutrient source. However, it remains unclear which bacterial enzymes initiate degradation of the complex O-glycans found in mucins. In the distal colon, these glycans are heavily sulfated, but specific sulfatases that are active on colonic mucins have not been identified. Here we show that sulfatases are essential to the utilization of distal colonic mucin O-glycans by the human gut symbiont Bacteroides thetaiotaomicron. We characterized the activity of 12 different sulfatases produced by this species, showing that they are collectively active on all known sulfate linkages in O-glycans. Crystal structures of three enzymes provide mechanistic insight into the molecular basis of substrate specificity. Unexpectedly, we found that a single sulfatase is essential for utilization of sulfated O-glycans in vitro and also has a major role in vivo. Our results provide insight into the mechanisms of mucin degradation by a prominent group of gut bacteria, an important process for both normal microbial gut colonization2 and diseases such as inflammatory bowel disease3.", "doi": "10.1038/s41586-021-03967-5", "pmid": "34616040", "labels": {"Glycoproteomics and MS Proteomics": "Collaborative"}, "xrefs": [{"db": "mid", "key": "NIHMS1805309"}, {"db": "pmc", "key": "PMC9128668"}, {"db": "pii", "key": "10.1038/s41586-021-03967-5"}], "notes": [], "created": "2021-12-09T21:41:51.821Z", "modified": "2024-01-16T13:46:30.061Z"}, {"entity": "publication", "iuid": "903f912e2763491b8c61bc2d0cdb703e", "links": {"self": {"href": "https://publications.scilifelab.se/publication/903f912e2763491b8c61bc2d0cdb703e.json"}, "display": {"href": "https://publications.scilifelab.se/publication/903f912e2763491b8c61bc2d0cdb703e"}}, "title": "Elastin-like recombinamers-based hydrogel modulates post-ischemic remodeling in a non-transmural myocardial infarction in sheep.", "authors": [{"family": "Contessotto", "given": "Paolo", "initials": "P", "orcid": "0000-0002-6990-9883", "researcher": {"href": "https://publications.scilifelab.se/researcher/cd9eff0e573f4f7097fb575bf6479f8e.json"}}, {"family": "Orbani\u0107", "given": "Doriana", "initials": "D", "orcid": "0000-0002-9723-7279", "researcher": {"href": "https://publications.scilifelab.se/researcher/07e26f981b9d44c88b3c72e5ca9acc68.json"}}, {"family": "Da Costa", "given": "Mark", "initials": "M", "orcid": "0000-0001-7713-2608", "researcher": {"href": "https://publications.scilifelab.se/researcher/a18320fbed7b43299aedc829736f4eb9.json"}}, {"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Owens", "given": "Peter", "initials": "P", "orcid": "0000-0003-1117-1035", "researcher": {"href": "https://publications.scilifelab.se/researcher/d2c23314e1964d9182b0e292ac0cdb7a.json"}}, {"family": "Chantepie", "given": "Sandrine", "initials": "S", "orcid": "0000-0003-1652-432X", "researcher": {"href": "https://publications.scilifelab.se/researcher/b080f580cda242108279d1eef8580735.json"}}, {"family": "Chinello", "given": "Clizia", "initials": "C", "orcid": "0000-0002-7921-7768", "researcher": {"href": "https://publications.scilifelab.se/researcher/da3a7a0cdecf441ba963745111e322c5.json"}}, {"family": "Newell", "given": "John", "initials": "J", "orcid": "0000-0001-7685-6655", "researcher": {"href": "https://publications.scilifelab.se/researcher/40a38064ac4c40a0b8a221cd906d3861.json"}}, {"family": "Magni", "given": "Fulvio", "initials": "F", "orcid": "0000-0002-8663-0374", "researcher": {"href": "https://publications.scilifelab.se/researcher/3d2bb884997b4437924cc2659b823637.json"}}, {"family": "Papy-Garcia", "given": "Dulce", "initials": "D", "orcid": "0000-0003-2225-9331", "researcher": {"href": "https://publications.scilifelab.se/researcher/697039fd70604a79804beb2e8179d9cf.json"}}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG"}, {"family": "Kilcoyne", "given": "Michelle", "initials": "M", "orcid": "0000-0002-8870-1308", "researcher": {"href": "https://publications.scilifelab.se/researcher/d1d1606f98e540fbb09f7251adf921a2.json"}}, {"family": "Dockery", "given": "Peter", "initials": "P", "orcid": "0000-0001-5103-6589", "researcher": {"href": "https://publications.scilifelab.se/researcher/5355752094da43a39ef13af20f42ae4c.json"}}, {"family": "Rodr\u00edguez-Cabello", "given": "Jos\u00e9 C", "initials": "JC", "orcid": "0000-0002-3438-858X", "researcher": {"href": "https://publications.scilifelab.se/researcher/20649ea23f6d4c85ba4b49a49e474d68.json"}}, {"family": "Pandit", "given": "Abhay", "initials": "A", "orcid": "0000-0002-6292-4933", "researcher": {"href": "https://publications.scilifelab.se/researcher/b4611c209a394949bd971c8b12692fac.json"}}], "type": "journal article", "published": "2021-02-17", "journal": {"title": "Sci Transl Med", "issn": "1946-6242", "volume": "13", "issue": "581", "issn-l": "1946-6234"}, "abstract": "Ischemic heart disease is a leading cause of mortality due to irreversible damage to cardiac muscle. Inspired by the post-ischemic microenvironment, we devised an extracellular matrix (ECM)-mimicking hydrogel using catalyst-free click chemistry covalent bonding between two elastin-like recombinamers (ELRs). The resulting customized hydrogel included functional domains for cell adhesion and protease cleavage sites, sensitive to cleavage by matrix metalloproteases overexpressed after myocardial infarction (MI). The scaffold permitted stromal cell invasion and endothelial cell sprouting in vitro. The incidence of non-transmural infarcts has increased clinically over the past decade, and there is currently no treatment preventing further functional deterioration in the infarcted areas. Here, we have developed a clinically relevant ovine model of non-transmural infarcts induced by multiple suture ligations. Intramyocardial injections of the degradable ELRs-hydrogel led to complete functional recovery of ejection fraction 21 days after the intervention. We observed less fibrosis and more angiogenesis in the ELRs-hydrogel-treated ischemic core region compared to the untreated animals, as validated by the expression, proteomic, glycomic, and histological analyses. These findings were accompanied by enhanced preservation of GATA4+ cardiomyocytes in the border zone of the infarct. We propose that our customized ECM favors cardiomyocyte preservation in the border zone by modulating the ischemic core and a marked functional recovery. The functional benefits obtained by the timely injection of the ELRs-hydrogel in a clinically relevant MI model support the potential utility of this treatment for further clinical translation.", "doi": "10.1126/scitranslmed.aaz5380", "pmid": "33597263", "labels": {"Glycoproteomics and MS Proteomics": "Service"}, "xrefs": [{"db": "pii", "key": "13/581/eaaz5380"}], "notes": [], "created": "2021-12-09T21:53:00.845Z", "modified": "2024-01-16T13:46:30.797Z"}, {"entity": "publication", "iuid": "7cb0012083b14d21a8283ff379002b6d", "links": {"self": {"href": "https://publications.scilifelab.se/publication/7cb0012083b14d21a8283ff379002b6d.json"}, "display": {"href": "https://publications.scilifelab.se/publication/7cb0012083b14d21a8283ff379002b6d"}}, "title": "NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods.", "authors": [{"family": "De Leoz", "given": "Maria Lorna A", "initials": "MLA"}, {"family": "Duewer", "given": "David L", "initials": "DL", "orcid": "0000-0002-3924-3064", "researcher": {"href": "https://publications.scilifelab.se/researcher/99b4df16309e4d2dbaa8d9bf3df820f2.json"}}, {"family": "Fung", "given": "Adam", "initials": "A"}, {"family": "Liu", "given": "Lily", "initials": "L"}, {"family": "Yau", "given": "Hoi Kei", "initials": "HK"}, {"family": "Potter", "given": "Oscar", "initials": "O"}, {"family": "Staples", "given": "Gregory O", "initials": "GO"}, {"family": "Furuki", "given": "Kenichiro", "initials": "K"}, {"family": "Frenkel", "given": "Ruth", "initials": "R"}, {"family": "Hu", "given": "Yunli", "initials": "Y"}, {"family": "Sosic", "given": "Zoran", "initials": "Z"}, {"family": "Zhang", "given": "Peiqing", "initials": "P"}, {"family": "Altmann", "given": "Friedrich", "initials": "F", "orcid": "0000-0002-0112-7877", "researcher": {"href": "https://publications.scilifelab.se/researcher/16d364b528014f9596c4dfd5c67ff083.json"}}, {"family": "Grunwald-Grube", "given": 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{"family": "Larson", "given": "G\u00f6ran", "initials": "G", "orcid": "0000-0002-2616-0366", "researcher": {"href": "https://publications.scilifelab.se/researcher/62a940eae9164c56a1d2f9b8ef8242cd.json"}}, {"family": "Nilsson", "given": "Jonas", "initials": "J"}, {"family": "Meyer", "given": "Bernd", "initials": "B"}, {"family": "Wiegandt", "given": "Alena", "initials": "A"}, {"family": "Komatsu", "given": "Emy", "initials": "E"}, {"family": "Perreault", "given": "Helene", "initials": "H"}, {"family": "Bodnar", "given": "Edward D", "initials": "ED"}, {"family": "Said", "given": "Nassur", "initials": "N"}, {"family": "Francois", "given": "Yannis-Nicolas", "initials": "YN"}, {"family": "Leize-Wagner", "given": "Emmanuelle", "initials": "E"}, {"family": "Maier", "given": "Sandra", "initials": "S"}, {"family": "Zeck", "given": "Anne", "initials": "A"}, {"family": "Heck", "given": "Albert J R", "initials": "AJR", "orcid": "0000-0002-2405-4404", "researcher": {"href": "https://publications.scilifelab.se/researcher/ecb05632b366409da1c6a8395e2f5050.json"}}, {"family": "Yang", "given": "Yang", "initials": "Y"}, {"family": "Haselberg", "given": "Rob", "initials": "R"}, {"family": "Yu", "given": "Ying Qing", "initials": "YQ"}, {"family": "Alley", "given": "William", "initials": "W"}, {"family": "Leone", "given": "Joseph W", "initials": "JW"}, {"family": "Yuan", "given": "Hua", "initials": "H"}, {"family": "Stein", "given": "Stephen E", "initials": "SE"}], "type": "journal article", "published": "2020-01-00", "journal": {"volume": "19", "issn": "1535-9484", "issue": "1", "pages": "11-30", "title": "Mol. Cell Proteomics", "issn-l": "1535-9476"}, "abstract": "Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submitted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide community-derived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods.", "doi": "10.1074/mcp.RA119.001677", "pmid": "31591262", "labels": {"Glycoproteomics and MS Proteomics": "Collaborative"}, "xrefs": [{"db": "pmc", "key": "PMC6944243"}, {"db": "pii", "key": "S1535-9476(20)30003-7"}], "notes": [], "created": "2020-01-27T21:30:45.065Z", "modified": "2024-01-16T13:46:31.008Z"}, {"entity": "publication", "iuid": "c9b6610bc7434581a1b93a31a8c3dccd", "links": {"self": {"href": "https://publications.scilifelab.se/publication/c9b6610bc7434581a1b93a31a8c3dccd.json"}, "display": {"href": "https://publications.scilifelab.se/publication/c9b6610bc7434581a1b93a31a8c3dccd"}}, "title": "Ulvan lyase from Formosa agariphila and its applicability in depolymerisation of ulvan extracted from three different Ulva species", "authors": [{"family": "Konasani", "given": "Venkat Rao", "initials": "VR", "orcid": "0000-0002-7687-9563", "researcher": {"href": "https://publications.scilifelab.se/researcher/9a69b8251b5c4260877ad24872ad1b86.json"}}, {"family": "Jin", "given": "Chunsheng", "initials": "C", "orcid": "0000-0002-0229-102X", "researcher": {"href": "https://publications.scilifelab.se/researcher/458804f3f7274b8a9efe7a90469d0e56.json"}}, {"family": "Karlsson", "given": "Niclas G", "initials": "NG"}, {"family": "Albers", "given": "Eva", "initials": "E", "orcid": "0000-0002-1921-3415", "researcher": {"href": "https://publications.scilifelab.se/researcher/fc02c2b6700049e18c94250597f3081c.json"}}], "type": "journal-article", "published": "2018-12-00", "journal": {"volume": "36", "issn": "2211-9264", "issue": null, "pages": "106-114", "title": "Algal Research", "issn-l": "2211-9264"}, "abstract": null, "doi": "10.1016/j.algal.2018.10.016", "pmid": null, "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [], "notes": [], "created": "2018-10-31T13:03:31.852Z", "modified": "2025-10-17T13:03:58.377Z"}]}