{"entity": "researcher", "timestamp": "2026-08-20T20:37:29.894Z", "family": "Han", "given": "Xiao", "initials": "X", "orcid": "0000-0003-0879-4119", "affiliations": ["Science for Life Laboratory, Department of Medicine Solna, Karolinska Institute, and Division of Infectious Diseases, Karolinska University Hospital, Solna, SE-17176 Stockholm, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed"}}, "publications": [{"entity": "publication", "iuid": "5003f858767a4018b4b72e7a83ccc4bf", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/5003f858767a4018b4b72e7a83ccc4bf.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/5003f858767a4018b4b72e7a83ccc4bf"}}, "title": "Solution architecture of G3BP1 reveals pH-dependent conformational switching underlying liquid-liquid phase separation", "authors": [{"family": "Han", "given": "Xiao", "initials": "X", "orcid": "0000-0003-0879-4119", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed.json"}}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Graewert", "given": "Melissa A", "initials": "MA"}, {"family": "Zhou", "given": "Qianyu", "initials": "Q"}, {"family": "Resink", "given": "Tom", "initials": "T", "orcid": "0000-0002-2851-1684", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0c147e9bc8e1457489364f54d61983a0.json"}}, {"family": "Blanchet", "given": "Clement E", "initials": "CE"}, {"family": "McInerney", "given": "Gerald", "initials": "G"}, {"family": "Alici", "given": "Evren", "initials": "E", "orcid": "0000-0001-5307-6648", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1b15e3ead7914feb86af38946f373dfb.json"}}, {"family": "Ljunggren", "given": "Hans Gustaf", "initials": "HG"}, {"family": "Farnebo", "given": "Marianne", "initials": "M"}, {"family": "Svergun", "given": "Dmitri", "initials": "D"}, {"family": "Achour", "given": "Adnane", "initials": "A"}], "type": "posted-content", "published": "2025-03-29", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2025.03.27.645651", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:01:50.979Z", "modified": "2026-08-20T11:01:51.108Z"}, {"entity": "publication", "iuid": "93555e317ef54e44bd5030caa6749aa4", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/93555e317ef54e44bd5030caa6749aa4.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/93555e317ef54e44bd5030caa6749aa4"}}, "title": "High Resolution Crystal Structure of the Pyruvate Kinase Tetramer in Complex with the Allosteric Activator Mitapivat/AG-348", "authors": [{"family": "Han", "given": "Xiao", "initials": "X", "orcid": "0000-0003-0879-4119", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Zhang", "given": "Cheng", "initials": "C", "orcid": "0000-0002-3721-8586", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f46e4161be08458994efddb75ed75874.json"}}, {"family": "Mardinoglu", "given": "Adil", "initials": "A", "orcid": "0000-0002-4254-6090", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ca58bf2d214047e0ae5e38a42a0f2808.json"}}, {"family": "Achour", "given": "Adnane", "initials": "A", "orcid": "0000-0003-0432-710X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/65fba324156a4fcbafbe636e642587a9.json"}}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}], "type": "journal-article", "published": "2024-05-05", "journal": {"title": "Crystals", "issn": "2073-4352", "volume": "14", "issue": "5", "pages": "441", "issn-l": null}, "abstract": null, "doi": "10.3390/cryst14050441", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:40:24.382Z", "modified": "2026-08-20T13:40:24.520Z"}, {"entity": "publication", "iuid": "c2f76c44eb7f4e60b25591e87657cc4d", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/c2f76c44eb7f4e60b25591e87657cc4d.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/c2f76c44eb7f4e60b25591e87657cc4d"}}, "title": "Caprin-1 binding to the critical stress granule protein G3BP1 is influenced by pH.", "authors": [{"family": "Schulte", "given": "Tim", "initials": "T"}, {"family": "Panas", "given": "Marc D", "initials": "MD"}, {"family": "Han", "given": "Xiao", "initials": "X", "orcid": "0000-0003-0879-4119", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed.json"}}, {"family": "Williams", "given": "Lucy", "initials": "L"}, {"family": "Kedersha", "given": "Nancy", "initials": "N"}, {"family": "Fleck", "given": "Jonas Simon", "initials": "JS"}, {"family": "Tan", "given": "Timothy J C", "initials": "TJC"}, {"family": "Dopico", "given": "Xaquin Castro", "initials": "XC", "orcid": "0000-0002-9005-6774", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/473ffce480ca4f2e8f75ad7bb4097e17.json"}}, {"family": "Olsson", "given": "Anders", "initials": "A"}, {"family": "Morro", "given": "Ainhoa Moliner", "initials": "AM"}, {"family": "Hanke", "given": "Leo", "initials": "L", "orcid": "0000-0001-5514-2418", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c1c38fa28e3d4733978f027a582c2230.json"}}, {"family": "Nilvebrant", "given": "Johan", "initials": "J"}, {"family": "Giang", "given": "Kim Anh", "initials": "KA"}, {"family": "Nygren", "given": "Per-\u00c5ke", "initials": "P\u00c5"}, {"family": "Anderson", "given": "Paul", "initials": "P"}, {"family": "Achour", "given": "Adnane", "initials": "A", "orcid": "0000-0003-0432-710X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/65fba324156a4fcbafbe636e642587a9.json"}}, {"family": "McInerney", "given": "Gerald M", "initials": "GM", "orcid": "0000-0003-2257-7241", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/012d1aaf306b43dc89309b45ccc6b649.json"}}], "type": "journal article", "published": "2023-05-00", "journal": {"title": "Open Biol", "issn": "2046-2441", "volume": "13", "issue": "5", "pages": "220369", "issn-l": "2046-2441"}, "abstract": "G3BP is the central node within stress-induced protein-RNA interaction networks known as stress granules (SGs). The SG-associated proteins Caprin-1 and USP10 bind mutually exclusively to the NTF2 domain of G3BP1, promoting and inhibiting SG formation, respectively. Herein, we present the crystal structure of G3BP1-NTF2 in complex with a Caprin-1-derived short linear motif (SLiM). Caprin-1 interacts with His-31 and His-62 within a third NTF2-binding site outside those covered by USP10, as confirmed using biochemical and biophysical-binding assays. Nano-differential scanning fluorimetry revealed reduced thermal stability of G3BP1-NTF2 at acidic pH. This destabilization was counterbalanced significantly better by bound USP10 than Caprin-1. The G3BP1/USP10 complex immunoprecipated from human U2OS cells was more resistant to acidic buffer washes than G3BP1/Caprin-1. Acidification of cellular condensates by approximately 0.5 units relative to the cytosol was detected by ratiometric fluorescence analysis of pHluorin2 fused to G3BP1. Cells expressing a Caprin-1/FGDF chimera with higher G3BP1-binding affinity had reduced Caprin-1 levels and slightly reduced condensate sizes. This unexpected finding may suggest that binding of the USP10-derived SLiM to NTF2 reduces the propensity of G3BP1 to enter condensates.", "doi": "10.1098/rsob.220369", "pmid": "37161291", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10170197"}, {"db": "figshare", "key": "10.6084/m9.figshare.c.6626084"}], "notes": [], "created": "2026-08-20T09:52:56.809Z", "modified": "2026-08-20T09:52:56.938Z"}, {"entity": "publication", "iuid": "c84f34304d684326a7455384401c79b6", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/c84f34304d684326a7455384401c79b6.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/c84f34304d684326a7455384401c79b6"}}, "title": "Successive crystal structure snapshots suggest the basis for MHC class I peptide loading and editing by tapasin.", "authors": [{"family": "Hafstrand", "given": "Ida", "initials": "I", "orcid": "0000-0002-1012-9532", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/30b0065eee584566a6d75a1df61c0836.json"}}, {"family": "Sayitoglu", "given": "Ece Canan", "initials": "EC"}, {"family": "Apavaloaei", "given": "Anca", "initials": "A", "orcid": "0000-0001-6896-1199", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/456edb69e56f47b4b9992e5d07994c6e.json"}}, {"family": "Josey", "given": "Benjamin John", "initials": "BJ"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Han", "given": "Xiao", "initials": "X", "orcid": "0000-0003-0879-4119", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed.json"}}, {"family": "Pellegrino", "given": "Sara", "initials": "S"}, {"family": "Ozkazanc", "given": "Didem", "initials": "D"}, {"family": "Potens", "given": "Ren\u00e9e", "initials": "R"}, {"family": "Janssen", "given": "Linda", "initials": "L"}, {"family": "Nilvebrant", "given": "Johan", "initials": "J", "orcid": "0000-0002-6104-6446", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5cd15a9b2af64e4b977d064bacad0330.json"}}, {"family": "Nygren", "given": "Per-\u00c5ke", "initials": "P\u00c5", "orcid": "0000-0003-4214-6991", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/db3f3b9b876c486e9c8acaa5efcfff18.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Springer", "given": "Sebastian", "initials": "S", "orcid": "0000-0002-5527-6149", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4b53dfef715d45569df53ba2bae9cc84.json"}}, {"family": "Georgoudaki", "given": "Anna-Maria", "initials": "AM"}, {"family": "Duru", "given": "Adil Doganay", "initials": "AD"}, {"family": "Achour", "given": "Adnane", "initials": "A"}], "type": "journal article", "published": "2019-03-12", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "116", "issue": "11", "pages": "5055-5060", "issn-l": "0027-8424"}, "abstract": "MHC-I epitope presentation to CD8+ T cells is directly dependent on peptide loading and selection during antigen processing. However, the exact molecular bases underlying peptide selection and binding by MHC-I remain largely unknown. Within the peptide-loading complex, the peptide editor tapasin is key to the selection of MHC-I-bound peptides. Here, we have determined an ensemble of crystal structures of MHC-I in complex with the peptide exchange-associated dipeptide GL, as well as the tapasin-associated scoop loop, alone or in combination with candidate epitopes. These results combined with mutation analyses allow us to propose a molecular model underlying MHC-I peptide selection by tapasin. The N termini of bound peptides most probably bind first in the N-terminal and middle region of the MHC-I peptide binding cleft, upon which the peptide C termini are tested for their capacity to dislodge the tapasin scoop loop from the F pocket of the MHC-I cleft. Our results also indicate important differences in peptide selection between different MHC-I alleles.", "doi": "10.1073/pnas.1807656116", "pmid": "30808808", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6421438"}, {"db": "pii", "key": "1807656116"}, {"db": "PDB", "key": "6GB7"}, {"db": "PDB", "key": "6GB5"}, {"db": "PDB", "key": "6GB6"}], "notes": [], "created": "2026-08-20T09:29:48.827Z", "modified": "2026-08-20T09:29:49.027Z"}]}