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1.	Adamina, M, et al. (author) The impact of surgical delay on resectability of colorectal cancer: An international prospective cohort study 2022 In: Colorectal disease : the official journal of the Association of Coloproctology of Great Britain and Ireland. - : Wiley. - 1463-1318. ; 24:6, s. 708-726 Journal article (peer-reviewed)
2.	Sabirsh, A, et al. (author) Residues from transmembrane helices 3 and 5 participate in leukotriene B-4 binding to BLT1 2006 In: Biochemistry. - : American Chemical Society (ACS). - 0006-2960 .- 1520-4995. ; 45:18, s. 5733-5744 Journal article (peer-reviewed)abstract Leukotrienes are inflammatory mediators that bind to seven transmembrane, G-protein-coupled receptors (GPCRs). Here we examine residues from transmembrane helices 3 and 5 of the leukotriene B-4 (LTB4) receptor BLT1 to elucidate how these residues are involved in ligand binding. We have selected these residues on the basis of (1) amino acid sequence analysis, (2) receptor binding and activation studies with a variety of leukotriene-like ligands and recombinant BLT1 receptors, (3) previously published recombinant BLT1 mutants, and (4) a computed model of the active structure of the BLT1 receptor. We propose that LTB4 binds with the polar carboxylate group of LTB4 near the extracellular surface of BLT1 and with the hydrophobic LTB4 tail pointing into the transmembrane regions of the receptor protein. The carboxylate group and the two hydroxyls of LTB4 interact with Arg178 and Glu185 in transmembrane helix 5. Residues from transmembrane helix 3, Val 105 and Ile 108, also line the pocket deeper inside the receptor. LTB4 is becoming increasingly important as an immunomodulator during a number of pathologies, including atherosclerosis. Detailed information about the LTB4 binding mechanism, and the receptor residues involved, will hopefully aid in the design of new immunomodulatory drugs.
3.	Schache, AG, et al. (author) Global wealth disparities drive adherence to COVID-safe pathways in head and neck cancer surgery 2021 In: BJS open. - : Oxford University Press (OUP). - 2474-9842. ; 5:6 Journal article (peer-reviewed)
4.	Glasbey, JC, et al. (author) 2021 swepub:Mat__t
5.	2021 swepub:Mat__t

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Type of publication: journal article (3)

Type of content: peer-reviewed (3)

Author/Editor: Alameer, E (5); Qureshi, A. (4); Martin, J. (4); Kumar, A. (4); Moore, R. (4); Sharma, N. (4); show more...; Desai, A. (4); Conti, L. (4); Knight, A. (4); Cox, D (4); Adamina, M (4); Cunha, MF (4); Emile, S (4); Ghosh, D (4); Lawday, S (4); Li, E (4); Mohan, HM (4); Pata, F (4); Pockney, P (4); Benson, RA (4); Bywater, E (4); Dawson, BE (4); Evans, JP (4); Jones, CS (4); Khatri, C (4); Khaw, RA (4); Gallo, G (4); Moug, S (4); Roberts, K (4); Satoi, S (4); Ford, S (4); Fiore, M (4); Kolias, A (4); Shaw, R (4); Winter, SC (4); Ho, M (4); Biel, JR (4); Ganly, I (4); Vidya, R (4); Sundar, S (4); Agarwal, A (4); Alser, O (4); Alshaar, M (4); Arnaud, AP (4); Ayasra, F (4); Barlow, E (4); Brar, A (4); Breen, KA (4); Burke, J (4); Chaar, M (4); show less...

University: Karolinska Institutet (5); Lund University (1)

Language: English (5)

Research subject (UKÄ/SCB): Natural sciences (1)

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