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  1. AU=Alderton Alexandra
  2. AU=Zhao Guanlan
  3. AU="Seiradake, Elena"
  4. AU="Daqiu Yin"
  5. AU="Ribeiro, Miriam O"
  6. AU="Zhang, Yuanlin"
  7. AU="Conturso, Alaina C"
  8. AU="Wang, Zuyi"
  9. AU="Ambade, Preshit Nemdas"
  10. AU="Sarmah, Deepraj"
  11. AU="Little, James W."
  12. AU="Templin, Zoe"
  13. AU="Levick, Samantha"
  14. AU="Tatakis, Fotis"
  15. AU="de Vries, Florentine R"
  16. AU="Tsai, Y-T" AU="Tsai, Y-T"
  17. AU="Gonakoti, Sriram"
  18. AU="Wulf, J"
  19. AU="Mardsen, D"
  20. AU="James, David B A"
  21. AU="Montabone, Erika"
  22. AU="Susan J. Burke"
  23. AU="Chen, Yuguang"
  24. AU="Zhao, Zhenghuan"
  25. AU="De Chiara, Anna Rosaria"
  26. AU="Savage, Anne"
  27. AU="Salamanca, Albert"
  28. AU="Zhong, Xiao-Song"
  29. AU="Deguchi, Masashi"
  30. AU="Żmuda, J"
  31. AU="Liao, Yanyan"
  32. AU="Zhu, Jin-Wei"
  33. AU="Khan, Azkia"
  34. AU="Folkman, Judah"
  35. AU=Bhatia Rajesh
  36. AU="Thobois, Stéphane"
  37. AU="Lai, Chien-Chih"
  38. AU="Ahn, Bo Young"
  39. AU="Jeje, Olamide"
  40. AU="Fine, Samson W"
  41. AU="Riemann, Burkhard"
  42. AU="Nazir, Ahsan"
  43. AU="Kawakita, Emi"
  44. AU="Wang, Junnian"
  45. AU="Nie, Chong"

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  1. Artikel ; Online: Is Internal brace augmentation a gold standard treatment compared to isolated Modified Brostrom Gould repair for chronic lateral ligament ankle instability? Effect on functional outcome and Return to preinjury activity: A retrospective analysis.

    Jain, Nimesh P / Ayyaswamy, Brijesh / Griffiths, Alexandra / Alderton, Elizabeth / Kostusiak, Milosz / Limaye, Rajiv V

    Foot (Edinburgh, Scotland)

    2021  Band 50, Seite(n) 101865

    Abstract: Introduction: Modified Brostrom Gould (MBG) repair is widely accepted procedure for chronic lateral ankle instability (CLAI), but there are limitations with regards to strength of repair and risk of reinjury and complications. Internal brace has been ... ...

    Abstract Introduction: Modified Brostrom Gould (MBG) repair is widely accepted procedure for chronic lateral ankle instability (CLAI), but there are limitations with regards to strength of repair and risk of reinjury and complications. Internal brace has been recently used as augmentation of standard MBG repair. It provides stronger construct, facilitates early mobilisation and protects repaired ligament with minimal surgical morbidity. The aim of present study is to compare the outcome of MBG repair without and with Internal brace augmentation (IB) in CLAI.
    Methods: Retrospective analysis of 172 patients with CLAI who underwent MBG repair with or without IBA between November 2017 and October 2019. Patients were evaluated for Visual analogue scale (VAS), Manchester-oxford foot questionnaire (MOxFQ), Patients subjective satisfaction and return to preinjury activity level.
    Results: 148 patients were included in the study with 87 in MBG group and 61 in IB group. The mean age, average injury-surgery interval and mean follow up duration was 40.6 ± 11.2 vs 37.5 ± 14.7 years, 13.1 ± 10.3 vs 14.1 ± 8 months and mean follow up duration of 24.2 ± 5.1 vs 20.7 ± 6.0 months respectively (p > 0.05). The mean time to return to preinjury activity level was significantly better in IB group compared to MBG group of 12.1 ± 2.3 vs 20.3 ± 3.9 weeks, p < 0.001. 55 (90.2%) patients in IB and 73 (83.7%) in MBG group return to preinjury activity level. Mean postoperative VAS score (1.9 ± 1.5 vs. 1.7 ± 1.4, p = 0.428), Mean MOxFQ score (19.7 ± 22.2 vs. 18.2 ± 15.4, p = 0.674) showed no significant difference between MBG and IB group respectively, at final follow up.
    Conclusion: The use of IB augmentation with MBG repair showed significantly better outcome in terms of early rehabilitation and return to preinjury activity level compared to isolated MBG repair. The functional outcome and VAS score were better in IB group compared to MBG group with no significant difference.
    Level of evidence: Level IV retrospective study.
    Mesh-Begriff(e) Adult ; Ankle ; Ankle Joint ; Arthroscopy/methods ; Humans ; Joint Instability/surgery ; Lateral Ligament, Ankle/injuries ; Lateral Ligament, Ankle/surgery ; Middle Aged ; Retrospective Studies ; Treatment Outcome ; Young Adult
    Sprache Englisch
    Erscheinungsdatum 2021-09-23
    Erscheinungsland Scotland
    Dokumenttyp Journal Article
    ZDB-ID 1070358-5
    ISSN 1532-2963 ; 0958-2592
    ISSN (online) 1532-2963
    ISSN 0958-2592
    DOI 10.1016/j.foot.2021.101865
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Phytoremediation of microbial contamination in soil by New Zealand native plants

    Gutierrez-Gines, Maria Jesus / Alizadeh, Hossein / Alderton, Elizabeth / Ambrose, Vikki / Meister, Alexandra / Robinson, Brett H / Halford, Sky / Prosser, Jennifer A / Horswell, Jacqui

    Applied soil ecology. 2021 Nov., v. 167

    2021  

    Abstract: Novel research has demonstrated that the roots of some bioactive plants - called pathogen phytoremediation plants - enhance die-off of pathogenic organisms in the soil. Strategic establishment of pathogen phytoremediation plants may reduce the transport ... ...

    Abstract Novel research has demonstrated that the roots of some bioactive plants - called pathogen phytoremediation plants - enhance die-off of pathogenic organisms in the soil. Strategic establishment of pathogen phytoremediation plants may reduce the transport of human pathogens to water sources. Such plantings could be used in riparian margins, as buffer strips to protect drinking water supplies, or block planting in ‘critical source areas’ of microbial contamination, such as grazing paddocks, organic waste – including sewage sludge - amended land, animal feedlots and housing facilities, and manure storage areas. This work aimed to investigate the antimicrobial activity of a range of New Zealand native plants known for their antimicrobial potential from previous research or through indigenous knowledge, and to assess if any of them could potentially be used for pathogen phytoremediation. Two laboratory screening experiments demonstrated the antimicrobial activity of Leptospermum scoparium, including the local variety swamp mānuka, Kunzea ericoides, Pseudowintera colorata, and Metrosideros robusta against three human pathogens and two indicator organisms. A greenhouse experiment showed a 90% reduction of Escherichia coli numbers in dairy shed effluent irrigated pots after 14 days in soils under swamp L. scoparium and M. robusta, compared with 45 days in soil under Lolium perenne. The pH in the soil under swamp L. scoparium and M. robusta was significantly lower than under L. perenne, which could partially explain the faster E. coli reduction.
    Schlagwörter Escherichia coli ; Kunzea ericoides ; Leptospermum scoparium ; Lolium perenne ; Metrosideros ; antimicrobial properties ; die-off ; feedlots ; greenhouse experimentation ; humans ; indigenous knowledge ; manure storage ; microbial contamination ; organic wastes ; pH ; phytoremediation ; sewage sludge ; soil ; soil ecology ; swamps ; New Zealand
    Sprache Englisch
    Erscheinungsverlauf 2021-11
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    Anmerkung NAL-AP-2-clean
    ZDB-ID 1196758-4
    ISSN 0929-1393
    ISSN 0929-1393
    DOI 10.1016/j.apsoil.2021.104040
    Datenquelle NAL Katalog (AGRICOLA)

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  3. Artikel: Ancient conserved domain protein-1 binds copper and modifies its retention in cells.

    Alderton, Alexandra / Davies, Paul / Illman, Katie / Brown, David R

    Journal of neurochemistry

    2007  Band 103, Heft 1, Seite(n) 312–321

    Abstract: The ancient conserved domain protein (ACDP) family are a recently identified group of homologous mammalian proteins. Some family members have been suggested to have roles in the metabolism of metals. We investigated the capacity of ACDP-1 to bind metals. ...

    Abstract The ancient conserved domain protein (ACDP) family are a recently identified group of homologous mammalian proteins. Some family members have been suggested to have roles in the metabolism of metals. We investigated the capacity of ACDP-1 to bind metals. Using immobilised metal affinity chromatography and isothermal titration calorimetry we determined that ACDP-1 is a high affinity copper binding protein able to bind copper at nanomolar concentrations. In addition the promoter of ACDP-1 contains metal response elements and the cellular expression of ACDP-1 alters cellular retention of copper. However, cellular expression of ACDP-1 does not alter cellular resistance to the toxicity of copper or other metals. As our findings place the subcellular localisation of ACDP-1 in the cytoplasm it is possible that ACDP-1 represent a novel copper chaperone or storage protein.
    Mesh-Begriff(e) Amino Acid Sequence ; Animals ; COS Cells ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cation Transport Proteins ; Cell Line ; Cercopithecus aethiops ; Cloning, Molecular ; Copper/metabolism ; Copper/toxicity ; Cyclins/genetics ; Cyclins/metabolism ; Cytoplasm/metabolism ; Metals, Heavy/toxicity ; Mice ; Molecular Sequence Data ; Sequence Homology, Amino Acid
    Chemische Substanzen ACDP-1 protein, mouse ; Carrier Proteins ; Cation Transport Proteins ; Cyclins ; Metals, Heavy ; Copper (789U1901C5)
    Sprache Englisch
    Erscheinungsdatum 2007-10
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/j.1471-4159.2007.04751.x
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: Ancient conserved domain protein-1 binds copper and modifies its retention in cells

    Alderton, Alexandra / Davies, Paul / Illman, Katie / Brown, David R

    Journal of neurochemistry. 2007 Oct., v. 103, no. 1

    2007  

    Abstract: The ancient conserved domain protein (ACDP) family are a recently identified group of homologous mammalian proteins. Some family members have been suggested to have roles in the metabolism of metals. We investigated the capacity of ACDP-1 to bind metals. ...

    Abstract The ancient conserved domain protein (ACDP) family are a recently identified group of homologous mammalian proteins. Some family members have been suggested to have roles in the metabolism of metals. We investigated the capacity of ACDP-1 to bind metals. Using immobilised metal affinity chromatography and isothermal titration calorimetry we determined that ACDP-1 is a high affinity copper binding protein able to bind copper at nanomolar concentrations. In addition the promoter of ACDP-1 contains metal response elements and the cellular expression of ACDP-1 alters cellular retention of copper. However, cellular expression of ACDP-1 does not alter cellular resistance to the toxicity of copper or other metals. As our findings place the subcellular localisation of ACDP-1 in the cytoplasm it is possible that ACDP-1 represent a novel copper chaperone or storage protein.
    Schlagwörter copper
    Sprache Englisch
    Erscheinungsverlauf 2007-10
    Umfang p. 312-321.
    Verlag Blackwell Publishing Ltd
    Erscheinungsort Oxford, UK
    Dokumenttyp Artikel
    ZDB-ID 80158-6
    ISSN 1471-4159 ; 0022-3042 ; 1474-1644
    ISSN (online) 1471-4159
    ISSN 0022-3042 ; 1474-1644
    DOI 10.1111/j.1471-4159.2007.04751.x
    Datenquelle NAL Katalog (AGRICOLA)

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  5. Artikel ; Online: The effects of prion protein expression on metal metabolism.

    Kralovicova, Silvia / Fontaine, Sarah N / Alderton, Alexandra / Alderman, Julia / Ragnarsdottir, K Vala / Collins, Steven J / Brown, David R

    Molecular and cellular neurosciences

    2009  Band 41, Heft 2, Seite(n) 135–147

    Abstract: The prion protein is a glycoprotein that binds metals such as copper and manganese. When converted to a proteinase resistant isoform it is associated with prion diseases such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Although, ... ...

    Abstract The prion protein is a glycoprotein that binds metals such as copper and manganese. When converted to a proteinase resistant isoform it is associated with prion diseases such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Although, the co-ordination and metal affinity of the prion protein has been well studied, the association of the protein with cellular metal metabolism has been less well investigated. We used transgenic manipulation of prion protein expression and other recombinant techniques to alter expression of known copper binding proteins to investigate the role of the prion protein in copper metabolism. We found that changing the expression of the prion protein alters proteins associated with copper uptake, storage and export from the cell. In addition, alteration in the expression of superoxide dismutases increased prion protein expression dramatically. Reducing copper in the diet decreased expression of the prion protein in the brain while increased dietary manganese dramatically increased the protein's expression. Cellular prion infection also increased the expression of metal transporting proteins and increased cellular manganese concentrations. Overall our results show a close link between cellular resistance to oxidative stress and also copper metabolism. These findings are in line with previous data suggesting that the prion protein is an antioxidant and associated with copper uptake into cells. The disturbance to copper metabolism, as a result of altered prion protein expression clearly demonstrates the important role of the prion protein in copper metabolism. The implication is that prion protein expression has a homeostatic role in copper metabolism.
    Mesh-Begriff(e) Animals ; Brain/metabolism ; Cation Transport Proteins/metabolism ; Cattle ; Cell Line ; Copper/metabolism ; Diet ; Isoenzymes/genetics ; Isoenzymes/metabolism ; Manganese/metabolism ; Mice ; Mice, Knockout ; Mice, Transgenic ; Molecular Chaperones/metabolism ; Oxidative Stress ; Prion Diseases/metabolism ; Prions/genetics ; Prions/metabolism ; Superoxide Dismutase/genetics ; Superoxide Dismutase/metabolism ; Transgenes
    Chemische Substanzen Atox1 protein, mouse ; Cation Transport Proteins ; Ccs protein, mouse ; Ctr1 protein, mouse ; Isoenzymes ; Molecular Chaperones ; Prions ; natural resistance-associated macrophage protein 1 ; solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2 ; Manganese (42Z2K6ZL8P) ; Copper (789U1901C5) ; Superoxide Dismutase (EC 1.15.1.1)
    Sprache Englisch
    Erscheinungsdatum 2009-06
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1046640-x
    ISSN 1095-9327 ; 1044-7431
    ISSN (online) 1095-9327
    ISSN 1044-7431
    DOI 10.1016/j.mcn.2009.02.002
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  6. Artikel ; Online: Evaluating the Effects of SARS-CoV-2 Spike Mutation D614G on Transmissibility and Pathogenicity

    Volz, Erik / Hill, Verity / McCrone, John T. / Price, Anna / Jorgensen, David / O’Toole, Áine / Southgate, Joel / Johnson, Robert / Jackson, Ben / Nascimento, Fabricia F. / Rey, Sara M. / Nicholls, Samuel M. / Colquhoun, Rachel M. / da Silva Filipe, Ana / Shepherd, James / Pascall, David J. / Shah, Rajiv / Jesudason, Natasha / Li, Kathy /
    Jarrett, Ruth / Pacchiarini, Nicole / Bull, Matthew / Geidelberg, Lily / Siveroni, Igor / Goodfellow, Ian / Loman, Nicholas J. / Pybus, Oliver G. / Robertson, Dave / Thomson, Emma C. / Rambaut, Andrew / Connor, Thomas R. / Koshy, Cherian / Wise, Emma / Cortes, Nick / Lynch, Jessica / Kidd, Stephen / Mori, Matilde / Fairley, Derek J. / Curran, Tanya / McKenna, James P. / Adams, Helen / Fraser, Christophe / Golubchik, Tanya / Bonsall, David / Moore, Catrin / Caddy, Sarah L. / Khokhar, Fahad A. / Wantoch, Michelle / Reynolds, Nicola / Warne, Ben / Maksimovic, Joshua / Spellman, Karla / McCluggage, Kathryn / John, Michaela / Beér, Robert / Afifi, Safiah / Morgan, Siân / Marchbank, Angela / Kitchen, C. / Gulliver, Huw / Merrick, Ian / Guest, Martyn / Munn, Robert / Workman, Trudy / Fuller, William / Bresner, Catherine / Snell, Luke B. / Charalampous, Themoula / Nebbia, Gaia / Batra, Rahul / Edgeworth, Jonathan / Robson, Samuel C. / Beckett, Angela / Loveson, Katie F. / Aanensen, David M. / Underwood, Anthony P. / Yeats, Corin A. / Abudahab, Khalil / Taylor, Ben E.W. / Menegazzo, Mirko / Clark, Gemma / Smith, Wendy / Khakh, Manjinder / Fleming, Vicki M. / Lister, Michelle M. / Howson-Wells, Hannah C. / Berry, Louise / Boswell, Tim / Joseph, Amelia / Willingham, Iona / Bird, Paul / Helmer, Thomas / Fallon, Karlie / Holmes, Christopher / Tang, Julian / Raviprakash, Veena / Campbell, Sharon / Sheriff, Nicola / Loose, Matthew W. / Holmes, Nadine / Moore, Christopher / Carlile, Matthew / Wright, Victoria / Sang, Fei / Debebe, Johnny / Coll, Francesc / Signell, Adrian W. / Betancor, Gilberto / Wilson, Harry D. / Feltwell, Theresa / Houldcroft, Charlotte J. / Eldirdiri, Sahar / Kenyon, Anita / Davis, Thomas / Pybus, Oliver / Du Plessis, L. / Zarebski, Alex / Raghwani, Jayna / Kraemer, Moritz / Francois, Sarah / Attwood, Stephen / Vasylyeva, Tetyana / Török, Estée / Hamilton, William L. / Goodfellow, Ian G. / Hall, Grant / Jahun, Aminu S. / Chaudhry, Yasmin / Hosmillo, Myra / Pinckert, Malte L. / Georgana, Iliana / Yakovleva, Anna / Meredith, Luke W. / Moses, S. / Lowe, Hannah / Ryan, Felicity / Fisher, Chloe L. / Awan, Ali R. / Boyes, John / Breuer, Judith / Harris, Kathryn Ann / Brown, Julianne Rose / Shah, Divya / Atkinson, Laura / Lee, Jack C.D. / Alcolea-Medina, Adela / Moore, Nathan / Cortes, Nicholas / Williams, Rebecca / Chapman, Michael R. / Levett, Lisa J. / Heaney, Judith / Smith, Darren L. / Bashton, Matthew / Young, Gregory R. / Allan, John / Loh, Joshua / Randell, Paul A. / Cox, Ali / Madona, Pinglawathee / Holmes, Alison / Bolt, Frances / Price, James / Mookerjee, Siddharth / Rowan, Aileen / Taylor, Graham P. / Ragonnet-Cronin, Manon / Johnson, Rob / Boyd, Olivia / Volz, Erik M. / Brunker, Kirstyn / Smollett, Katherine L. / Quick, Joshua / McMurray, Claire / Stockton, Joanne / Nicholls, Sam / Rowe, William / Poplawski, Radoslaw / Martinez-Nunez, Rocio T. / Mason, Jenifer / Robinson, Trevor I. / O'Toole, Elaine / Watts, Joanne / Breen, Cassie / Cowell, Angela / Ludden, Catherine / Sluga, Graciela / Machin, Nicholas W. / Ahmad, Shazaad S.Y. / George, Ryan P. / Halstead, Fenella / Sivaprakasam, Venkat / Shepherd, James G. / Asamaphan, Patawee / Niebel, Marc O. / Li, Kathy K. / Shah, Rajiv N. / Jesudason, Natasha G. / Parr, Yasmin A. / Tong, Lily / Broos, Alice / Mair, Daniel / Nichols, Jenna / Carmichael, Stephen N. / Nomikou, Kyriaki / Aranday-Cortes, Elihu / Johnson, NaTasha / Starinskij, Igor / Orton, Richard J. / Hughes, Joseph / Vattipally, Sreenu / Singer, Joshua B. / Hale, Antony D. / Macfarlane-Smith, Louissa R. / Harper, Katherine L. / Taha, Yusri / Payne, Brendan A.I. / Burton-Fanning, Shirelle / Waugh, Sheila / Collins, Jennifer / Eltringham, Gary / Templeton, Kate E. / McHugh, Martin P. / Dewar, Rebecca / Wastenge, Elizabeth / Dervisevic, Samir / Stanley, Rachael / Prakash, Reenesh / Stuart, Claire / Elumogo, Ngozi / Sethi, Dheeraj K. / Meader, Emma J. / Coupland, Lindsay J. / Potter, Will / Graham, Clive / Barton, Edward / Padgett, Debra / Scott, Garren / Swindells, Emma / Greenaway, Jane / Nelson, Andrew / Yew, Wen C. / Resende Silva, Paola C. / Andersson, Monique / Shaw, Robert / Peto, Timothy / Justice, Anita / Eyre, David / Crooke, Derrick / Hoosdally, Sarah / Sloan, Tim J. / Duckworth, Nichola / Walsh, Sarah / Chauhan, Anoop J. / Glaysher, Sharon / Bicknell, Kelly / Wyllie, Sarah / Butcher, Ethan / Elliott, Scott / Lloyd, Allyson / Impey, Robert / Levene, Nick / Monaghan, Lynn / Bradley, Declan T. / Allara, Elias / Pearson, Clare / Muir, Peter / Vipond, Ian B. / Hopes, Richard / Pymont, Hannah M. / Hutchings, Stephanie / Curran, Martin D. / Parmar, Surendra / Lackenby, Angie / Mbisa, Tamyo / Platt, Steven / Miah, Shâhjahân / Bibby, David / Manso, Carmen / Hubb, Jonathan / Chand, Meera / Dabrera, Gavin / Ramsay, Mary / Bradshaw, Daniel / Thornton, Alicia / Myers, Richard / Schaefer, Ulf / Groves, Natalie / Gallagher, Eileen / Lee, David / Williams, David / Ellaby, Nicholas / Harrison, Ian / Hartman, Hassan / Manesis, Nikos / Patel, Vineet / Bishop, Chloe / Chalker, Vicki / Osman, Husam / Bosworth, Andrew / Robinson, Esther / Holden, Matthew T.G. / Shaaban, Sharif / Birchley, Alec / Adams, Alexander / Davies, Alisha / Gaskin, Amy / Plimmer, Amy / Gatica-Wilcox, Bree / McKerr, Caoimhe / Moore, Catherine / Williams, Chris / Heyburn, David / De Lacy, Elen / Hilvers, Ember / Downing, Fatima / Shankar, Giri / Jones, Hannah / Asad, Hibo / Coombes, Jason / Watkins, Joanne / Evans, Johnathan M. / Fina, Laia / Gifford, Laura / Gilbert, Lauren / Graham, Lee / Perry, Malorie / Morgan, Mari / Cronin, Michelle / Craine, Noel / Jones, Rachel / Howe, Robin / Corden, Sally / Rey, Sara / Kumziene-Summerhayes, Sara / Taylor, Sarah / Cottrell, Simon / Jones, Sophie / Edwards, Sue / O’Grady, Justin / Page, Andrew J. / Wain, John / Webber, Mark A. / Mather, Alison E. / Baker, David J. / Rudder, Steven / Yāsir, Muḥammad / Thomson, Nicholas M. / Aydin, Alp / Tedim, Ana P. / Kay, Gemma L. / Trotter, Alexander J. / Gilroy, Rachel A.J. / Alikhan, Nabil-Fareed / de Oliveira Martins, Leonardo / Le-Viet, Thanh / Meadows, Lizzie / Kolyva, Anastasia / Diaz, Maria / Bell, Andrew / Gutierrez, Ana Victoria / Charles, Ian G. / Adriaenssens, Evelien M. / Kingsley, Robert A. / Casey, Anna / Simpson, D. A. / Molnár, Zoltán / Thompson, Thomas / Acheson, Erwan / Masoli, Jane A.H. / Knight, Bridget A. / Hattersley, Andrew / Ellard, Sian / Auckland, Cressida / Mahungu, Tabitha W. / Irish-Tavares, Dianne / Haque, Tanzina / Bourgeois, Yann / Scarlett, Garry P. / Partridge, David G. / Raza, Mohammad / Evans, Cariad / Johnson, Kate / Liggett, Steven / Baker, Paul / Essex, Sarah / Lyons, Ronan A. / Caller, Laura G. / Castellano, Sergi / Williams, Rachel J. / Kristiansen, Mark / Roy, Sunando / Williams, Charlotte A. / Dyal, Patricia L. / Tutill, Helena J. / Panchbhaya, Yasmin N. / Forrest, Leysa M. / Niola, Paola / Findlay, Jacqueline / Brooks, Tony T. / Gavriil, Artemis / Mestek-Boukhibar, Lamia / Weeks, Sam / Pandey, Sarojini / Berry, Lisa / Jones, K. E. / Richter, Alex / Beggs, Andrew / Smith, Colin P. / Bucca, Giselda / Hesketh, Andrew R. / Harrison, Ewan M. / Peacock, Sharon J. / Eser, Sophie / Churcher, Carol M. / Bellis, Katherine L. / Girgis, Sophia T. / Naydenova, Plamena / Blane, Beth / Sridhar, Sushmita / Ruis, Chris / Forrest, Sally / Cormie, Claire / Gill, Harmeet K. / Dias, Joana / Higginson, Ellen E. / Maes, Mailis / Young, Jamie / Kermack, Leanne M. / Hadjirin, Nazreen F. / Aggarwal, Dinesh / Griffith, Luke / Swingler, Tracey / Davidson, Rose K. / Williams, Thomas / Balcazar, Carlos E. / Gallagher, Michael D. / O'Toole, Áine / Rooke, Stefan / Colquhoun, Rachel / Ashworth, Jordan / McCrone, J.T. / Scher, Emily / Yu, Xiaoyu / Williamson, Kathleen A. / Stanton, Thomas D. / Michell, Stephen L. / Bewshea, Claire M. / Temperton, Ben / Michelsen, Michelle L. / Warwick-Dugdale, Joanna / Manley, Robin / Farbos, Audrey / Harrison, James W. / Sambles, Christine M. / Studholme, David J. / Jeffries, Aaron R. / Darby, Alistair C. / Hiscox, Julian A. / Paterson, Steve / Iturriza-Gomara, Miren / Jackson, Kathryn A. / Lucaci, Anita O. / Vamos, Edith E. / Hughes, Margaret / Rainbow, Lucille / Eccles, Richard / Nelson, Charlotte / Whitehead, Mark / Turtle, Lance / Haldenby, Sam T. / Gregory, Richard / Gemmell, Matthew / Kwiatkowski, Dominic / de Silva, Thushan I. / Smith, Nikki / Angyal, Adrienn / Lindsey, Benjamin B. / Groves, Danielle C. / Green, Luke R. / Wang, Dennis / Freeman, Timothy M. / Parker, Matthew D. / Keeley, Alexander J. / Parsons, Paul J. / Tucker, Rachel M. / Brown, Rebecca / Wyles, Matthew / Constantinidou, Chrystala / Unnikrishnan, Meera / Ott, Sascha / Cheng, Jeffrey K.J. / Bridgewater, Hannah E. / Frost, Lucy R. / Taylor-Joyce, Grace / Stark, Richard / Baxter, Laura / Alam, Mohammad T. / Brown, Paul E. / McClure, Patrick C. / Chappell, Joseph G. / Tsoleridis, Theocharis / Ball, Jonathan / Gramatopoulos, Dimitris / Buck, David / Todd, John A. / Green, Angie / Trebes, Amy / MacIntyre-Cockett, George / de Cesare, Mariateresa / Langford, Cordelia / Alderton, Alex / Amato, Roberto / Goncalves, Sonia / Jackson, David K. / Johnston, Ian / Sillitoe, John / Palmer, Steve / Lawniczak, Mara / Berriman, Matt / Danesh, John / Livett, Rich / Shirley, Lesley / Farr, Ben / Quail, Mike / Thurston, Scott / Park, Naomi / Betteridge, Emma / Weldon, Danni / Goodwin, Scott / Nelson, Rachel / Beaver, Charlotte / Letchford, Laura / Jackson, David A. / Foulser, Luke / McMinn, Liz / Prestwood, Liam / Kay, Sally / Kane, Leanne / Dorman, Matthew J. / Martincorena, Inigo / Puethe, Christoph / Keatley, Jon-Paul / Tonkin-Hill, Gerry / Smith, Christen / Jamrozy, Dorota / Beale, Mathew A. / Patel, Minal / Ariani, Cristina / Spencer-Chapman, Michael / Drury, Eleanor / Lo, Stephanie / Rajatileka, Shavanthi / Scott, Carol / James, Keith / Buddenborg, Sarah K. / Berger, Duncan J. / Patel, Gaurang / Garcia-Casado, Maria V. / Dibling, Thomas / McGuigan, Samantha / Rogers, Hazel A. / Hunter, Adam D. / Souster, Emily / Neaverson, Alexandra S.

    Cell. 2021 Jan. 07, v. 184, no. 1 p.64-75.e11

    2021  

    Abstract: Global dispersal and increasing frequency of the SARS-CoV-2 spike protein variant D614G are suggestive of a selective advantage but may also be due to a random founder effect. We investigate the hypothesis for positive selection of spike D614G in the ... ...

    Körperschaft COG-UK Consortium
    Abstract Global dispersal and increasing frequency of the SARS-CoV-2 spike protein variant D614G are suggestive of a selective advantage but may also be due to a random founder effect. We investigate the hypothesis for positive selection of spike D614G in the United Kingdom using more than 25,000 whole genome SARS-CoV-2 sequences. Despite the availability of a large dataset, well represented by both spike 614 variants, not all approaches showed a conclusive signal of positive selection. Population genetic analysis indicates that 614G increases in frequency relative to 614D in a manner consistent with a selective advantage. We do not find any indication that patients infected with the spike 614G variant have higher COVID-19 mortality or clinical severity, but 614G is associated with higher viral load and younger age of patients. Significant differences in growth and size of 614G phylogenetic clusters indicate a need for continued study of this variant.
    Schlagwörter COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; data collection ; founder effect ; genetic analysis ; genome ; mortality ; mutation ; pathogenicity ; phylogeny ; viral load ; United Kingdom ; COVID-19 ; SARS-CoV-2 ; evolution ; epidemiology ; spike
    Sprache Englisch
    Erscheinungsverlauf 2021-0107
    Umfang p. 64-75.e11.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel ; Online
    Anmerkung NAL-AP-2-clean
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2020.11.020
    Datenquelle NAL Katalog (AGRICOLA)

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