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Yang, Bowen ; Goh, Yin Min ; Sung, Suk Hyun ; Ye, Gaihua ; Biswas, Sananda ; Kaib, David A. S. ; Dhakal, Ramesh ; Yan, Shaohua ; Li, Chenghe ; Jiang, Shengwei ; Chen, Fangchu ; Lei, Hechang ; He, Rui ; Valentí, Roser ; Winter, Stephen M. ; Hovden, Robert ; Tsen, Adam W.
Layered {\alpha}-RuCl3 is a promising material to potentially realize the long-sought Kitaev quantum spin liquid with fractionalized excitations. While evidence of this exotic state has been reported under a modest in-plane magnetic field, such behavior is largely inconsistent with theoretical expectations of Kitaev phases emerging only in out-of-plane fields. These predicted field-induced states have been mostly out of reach due to the strong easy-plane anisotropy of bulk crystals, however. We use a combination of tunneling spectroscopy, magnetotransport, electron diffraction, and ab initio calculations to study the layer-dependent magnons, anisotropy, structure, and exchange coupling in atomically thin samples. Due to structural distortions, the sign of the average off-diagonal exchange changes in monolayer {\alpha}-RuCl3, leading to a reversal of magnetic anisotropy to easy-axis. Our work provides a new avenue to tune the magnetic interactions in {\alpha}-RuCl3 and allows theoretically predicted quantum spin liquid phases for out-of-plane fields to be more experimentally accessible.
Welzel, Tania Mara ; Yang, Min ; Sajeev, Gautam ; Chen, Yaozhu J. ; Pinsky, Brett ; Bao, Yanjun ; Wu, Eric Q. ; Dieterich, Douglas
Introduction: The new direct acting antiviral (DAA) therapies are able to effectively treat chronic hepatitis C (CHC). This study elicited the preferences of CHC patients for treatment attributes of new DAAs.
Methods: An online discrete choice experiment survey was designed to collect data from adult CHC patients in the USA, UK, France, Germany, Spain, and Italy. Patients were asked to choose from alternative hypothetical DAA options, defined by differing levels of nine attributes [i.e., treatment duration, tablet count and packaging, cure rate, required office visits when on treatment, modifications to statins or to proton pump inhibitors (PPIs), and risks of diarrhea, headache and nausea]. Logistic regression was used to assess preference for the treatment options.
Results: A total of 328 patients with CHC completed the survey (USA, n = 227; European countries, n = 101), with a mean age of 47.7 years (SD = 14.4) and an average 11.2 years since CHC diagnosis; 51% of patients were female. More than half (60%) of the patients had treatment for CHC. Patients significantly preferred a DAA regimen with higher cure rate, shorter treatment duration, lower risks of diarrhea, headache, and nausea (all p < 0.001), reduced need for office visits when on treatment (p = 0.044), and without requiring dose reduction or timing change in PPIs (p = 0.032). Tablet counts were not found to be statistically significant.
Conclusion: Given the overall high cure rates of new DAAs, CHC patients' preferences for therapy may be influenced by treatment attributes other than cure rates and tolerability. Treatments that are more convenient and require less disruption to their daily life (e.g., shorter treatment duration, no modification in PPI use, and fewer office visits when on treatment) are important to patients with CHC and should be considered when making treatment decisions.
The genus Parandes Muir, 1925 (Cixiinae, Andini) is recorded from China for the first time with two new species, Parandes circinatus Wang & Chen sp. nov. and Parandes fuscus Wang & Chen sp. nov. Color images for the adults of the two new species and line drawings for the genitalia are provided. A key is presented to separate all species within the genus.
Randall, Joshua C. ; Winkler, Thomas W. ; Kutalik, Zoltán ; I. Berndt, Sonja ; Jackson, Anne U. ; Monda, Keri L. ; Kilpeläinen, Tuomas O. ; Esko, Tõnu ; Mägi, Reedik ; Li, Shengxu ; Workalemahu, Tsegaselassie ; Feitosa, Mary F. ; Croteau-Chonka, Damien C. ; Day, Felix R. ; Fall, Tove ; Ferreira, Teresa ; Gustafsson, Stefan ; Locke, Adam E. ; Mathieson, Iain ; Scherag, André ; Vedantam, Sailaja ; Wood, Andrew R. ; Liang, Liming ; Steinthorsdottir, Valgerdur ; Thorleifsson, Gudmar ; Dermitzakis, Emmanouil T. ; Dimas, Antigone S. ; Karpe, Fredrik ; Min, Josine L. ; Nicholson, George ; Clegg, Deborah J. ; Person, Thomas ; Krohn, Jon P. ; Bauer, Sabrina ; Buechler, Christa ; Eisinger, Kristina ; Bonnefond, Amélie ; Froguel, Philippe ; Hottenga, Jouke-Jan ; Prokopenko, Inga ; Waite, Lindsay L. ; Harris, Tamara B. ; Smith, Albert Vernon ; Shuldiner, Alan R. ; McArdle, Wendy L. ; Caulfield, Mark J. ; Munroe, Patricia B. ; Grönberg, Henrik ; Chen, Yii-Der Ida ; Li, Guo ; Beckmann, Jacques S. ; Johnson, Toby ; Thorsteinsdottir, Unnur ; Teder-Laving, Maris ; Khaw, Kay-Tee ; Wareham, Nicholas J. ; Zhao, Jing Hua ; Amin, Najaf ; Oostra, Ben A. ; Kraja, Aldi T. ; Province, Michael A. ; Cupples, L. Adrienne ; Heard-Costa, Nancy L. ; Kaprio, Jaakko ; Ripatti, Samuli ; Surakka, Ida ; Collins, Francis S. ; Saramies, Jouko ; Tuomilehto, Jaakko ; Jula, Antti ; Salomaa, Veikko ; Erdmann, Jeanette ; Hengstenberg, Christian ; Loley, Christina ; Schunkert, Heribert ; Lamina, Claudia ; Wichmann, Heinz Erich ; Albrecht, Eva ; Gieger, Christian ; Hicks, Andrew A. ; Johansson, Åsa ; Pramstaller, Peter P. ; Kathiresan, Sekar ; Speliotes, Elizabeth K. ; Penninx, Brenda W. J. H. ; Hartikainen, Anna-Liisa ; Jarvelin, Marjo-Riitta ; Gyllensten, Ulf ; Boomsma, Dorret I. ; Campbell, Harry ; Wilson, James F. ; Chanock, Stephen J. ; Farrall, Martin ; Goel, Anuj ; Medina-Gomez, Carolina ; Rivadeneira, Fernando ; Estrada, Karol ; Uitterlinden, André G. ; Hofman, Albert ; Zillikens, M. Carola ; Heijer, Martin den ; Kiemeney, Lambertus Adrianus ; Maschio, Andrea ; Hall, Per ; Tyrer, Jonathan ; Teumer, Alexander ; Völzke, Henry ; Kovacs, Peter ; Tönjes, Anke ; Mangino, Massimo ; Spector, Tim D. ; Hayward, Caroline ; Rudan, Igor ; Hall, Alistair S. ; Samani, Nilesh J. ; Attwood, Antony Paul ; Sambrook, Jennifer G. ; Hung, Joseph ; Palmer, Lyle J. ; Lokki, Marja-Liisa ; Sinisalo, Juha ; Boucher, Gabrielle ; Huikuri, Heikki ; Lorentzon, Mattias ; Ohlsson, Claes ; Eklund, Niina ; Eriksson, Johan G. ; Barlassina, Cristina ; Rivolta, Carlo ; Nolte, Ilja M. ; Snieder, Harold ; Klauw, Melanie M. van der ; Vliet-Ostaptchouk, Jana V. van ; Gejman, Pablo V. ; Shi, Jianxin ; Jacobs, Kevin B. ; Wang, Zhaoming ; Bakker, Stephan J. L. ; Mateo Leach, Irene ; Navis, Gerjan ; Harst, Pim van der ; Martin, Nicholas Gordon ; Medland, Sarah E. ; Montgomery, Grant W. ; Yang, Jian ; Chasman, Daniel I. ; Ridker, Paul M. ; Rose, Lynda M. ; Lehtimäki, Terho ; Raitakari, Olli ; Absher, Devin ; Iribarren, Carlos ; Basart, Hanneke ; Hovingh, Kees G. ; Hyppönen, Elina ; Power, Chris ; Power, Chris ; Anderson, Denise ; Beilby, John P. ; Hui, Jennie ; Jolley, Jennifer ; Sager, Hendrik ; Bornstein, Stefan R. ; Schwarz, Peter E. H. ; Kristiansson, Kati ; Perola, Markus ; Lindström, Jaana ; Swift, Amy J. ; Uusitupa, Matti ; Atalay, Mustafa ; Lakka, Timo A. ; Rauramaa, Rainer ; Bolton, Jennifer L. ; Fowkes, Gerry ; Fraser, Ross M. ; Price, Jackie F. ; Fischer, Krista ; KrjutÅ¡kov, Kaarel ; Metspalu, Andres ; Mihailov, Evelin ; Langenberg, Claudia ; Luan, Jian'an ; Ong, Ken K. ; Chines, Peter S. ; Keinanen-Kiukaanniemi, Sirkka M. ; Saaristo, Timo E. ; Edkins, Sarah ; Franks, Paul W. ; Hallmans, Göran ; Shungin, Dmitry ; Morris, Andrew David ; Palmer, Colin N. A. ; Erbel, Raimund ; Moebus, Susanne ; Nöthen, Markus Maria ; Pechlivanis, Sonali ; Hveem, Kristian ; Narisu, Narisu ; Hamsten, Anders ; Humphries, Steve E. ; Strawbridge, Rona J. ; Tremoli, Elena ; Grallert, Harald ; Thorand, Barbara ; Illig, Thomas ; Koenig, Wolfgang ; Müller-Nurasyid, Martina ; Peters, Annette ; Böhm, Bernhard O. ; Kleber, Marcus E. ; März, Winfried ; Winkelmann, Bernhard R. ; Kuusisto, Johanna ; Laakso, Markku ; Arveiler, Dominique ; Cesana, Giancarlo ; Kuulasmaa, Kari ; Virtamo, Jarmo ; Yarnell, John W. G. ; Kuh, Diana ; Wong, Andrew ; Lind, Lars ; Faire, Ulf de ; Gigante, Bruna ; Magnusson, Patrik K. E. ; Pedersen, Nancy L. ; Dedoussis, George ; Dimitriou, Maria ; Kolovou, Genovefa ; Kanoni, Stavroula ; Stirrups, Kathleen ; Bonnycastle, Lori L. ; Njølstad, Inger ; Wilsgaard, Tom ; Ganna, Andrea ; Rehnberg, Emil ; Hingorani, Aroon ; Kivimaki, Mika ; Kumari, Meena ; Assimes, Themistocles L. ; Barroso, Inês ; Boehnke, Michael ; Borecki, Ingrid B. ; Deloukas, Panos ; Fox, Caroline S. ; Frayling, Timothy ; Groop, Leif C. ; Haritunians, Talin ; Hunter, David ; Ingelsson, Erik ; Kaplan, Robert ; Mohlke, Karen L. ; North, Kari E. ; Lindgren, Cecilia M. ; Qi, Lu ; Loos, Ruth J. F. ; Heid, Iris M. ; Hirschhorn, Joel N. ; McCarthy, Mark I. ; Abecasis, Gonçalo R. ; Stefansson, Kari ; Strachan, David P. ; Schlessinger, David ; O'Connell, Jeffrey R. ; Duijn, Cornelia M. van
Men and women differ substantially regarding height, weight, and body fat. Interestingly, previous work detecting genetic effects for waist-to-hip ratio, to assess body fat distribution, has found that many of these showed sex-differences. However, systematic searches for sex-differences in genetic effects have not yet been conducted. Therefore, we undertook a genome-wide search for sexually dimorphic genetic effects for anthropometric traits including 133,723 individuals in a large meta-analysis and followed promising variants in further 137,052 individuals, including a total of 94 studies. We identified seven loci with significant sex-difference including four previously established (near GRB14/COBLL1, LYPLAL1/SLC30A10, VEGFA, ADAMTS9) and three novel anthropometric trait loci (near MAP3K1, HSD17B4, PPARG), all of which were significant in women, but not in men. Of interest is that sex-difference was only observed for waist phenotypes, but not for height or body-mass-index. We found no evidence for sex-differences with opposite effect direction for men and women. The PPARG locus is of specific interest due to its link to diabetes genetics and therapy. Our findings demonstrate the importance of investigating sex differences, which may lead to a better understanding of disease mechanisms with a potential relevance to treatment options.
The ABC transporter Mdl1p, a structural and functional homologue of the transporter associated with antigen processing (TAP) plays an important role in intracellular peptide transport from the mitochondrial matrix of Saccharomyces cerevisiae. To characterize the ATP hydrolysis cycle of Mdl1p, the nucleotide-binding domain (NBD) was overexpressed in Escherichia coli and purified to homogeneity. The isolated NBD was active in ATP binding and hydrolysis with a turnover of 25 ATP per minute and a Km of 0.6 mm and did not show cooperativity in ATPase activity. However, the ATPase activity was non-linearly dependent on protein concentration (Hill coefficient of 1.7), indicating that the functional state is a dimer. Dimeric catalytic transition states could be trapped either by incubation with orthovanadate or beryllium fluoride, or by mutagenesis of the NBD. The nucleotide composition of trapped intermediate states was determined using [alpha-32P]ATP and [gamma-32P]ATP. Three different dimeric intermediate states were isolated, containing either two ATPs, one ATP and one ADP, or two ADPs. Based on these experiments, it was shown that: (i) ATP binding to two NBDs induces dimerization, (ii) in all isolated dimeric states, two nucleotides are present, (iii) phosphate can dissociate from the dimer, (iv) both nucleotides are hydrolyzed, and (v) hydrolysis occurs in a sequential mode. Based on these data, we propose a processive-clamp model for the catalytic cycle in which association and dissociation of the NBDs depends on the status of bound nucleotides.
The transporter associated with antigen processing (TAP) is a key component of the cellular immune system. As a member of the ATP-binding cassette (ABC) superfamily, TAP hydrolyzes ATP to energize the transport of peptides from the cytosol into the lumen of the endoplasmic reticulum. TAP is composed of TAP1 and TAP2, each containing a transmembrane domain and a nucleotide-binding domain (NBD). Here we investigated the role of the ABC signature motif (C-loop) on the functional non-equivalence of the NBDs, which contain a canonical C-loop (LSGGQ) for TAP1 and a degenerate C-loop (LAAGQ) for TAP2. Mutation of the leucine or glycine (LSGGQ) in TAP1 fully abolished peptide transport. However, TAP complexes with equivalent mutations in TAP2 still showed residual peptide transport activity. To elucidate the origin of the asymmetry of the NBDs of TAP, we further examined TAP complexes with exchanged C-loops. Strikingly, the chimera with two canonical C-loops showed the highest transport rate whereas the chimera with two degenerate C-loops had the lowest transport rate, demonstrating that the ABC signature motifs control peptide transport efficiency. All single site mutants and chimeras showed similar activities in peptide or ATP binding, implying that these mutations affect the ATPase activity of TAP. In addition, these results prove that the serine of the C-loop is not essential for TAP function but rather coordinates, together with other residues of the C-loop, the ATP hydrolysis in both nucleotide-binding sites.
The transporter associated with antigen processing (TAP) plays a key role in the adaptive immune response by pumping antigenic peptides into the endoplasmic reticulum for subsequent loading of major histocompatibility complex class I molecules. TAP is a heterodimer consisting of TAP1 and TAP2. Each subunit is composed of a transmembrane domain and a nucleotide-binding domain, which energizes the peptide transport. To analyze ATP hydrolysis of each subunit we developed a method of trapping 8-azido-nucleotides to TAP in the presence of phosphate transition state analogs followed by photocross-linking, immunoprecipitation, and high resolution SDS-PAGE. Strikingly, trapping of both TAP subunits by beryllium fluoride is peptide-specific. The peptide concentration required for half-maximal trapping is identical for TAP1 and TAP2 and directly correlates with the peptide binding affinity. Only a background level of trapping was observed for low affinity peptides or in the presence of the herpes simplex viral protein ICP47, which specifically blocks peptide binding to TAP. Importantly, the peptide-induced trapped state is reached after ATP hydrolysis and not in a backward reaction of ADP binding and trapping. In the trapped state, TAP can neither bind nor exchange nucleotides, whereas peptide binding is not affected. In summary, these data support the model that peptide binding induces a conformation that triggers ATP hydrolysis in both subunits of the TAP complex within the catalytic cycle.
The transporter associated with antigen processing (TAP) plays a pivotal role in the adaptive immune response against virus-infected or malignantly transformed cells. As member of the ABC transporter family, TAP hydrolyzes ATP to energize the transport of antigenic peptides from the cytosol into the lumen of the endoplasmic reticulum. TAP forms a heterodimeric complex composed of TAP1 and TAP2 (ABCB2/3). Both subunits contain a hydrophobic transmembrane domain and a hydrophilic nucleotide-binding domain. The aim of this work was to study the ATP hydrolysis event of the TAP complex and gain further insights into the mechanism of peptide transport process. To analyze ATP hydrolysis of each subunit I developed a method of trapping 8- azido-nucleotides to TAP in the presence of phosphate transition state analogs followed by photocross-linking, immunoprecipitation, and high-resolution SDS-PAGE. Strikingly, trapping of both TAP subunits by beryllium fluoride is peptide-specific. The peptide concentration required for half-maximal trapping is identical for TAP1 and TAP2 and directly correlates with the peptide-binding affinity. Only background levels of trapping were observed for low affinity peptides or in the presence of the herpes simplex viral protein ICP47, which specifically blocks peptide binding to TAP. Importantly, the peptideinduced trapped state is reached after ATP hydrolysis and not in a backward reaction of ADP binding and trapping. In the trapped state, TAP can neither bind nor exchange nucleotides, whereas peptide binding is not affected. In summary, these data support the model that peptide binding induces a conformation that triggers ATP hydrolysis in both subunits of the TAP complex within the catalytic cycle. The role of the ABC signature motif (C-loop) on the functional non-equivalence of the NBDs was investigated. The C-loops of TAP transporter contain a canonical C-loop (LSGGQ) for TAP1 and a degenerated ABC signature motif (LAAGQ) for TAP2. Mutation of the leucine or glycine (LSGGQ) in TAP1 fully abolished peptide transport. TAP complexes with equivalent mutations in TAP2 showed however still residual peptide transport activity. To elucidate the origin of the asymmetry of the NBDs of TAP, we further examined TAP complexes with exchanged C-loops. Strikingly, the chimera with two canonical C-loops showed the highest transport rate whereas the chimera with two degenerated C-loops had the lowest transport rate, demonstrating that the ABC signature motifs control the peptide transport efficiency. All single-site mutants and chimeras showed similar activities in peptide or ATP binding, implying that these mutations affect the ATPase activity of TAP. In addition, these results prove that the serine of the C-loop is not essential for TAP function, but rather coordinates, together with other residues of the C-loop, the ATP hydrolysis in both nucleotide-binding sites. To study the coupling between the ATP binding/hydrolysis and the peptide binding, the putative catalytic bases of the TAP complex were mutated to generate the so-called EQ mutants. The mutations did not influence the peptide-binding ability. Dimerization of the NBDs of EQ mutants upon ATP binding does not alter the peptide binding property. At 27°C, both ATP and ADP could induce the loss of peptide-binding ability (Bmax) only in the variants bearing a mutated TAP2. Further studies are required to deduce at which stage in the catalytic cycle the peptide-binding site is affected. In addition, mutation of the putative catalytic base of both subunits showed a magnesium-dependent peptide transport activity, demonstrating these mutants did not abolish the ATP hydrolysis. Thus, the function of this acidic residue as the catalytic base is not likely to be universe for all ABC transporters.
Acharya, Shreyasi ; Adamová, Dagmar ; Aglieri Rinella, Gianluca ; Agnello, Michelangelo ; Agrawal, Neelima ; Ahammed, Zubayer ; Ahmad, Shakeel ; Ahn, Sang Un ; Ahuja, Ishaan ; Akindinov, Alexander ; Al-Turany, Mohammad ; Aleksandrov, Dmitry ; Alessandro, Bruno ; Alfanda, Haidar Mas’ud ; Alfaro Molina, Jose Ruben ; Ali, Bushra ; Alici, Andrea ; Alizadehvandchali, Negin ; Alkin, Anton ; Alme, Johan ; Alocco, Giacomo ; Alt, Torsten ; Altamura, Anna Rita ; Altsybeev, Igor ; Anaam, Mustafa Naji ; Andrei, Cristian ; Andreou, Nicodemos ; Andronic, Anton ; Andronov, Evgeny ; Anguelov, Venelin ; Antinori, Federico ; Antonioli, Pietro ; Apadula, Nicole ; Aphecetche, Laurent Bernard ; Appelshäuser, Harald ; Arata, Carolina ; Arcelli, Silvia ; Aresti, Mauro ; Arnaldi, Roberta ; Arneiro, Jhoao Gabriel Martins Campos Almeida ; Arsene, Ionut Cristian ; Arslandok, Mesut ; Augustinus, Andre ; Averbeck, Ralf Peter ; Azmi, Mohd Danish ; Baba, Hitoshi ; Badalà, Angela ; Bae, Joonsuk ; Baek, Yong Wook ; Bai, Xiaozhi ; Bailhache, Raphaëlle ; Bailung, Yoshini ; Bala, Renu ; Balbino, Alessandro ; Baldisseri, Alberto ; Balis, Bartosz ; Banerjee, Debjani ; Banoo, Zarina ; Barile, Francesco ; Barioglio, Luca ; Barlou, Maria ; Barman, Banajit ; Barnaföldi, Gergely Gábor ; Barnby, Lee Stuart ; Barreau, Emilie Martine ; Ramillien Barret, Valerie ; Barreto De Oliveira Campos, Leonardo ; Bartels, Clara ; Barth, Klaus ; Bartsch, Esther ; Bastid, Nicole ; Basu, Sumit ; Batigne, Guillaume ; Battistini, Daniel ; Batyunya, Boris ; Bauri, Dibakar ; Bazo Alba, José Luis ; Bearden, Ian Gardner ; Beattie, Caitlin ; Becht, Pascal ; Behera, Debadatta ; Belikov, Iouri ; Bell Hechavarria, Ailec de la Caridad ; Bellini, Francesca ; Bellwied, Rene ; Belokurova, Svetlana ; Espinoza Beltran, Lucina Gabriela ; Vasquez Beltran, Yael Antonio ; Bencédi, Gyula ; Beolè, Stefania ; Berdnikov, Yaroslav ; Berdnikova, Anastasia ; Bergmann, Luisa ; Besoiu, Mihaela Gabriela ; Betev, Latchezar ; Bhaduri, Partha Pratim ; Bhasin, Anju ; Bhat, Mohammad Asif ; Bhattacharjee, Buddhadeb ; Bianchi, Livio ; Bianchi, Nicola ; Bielčík, Jaroslav ; Bielčíková, Jana ; Bigot, Alexandre Patrick ; Bilandzic, Ante ; Biro, Gabor ; Biswas, Saikat ; Bize, Nicolas Luc ; Blair, Justin Thomas ; Blau, Dmitry S. ; Blidaru, Mihail-Bogdan ; Bluhme, Nora ; Blume, Christoph ; Boca, Gianluigi ; Bock, Friederike ; Bodova, Tea ; Boi, Stefano ; Bok, Jeongsu ; Boldizsar, Laszlo ; Bombara, Marek ; Bond, Peter Matthew ; Bonomi, Germano ; Borel, Herve ; Borissov, Alexander ; Borquez Carcamo, Andres Gerardo ; Bossi, Hannah ; Botta, Elena ; El Mard Bouziani, Youssef ; Bratrud, Lars ; Braun-Munzinger, Peter ; Bregant, Marco ; Broz, Michal ; Bruno, Giuseppe Eugenio ; Buckland, Matthew Daniel ; Budnikov, Dmitry ; Büsching, Henner ; Bufalino, Stefania ; Bühler, Paul ; Burmasov, Nazar ; Buthelezi, Edith Zinhle ; Bylinkin, Alexander ; Bysiak, Sebastian Adam ; Cabanillas Noris, Juan Carlos ; Cai, Mengke ; Caines, Helen Louise ; Caliva, Alberto ; Calvo Villar, Ernesto ; Mejia Camacho, Juan Manuel ; Camerini, Paolo ; Canedo, Fabio de Moraes Canedo ; Carabas, Mihai ; Amatriain Carballo, Aitor ; Carnesecchi, Francesca ; Caron, Robin Albert Andre ; Abranches De Carvalho, Leopoldo ; Castillo Castellanos, Javier Ernesto ; Catalano, Fabio ; Ceballos Sanchez, Cesar ; Chakaberia, Irakli ; Chakraborty, Pritam ; Chandra, Sinjini ; Chapeland, Sylvain ; Chartier, Marielle ; Chattopadhyay, Subhasis ; Chattopadhyay, Sukalyan ; García Chávez, Tonatiuh ; Cheng, Tiantian ; Cheshkov, Cvetan Valeriev ; Cheynis, Brigitte ; Chibante Barroso, Vasco Miguel ; Chinellato, David Dobrigkeit ; Chizzali, Emma Sophia ; Cho, Jaeyoon ; Cho, Soyeon ; Chochula, Peter ; Choudhury, Dhrubajyoti ; Christakoglou, Panagiotis ; Christensen, Christian Holm ; Christiansen, Peter L. ; Chujo, Tatsuya ; Ciacco, Mario ; Cicalò, Corrado ; Ciupek, Michael Rudolf ; Clai, Giulia ; Colamaria, Fabio Filippo ; Colburn, Jonathan Samuel ; Colella, Domenico ; Colocci, Manuel ; Concas, Matteo ; Conesa Balbastre, Gustavo ; Conesa Del Valle, Zaida ; Contin, Giacomo ; Contreras Nuno, Jesus Guillermo ; Coquet, Maurice Louis ; Cortese, Pietro ; Cosentino, Mauro Rogerio ; Costa, Filippo ; Costanza, Susanna ; Cot, Corentin ; Crkovská, Jana ; Crochet, Philippe ; Cruz Torres, Reynier ; Cui, Pengyao ; Dainese, Andrea ; Danisch, Meike Charlotte ; Danu, Andrea ; Das, Prottay ; Das, Prottoy ; Das, Supriya ; Dash, Archita Rani ; Dash, Sadhana ; Regules Medel, Hector David ; De Caro, Annalisa ; De Cataldo, Giacinto ; Cuveland, Jan de ; De Falco, Alessandro ; De Gruttola, Daniele ; De Marco, Nora ; De Martin, Chiara ; De Pasquale, Salvatore ; Deb, Rohaan ; Del Grande, Raffaele ; Dello Stritto, Luigi ; Deng, Wenjing ; Dhankher, Preeti ; Di Bari, Domenico ; Di Mauro, Antonio ; Diab, Batoul ; Arteche Diaz, Raul ; Dietel, Thomas ; Ding, Yanchun ; Ditzel, Janik ; Divià, Roberto ; Dixit, Dhruv Utpalkumar ; Djuvsland, Øystein ; Dmitrieva, Uliana ; Dobrin, Alexandru Florin ; Donigus, Benjamin ; Dubinski, Jan Michal ; Dubla, Andrea ; Dudi, Sandeep ; Dupieux, Pascal ; Durkac, Martin ; Dzalaiova, Natalia ; Eder, Tabea Maria ; Ehlers, Raymond James, III ; Eisenhut, Florian ; Ejima, Ren ; Elia, Domenico ; Erazmus, Barbara Ewa ; Ercolessi, Francesca ; Espagnon, Bruno ; Eulisse, Giulio ; Evans, David ; Evdokimov, Sergey ; Fabbietti, Laura ; Faggin, Mattia ; Faivre, Julien ; Fan, Feng ; Fan, Wenqing ; Fantoni, Alessandra ; Fasel, Markus ; Feliciello, Alessandro ; Feofilov, Grigori A. ; Fernández Téllez, Arturo ; Ferrandi De Oliveira, Lucas ; Bertran Ferrer, Marta ; Ferrero, Andrea ; Ferrero, Chiara ; Ferretti, Alessandro ; Feuillard, Victor Jose Gaston ; Filova, Vendulka ; Finogeev, Dmitry ; Fionda, Fiorella Maria Celeste ; Flatland, Erlend ; Flor, Fernando Antonio ; Flores, Amanda Nicole ; Foertsch, Siegfried Valentin ; Fokin, Ilya ; Fokin, Sergey ; Fragiacomo, Enrico ; Frajna, Eszter ; Fuchs, Ulrich ; Funicello, Nicola ; Furget, Christophe ; Furs, Artur ; Fusayasu, Takahiro ; Gaardhoeje, Jens Joergen ; Gagliardi, Martino ; Gago Medina, Alberto Martín ; Gahlaut, Tanu ; Duarte Galvan, Carlos ; Gangadharan, Dhevan Raja ; Ganoti, Paraskevi ; Garabatos Cuadrado, Jose Maria ; Tavira Garcia, Andrea ; Alvarado Garcia, Jesús Ricardo ; Garcia-Solis, Edmundo Javier ; Gargiulo, Corrado ; Gasik, Piotr ; Gautam, Amrit ; Ducati, Maria Beatriz de Leone Gay ; Germain, Marie ; Ghimouz, Abderrahmane ; Ghosh, Chandrasekhar ; Giacalone, Marco ; Gioachin, Giulia ; Giubellino, Paolo ; Giubilato, Piero ; Glaenzer, Aude Marie Camille ; Glässel, Peter ; Glimos, Ewa ; Goh, Daniel Jia Qin ; Gonzalez Sebastian, Victor Luis ; Gordeev, Pavel ; Gorgon, Marek Boguslaw ; Goswami, Kangkan ; Gotovac, Sven ; Grabski, Varlen ; Graczykowski, Łukasz Kamil ; Grecka, Ekaterina ; Grelli, Alessandro ; Grigoraș, Costin ; Grigoryev, Vladislav ; Grigoryan, Smbat ; Grosa, Fabrizio ; Große-Oetringhaus, Jan Fiete ; Grosso, Raffaele ; Grund, David ; Grünwald, Nadine Alice ; Garcia Guardiano, Gabriel ; Guernane, Rachid ; Guilbaud, Maxime Rene Joseph ; Gulbrandsen, Kristjan Herlache ; Gündem, Tuba ; Gunji, Taku ; Guo, Wenda ; Gupta, Anik ; Gupta, Ramni ; Gupta, Rashi ; Paisano Guzman, Sergio ; Gwizdziel, Katarzyna ; Gyulai, Laszlo ; Hadjidakis, Cynthia Marie ; Haider, Fakhar Ul ; Haidlova, Sara ; Haldar, Mintu ; Hamagaki, Hideki ; Hamdi, Abdennacer ; Han, Younghoon ; Hanley, Brian Gerald ; Hannigan, Ryan ; Hansen, Joachim ; Harris, John William ; Harton, Austin Vincent ; Hartung, Michael Volker ; Hassan, Hadi ; Hatzifotiadou, Despina ; Hauer, Philip ; Havener, Laura Brittany ; Hellbär, Ernst ; Helstrup, Håvard ; Hemmer, Marvin ; Herman, Tomáš ; Herrera Corral, Gerardo Antonio ; Herrmann, Florian ; Herrmann, Sarah Nina Edwige ; Hetland, Kristin Fanebust ; Heybeck, Benedict ; Hillemanns, Hartmut ; Hippolyte, Boris ; Hoffmann, Felix Willi ; Hofman, Bas ; Hong, Geunhee ; Horst, Maximilian ; Horzyk, Adrian ; Hou, Yongzhen ; Hristov, Peter ; Hughes, Charles ; Huhn, Patrick ; Huhta, Laura Maria ; Humanic, Thomas J. ; Hutson, Alek ; Hutter, Dirk ; Hwang, Minyoung Chris ; Ilkaev, Radiy ; Ilyas, Hira ; Inaba, Motoi ; Innocenti, Gian Michele ; Ippolitov, Mikhail ; Isakov, Artem ; Isidori, Tommaso ; Islam, Md Samsul ; Ivanov, Marian ; Ivanov, Marian ; Ivanov, Vladimir ; Iversen, Kaare Endrup ; Jablonski, Miroslaw ; Jacak, Barbara ; Jacazio, Nicolò ; Jacobs, Peter Martin ; Jadlovska, Slavka ; Jadlovsky, Jan ; Jaelani, Syaefudin ; Jahnke, Cristiane ; Jakubowska, Monika Joanna ; Janik, Malgorzata Anna ; Janson, Thomas ; Ji, Su-jeong ; Jia, Shihai ; Paz Jimenez, Alom Antonio ; Jonas, Florian ; Jones, Daniel Matthew ; Jowett, John M. ; Jung, Jerome ; Jung, Michael ; Junique, Antoine Jean-Simon ; Jusko, Anton ; Karwowska, Maja Jadwiga ; Kaewjai, Jetnipit ; Kalinak, Peter ; Kalteyer, Annalena Sophie ; Kalweit, Alexander Philipp ; Karatović, David ; Karavichev, Oleg V. ; Karavicheva, Tatiana L. ; Karczmarczyk, Przemyslaw ; Karpechev, Evgeny ; Kebschull, Udo ; Keidel, Ralf ; Keijdener, Darius ; Keil, Markus ; Ketzer, Bernhard ; Khade, Swapnesh Santosh ; Khan, Ahsan Mehmood ; Khan, Shaista ; Khanzadeev, Alexei ; Kharlov, Yury ; Khatun, Anisa ; Khuntia, Arvind ; Khuranova, Zhanna ; Kileng, Bjarte ; Kim, Beomkyu ; Kim, Chong ; Kim, Dong Jo ; Kim, Eun Joo ; Kim, Jaehyun ; Kim, Jiyoung ; Kim, Junlee ; Kim, Minjung ; Kim, Se Yong ; Kim, Taejun ; Kimura, Kento ; Kirsch, Stefan ; Kisel, Ivan ; Kiselev, Sergej N. ; Kisiel, Adam Ryszard ; Kitowski, Jacek Pawel ; Klay, Jennifer Lynn ; Klein, Jochen ; Klein, Spencer Robert ; Klein-Bösing, Christian ; Kleiner, Matthias ; Klemenz, Thomas ; Kluge, Alexander ; Kobdaj, Chinorat ; Kollegger, Thorsten ; Kondratyev, Andrey ; Kondratyeva, Natalia ; König, Joshua Leon ; Königstorfer, Stephan Alexander ; Konopka, Piotr Jan ; Kornakov Van, Georgui ; Korwieser, Maximilian ; Koryciak, Sebastian Dominik ; Kotliarov, Artem ; Kovacic, Nino ; Kovalenko, Vladimir ; Kowalski, Marek ; Kozhuharov, Venelin Valeriev ; Králik, Ivan ; Kravčáková, Adela ; Krcal, Lubos ; Krivda, Marian ; Krizek, Filip ; Krizkova Gajdosova, Katarina ; Kroesen, Martin ; Krüger, Mario ; Krupová, Diana Maria ; Kryshen, Evgeny ; Kucera, Vit ; Kuhn, Christian Claude ; Kuijer, Paulus Gerardus ; Kumaoka, Takuya ; Kumar, Deekshit ; Kumar, Lokesh ; Kumar, Navneet ; Kumar, Shyam ; Kundu, Sourav ; Kurashvili, Podist ; Kurepin, Alexander ; Kurepin, Alexey B. ; Kuryakin, Alexey ; Kushpil, Svetlana ; Kuskov, Vladislav ; Kutyla, Monika ; Kweon, Min Jung ; Kwon, Youngil ; La Pointe, Sarah Louise ; La Rocca, Paola ; Lakrathok, Anantachai ; Lamanna, Massimo ; Landou, Aimeric Robin ; Langoy, Rune ; Larionov, Pavel ; Laudi, Elisa ; Lautner, Lukas ; Lavicka, Roman ; Lea, Ramona ; Lee, Hyungjun ; Legrand, Iosif-charles ; Legras, Gauthier ; Lehrbach, Johannes ; Lelek, Tomasz Marcin ; Lemmon, Roy Crawford ; Leon Monzon, Ildefonso ; Lesch, Marcel Markus ; Lesser, Ezra Douglas ; Lévai, Peter ; Li, Xiaomei ; Liang-gilman, Beatrice Eva ; Lien, Jørgen André ; Lietava, Roman ; Likmeta, Iris ; Lim, Bong-Hwi ; Lim, Sanghoon ; Lindenstruth, Volker ; Lindner, Amelia ; Lippmann, Christian ; Liu, Donghai ; Liu, Jian ; Setoue Liveraro, Gianni Shigeru ; Lofnes, Ingrid Mckibben ; Loizides, Constantinos ; Lokos, Sandor ; Lomker, Johanna ; Lončar, Petra ; Lopez, Xavier Bernard ; López Torres, Ernesto ; Lu, Pengzhong ; Lugo, Fabiola Viridiana ; Luhder, Jens Robert ; Lunardon, Marcello ; Luparello, Grazia ; Ma, Yu-Gang ; Mager, Magnus ; Maire, Antonin ; Makariev, Martin Vasilev ; Malaev, Mikhail ; Malfattore, Giovanni ; Malik, Nasir Mehdi ; Malik, Qasim Waheed ; Malik, Salman Khurshid ; Malinina, Liudmila ; Mallick, Dukhishyam ; Mallick, Neelkamal ; Mandaglio, Giuseppe ; Mandal, Sushobhan Kumar ; Manko, Vladislav ; Manso, Franck ; Manzari, Vito ; Mao, Yaxian ; Marcjan, Robert Waclaw ; Margagliotti, Giacomo Vito ; Margotti, Anselmo ; Marin, Ana Maria ; Markert, Christina ; Martinengo, Paolo ; Martínez Hernández, Mario Iván ; García Martínez, Ginés ; Martins Palhares, Maria Paula ; Masciocchi, Silvia ; Masera, Massimo ; Masoni, Alberto ; Massacrier, Laure Marie ; Massen, Olaf ; Mastroserio, Annalisa ; Matonoha, Oliver ; Mattiazzo, Serena ; Matyja, Adam Tomasz ; Mayer, Christoph ; Lafuente Mazuecos, Antonio ; Mazzaschi, Francesco ; Mazzilli, Marianna ; Mdhluli, Joyful Elma ; Melikyan, Yury ; Menchaca-rocha, Arturo Alejandro ; Munoz Mendez, Jesus Eduardo ; Meninno, Elisa ; Sasikumar Menon, Anjaly ; Meres, Michal ; Miake, Yasuo ; Micheletti, Luca ; Mihaylov, Dimitar Lubomirov ; Mikhaylov, Konstantin ; Miśkowiec, Dariusz Czesław ; Modak, Abhi ; Mohanty, Bedangadas ; Khan, Mohammed Mohisin ; Molander, Mikael Andreas ; Monira, Shirajum ; Mordasini, Cindy ; Moreira De Godoy Willems, Denise Aparecida ; Morozov, Igor ; Morsch, Andreas ; Mrnjavac, Teo ; Muccifora, Valeria ; Muhuri, Sanjib ; Mulligan, James Declan ; Mulliri, Alice ; Gameiro Munhoz, Marcelo ; Munzer, Robert Helmut ; Murakami, Hikari ; Murray, Sean ; Musa, Luciano ; Musinsky, Jan ; Myrcha, Julian Wojciech ; Naik, Bharati ; Nambrath, Anjali Ila ; Nandi, Basanta Kumar ; Nania, Rosario ; Nappi, Eugenio ; Nassirpour, Adrian Fereydon ; Nath, Abhishek ; Nattrass, Christine ; Naydenov, Momchil Nikolaev ; Neagu, Alexandra ; Negru, Adrian-eduard ; Nekrasova, Evgeniia ; Nellen, Lukas ; Nepeivoda, Roman ; Nese, Sigurd ; Nešković, Gvozden ; Nicassio, Nicola ; Nielsen, Borge Svane ; Nielsen, Emil Gorm ; Nikolaev, Sergey ; Nikulin, Sergey ; Nikulin, Vladimir ; Noferini, Francesco ; Noh, Seoyoung ; Nomokonov, Petr V. ; Norman, Jaime ; Novitzky, Norbert ; Nowakowski, Piotr ; Nyanin, Alexander ; Nystrand, Joakim Ingemar ; Oh, Saehanseul ; Ohlson, Alice ; Okorokov, Vitaly A. ; Oleniacz, Janusz ; Önnerstad, Anna ; Oppedisano, Chiara ; Ortiz Velasquez, Antonio ; Otwinowski, Jacek Tomasz ; Oya, Motomi ; Oyama, Ken ; Pachmayer, Yvonne C. ; Padhan, Sonali ; Pagano, Davide ; Paic, Guy ; Palasciano, Antonio ; Panebianco, Stefano Matthias ; Park, Hanseo ; Park, Hyebin ; Park, Jonghan ; Parkkila, Jasper Elias ; Patley, Yash ; Paul, Biswarup ; Pei, Hua ; Peitzmann, Thomas ; Peng, Xinye ; Pennisi, Michele ; Perciballi, Stefania ; Peresunko, Dmitry Yurevich ; Mesa Perez, Guillermo ; Pestov, Yury N. ; Petrov, Vitalii ; Petrovici, Mihai A. ; Pezzi, Rafael Peretti ; Piano, Stefano ; Pikna, Miroslav ; Pillot, Philippe ; Pinazza, Ombretta ; Pinsky, Lawrence ; Pinto, Chiara ; Pisano, Silvia ; Płoskoń, Mateusz ; Planinic, Mirko ; Pliquett, Fabian ; Poghosyan, Martin G. ; Polishchuk, Boris ; Politano, Stefano ; Poljak, Nikola ; Pop, Amalia ; Porteboeuf, Sarah Julie ; Pozdniakov, Valerii ; Yoval Pozos, Irandheny ; Pradhan, Kshitish Kumar ; Prasad, Sidharth Kumar ; Prasad, Suraj ; Preghenella, Roberto ; Prino, Francesco ; Pruneau, Claude A. ; Pshenichnov, Igor A. ; Puccio, Maximiliano ; Pucillo, Sara ; Pugelova, Zuzana ; Qiu, Shi ; Quaglia, Luca ; Ragoni, Simone ; Rai, Ananya ; Rakotozafindrabe, Andry Malala ; Ramello, Luciano ; Rami, Fouad ; Rodríguez Ramírez, Saúl Aníbal ; Rancien, Thibaut Albert ; Rasa, Marika ; Räsänen, Sami Sakari ; Rath, Rutuparna ; Rauch, Max Philip ; Ravasenga, Ivan ; Read, Kenneth Francis ; Reckziegel, Christian ; Redelbach, Andreas Ralph ; 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K+K− pairs may be produced in photonuclear collisions, either from the decays of photoproduced ϕ(1020) mesons, or directly as non-resonant K+K− pairs. Measurements of K+K− photoproduction probe the couplings between the ϕ(1020) and charged kaons with photons and nuclear targets. We present the first measurement of coherent photoproduction of K+K− pairs on lead ions in ultra-peripheral collisions using the ALICE detector, including the first investigation of direct K+K− production. There is significant K+K− production at low transverse momentum, consistent with coherent photoproduction on lead targets. In the mass range 1.1<MKK<1.4 GeV/c2 above the ϕ(1020) resonance, for rapidity |yKK|<0.8 and pT,KK<0.1 GeV/c, the measured coherent photoproduction cross section is dσ/dy = 3.37 ± 0.61 (stat.) ± 0.15 (syst.) mb. The centre-of-mass energy per nucleon of the photon-nucleus (Pb) system WγPb,n ranges from 33 to 188 GeV, far higher than previous measurements on heavy-nucleus targets. The cross section is larger than expected for ϕ(1020) photoproduction alone. The mass spectrum is fit to a cocktail consisting of ϕ(1020) decays, direct K+K− photoproduction, and interference between the two. The confidence regions for the amplitude and relative phase angle for direct K+K− photoproduction are presented.