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  1. Article ; Online: J-domain proteins: From molecular mechanisms to diseases.

    Marszalek, Jaroslaw / De Los Rios, Paolo / Cyr, Douglas / Mayer, Matthias P / Adupa, Vasista / Andréasson, Claes / Blatch, Gregory L / Braun, Janice E A / Brodsky, Jeffrey L / Bukau, Bernd / Chapple, J Paul / Conz, Charlotte / Dementin, Sébastien / Genevaux, Pierre / Genest, Olivier / Goloubinoff, Pierre / Gestwicki, Jason / Hammond, Colin M / Hines, Justin K /
    Ishikawa, Koji / Joachimiak, Lukasz A / Kirstein, Janine / Liberek, Krzysztof / Mokranjac, Dejana / Nillegoda, Nadinath / Ramos, Carlos H I / Rebeaud, Mathieu / Ron, David / Rospert, Sabine / Sahi, Chandan / Shalgi, Reut / Tomiczek, Bartlomiej / Ushioda, Ryo / Ustyantseva, Elizaveta / Ye, Yihong / Zylicz, Maciej / Kampinga, Harm H

    Cell stress & chaperones

    2023  Volume 29, Issue 1, Page(s) 21–33

    Abstract: J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how ...

    Abstract J-domain proteins (JDPs) are the largest family of chaperones in most organisms, but much of how they function within the network of other chaperones and protein quality control machineries is still an enigma. Here, we report on the latest findings related to JDP functions presented at a dedicated JDP workshop in Gdansk, Poland. The report does not include all (details) of what was shared and discussed at the meeting, because some of these original data have not yet been accepted for publication elsewhere or represented still preliminary observations at the time.
    MeSH term(s) HSP70 Heat-Shock Proteins/metabolism ; Molecular Chaperones/metabolism ; Poland ; HSP40 Heat-Shock Proteins/metabolism
    Chemical Substances HSP70 Heat-Shock Proteins ; Molecular Chaperones ; HSP40 Heat-Shock Proteins
    Language English
    Publishing date 2023-12-23
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1362749-1
    ISSN 1466-1268 ; 1355-8145
    ISSN (online) 1466-1268
    ISSN 1355-8145
    DOI 10.1016/j.cstres.2023.12.002
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4797: Show issues Location:
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  2. Article ; Online: Bacterial adaptation to cold: Conservation of a short J-domain co-chaperone and its protein partners in environmental proteobacteria.

    Weber, Lana / Gilat, Atar / Maillot, Nathanael / Byrne, Deborah / Arnoux, Pascal / Giudici-Orticoni, Marie-Thérèse / Méjean, Vincent / Ilbert, Marianne / Genest, Olivier / Rosenzweig, Rina / Dementin, Sébastien

    Environmental microbiology

    2023  Volume 25, Issue 11, Page(s) 2447–2464

    Abstract: Bacterial genomes are a huge reservoir of genes encoding J-domain protein co-chaperones ... AtcJ is a short J-domain protein that interacts with DnaK, but also with AtcC through its 21 amino acid ... represents a subfamily of short J-domain proteins that (i) are found in several environmental, mostly aquatic ...

    Abstract Bacterial genomes are a huge reservoir of genes encoding J-domain protein co-chaperones that recruit the molecular chaperone DnaK to assist protein substrates involved in survival, adaptation, or fitness. The atc operon of the aquatic mesophilic bacterium Shewanella oneidensis encodes the proteins AtcJ, AtcA, AtcB, and AtcC, and all of them, except AtcA, are required for growth at low temperatures. AtcJ is a short J-domain protein that interacts with DnaK, but also with AtcC through its 21 amino acid C-terminal domain. This interaction network is critical for cold growth. Here, we show that AtcJ represents a subfamily of short J-domain proteins that (i) are found in several environmental, mostly aquatic, β- or ɣ-proteobacteria and (ii) contain a conserved PX
    MeSH term(s) Proteobacteria/metabolism ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Arginine ; Cold Temperature ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Escherichia coli Proteins/genetics
    Chemical Substances arginine thiazolidinecarboxylate (57631-15-9) ; Molecular Chaperones ; Arginine (94ZLA3W45F) ; Bacterial Proteins ; Escherichia coli Proteins
    Language English
    Publishing date 2023-08-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020213-1
    ISSN 1462-2920 ; 1462-2912
    ISSN (online) 1462-2920
    ISSN 1462-2912
    DOI 10.1111/1462-2920.16478
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Defining the sequence requirements for the positioning of base J in DNA using SMRT sequencing.

    Genest, Paul-Andre / Baugh, Loren / Taipale, Alex / Zhao, Wanqi / Jan, Sabrina / van Luenen, Henri G A M / Korlach, Jonas / Clark, Tyson / Luong, Khai / Boitano, Matthew / Turner, Steve / Myler, Peter J / Borst, Piet

    Nucleic acids research

    2015  Volume 43, Issue 4, Page(s) 2102–2115

    Abstract: Base J (β-D-glucosyl-hydroxymethyluracil) replaces 1% of T in the Leishmania genome and is only ... the initial step in J synthesis. To determine the DNA sequences recognized by JBP1/2, we used SMRT sequencing ... recognizes base J in DNA. Leishmania DNA segments that normally contain J also picked up J when present ...

    Abstract Base J (β-D-glucosyl-hydroxymethyluracil) replaces 1% of T in the Leishmania genome and is only found in telomeric repeats (99%) and in regions where transcription starts and stops. This highly restricted distribution must be co-determined by the thymidine hydroxylases (JBP1 and JBP2) that catalyze the initial step in J synthesis. To determine the DNA sequences recognized by JBP1/2, we used SMRT sequencing of DNA segments inserted into plasmids grown in Leishmania tarentolae. We show that SMRT sequencing recognizes base J in DNA. Leishmania DNA segments that normally contain J also picked up J when present in the plasmid, whereas control sequences did not. Even a segment of only 10 telomeric (GGGTTA) repeats was modified in the plasmid. We show that J modification usually occurs at pairs of Ts on opposite DNA strands, separated by 12 nucleotides. Modifications occur near G-rich sequences capable of forming G-quadruplexes and JBP2 is needed, as it does not occur in JBP2-null cells. We propose a model whereby de novo J insertion is mediated by JBP2. JBP1 then binds to J and hydroxylates another T 13 bp downstream (but not upstream) on the complementary strand, allowing JBP1 to maintain existing J following DNA replication.
    MeSH term(s) DNA-Binding Proteins/metabolism ; Glucosides/analysis ; Glucosides/metabolism ; Leishmania/genetics ; Plasmids/genetics ; Protozoan Proteins/metabolism ; Sequence Analysis, DNA ; Uracil/analogs & derivatives ; Uracil/analysis ; Uracil/metabolism
    Chemical Substances DNA-Binding Proteins ; Glucosides ; J-specific DNA-binding protein, protozoa ; Protozoan Proteins ; 5-((glucopyranosyloxy)methyl)uracil (53910-96-6) ; Uracil (56HH86ZVCT)
    Language English
    Publishing date 2015-02-27
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkv095
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1067: Show issues Location:
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  4. Article ; Online: Glucosylated hydroxymethyluracil, DNA base J, prevents transcriptional readthrough in Leishmania.

    van Luenen, Henri G A M / Farris, Carol / Jan, Sabrina / Genest, Paul-Andre / Tripathi, Pankaj / Velds, Arno / Kerkhoven, Ron M / Nieuwland, Marja / Haydock, Andrew / Ramasamy, Gowthaman / Vainio, Saara / Heidebrecht, Tatjana / Perrakis, Anastassis / Pagie, Ludo / van Steensel, Bas / Myler, Peter J / Borst, Piet

    Cell

    2012  Volume 150, Issue 5, Page(s) 909–921

    Abstract: ... base J (β-D-glucosyl-hydroxymethyluracil). In Leishmania, about 99% of J is located in telomeric ... repeats. We show here that most of the remaining J is located at chromosome-internal RNA polymerase II ... termination sites. This internal J and telomeric J can be reduced by a knockout of J-binding protein 2 (JBP2 ...

    Abstract Some Ts in nuclear DNA of trypanosomes and Leishmania are hydroxylated and glucosylated to yield base J (β-D-glucosyl-hydroxymethyluracil). In Leishmania, about 99% of J is located in telomeric repeats. We show here that most of the remaining J is located at chromosome-internal RNA polymerase II termination sites. This internal J and telomeric J can be reduced by a knockout of J-binding protein 2 (JBP2), an enzyme involved in the first step of J biosynthesis. J levels are further reduced by growing Leishmania JBP2 knockout cells in BrdU-containing medium, resulting in cell death. The loss of internal J in JBP2 knockout cells is accompanied by massive readthrough at RNA polymerase II termination sites. The readthrough varies between transcription units but may extend over 100 kb. We conclude that J is required for proper transcription termination and infer that the absence of internal J kills Leishmania by massive readthrough of transcriptional stops.
    MeSH term(s) Gene Knockout Techniques ; Glucosides/metabolism ; Leishmania/genetics ; Leishmania/metabolism ; RNA Polymerase II/metabolism ; RNA, Double-Stranded/metabolism ; Transcription, Genetic ; Uracil/analogs & derivatives ; Uracil/metabolism
    Chemical Substances Glucosides ; RNA, Double-Stranded ; 5-((glucopyranosyloxy)methyl)uracil (53910-96-6) ; Uracil (56HH86ZVCT) ; RNA Polymerase II (EC 2.7.7.-)
    Language English
    Publishing date 2012-08-09
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2012.07.030
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 58: Show issues

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  5. Article ; Online: Search for Higgs and Z Boson Decays to J/ψγ and ϒ(nS)γ with the ATLAS Detector.

    Aad, G / Abbott, B / Abdallah, J / Abdel Khalek, S / Abdinov, O / Aben, R / Abi, B / Abolins, M / AbouZeid, O S / Abramowicz, H / Abreu, H / Abreu, R / Abulaiti, Y / Acharya, B S / Adamczyk, L / Adams, D L / Adelman, J / Adomeit, S / Adye, T /
    Agatonovic-Jovin, T / Aguilar-Saavedra, J A / Agustoni, M / Ahlen, S P / Ahmadov, F / Aielli, G / Akerstedt, H / Åkesson, T P A / Akimoto, G / Akimov, A V / Alberghi, G L / Albert, J / Albrand, S / Alconada Verzini, M J / Aleksa, M / Aleksandrov, I N / Alexa, C / Alexander, G / Alexandre, G / Alexopoulos, T / Alhroob, M / Alimonti, G / Alio, L / Alison, J / Allbrooke, B M M / Allison, L J / Allport, P P / Aloisio, A / Alonso, A / Alonso, F / Alpigiani, C / Altheimer, A / Alvarez Gonzalez, B / Alviggi, M G / Amako, K / Amaral Coutinho, Y / Amelung, C / Amidei, D / Amor Dos Santos, S P / Amorim, A / Amoroso, S / Amram, N / Amundsen, G / Anastopoulos, C / Ancu, L S / Andari, N / Andeen, T / Anders, C F / Anders, G / Anderson, K J / Andreazza, A / Andrei, V / Anduaga, X S / Angelidakis, S / Angelozzi, I / Anger, P / Angerami, A / Anghinolfi, F / Anisenkov, A V / Anjos, N / Annovi, A / Antonelli, M / Antonov, A / Antos, J / Anulli, F / Aoki, M / Aperio Bella, L / Arabidze, G / Arai, Y / Araque, J P / Arce, A T H / Arduh, F A / Arguin, J-F / Argyropoulos, S / Arik, M / Armbruster, A J / Arnaez, O / Arnal, V / Arnold, H / Arratia, M / Arslan, O / Artamonov, A / Artoni, G / Asai, S / Asbah, N / Ashkenazi, A / Åsman, B / Asquith, L / Assamagan, K / Astalos, R / Atkinson, M / Atlay, N B / Auerbach, B / Augsten, K / Aurousseau, M / Avolio, G / Axen, B / Ayoub, M K / Azuelos, G / Baak, M A / Baas, A E / Bacci, C / Bachacou, H / Bachas, K / Backes, M / Backhaus, M / Bagiacchi, P / Bagnaia, P / Bai, Y / Bain, T / Baines, J T / Baker, O K / Balek, P / Balestri, T / Balli, F / Banas, E / Banerjee, Sw / Bannoura, A A E / Bansil, H S / Barak, L / Baranov, S P / Barberio, E L / Barberis, D / Barbero, M / Barillari, T / Barisonzi, M / Barklow, T / Barlow, N / Barnes, S L / Barnett, B M / Barnett, R M / Barnovska, Z / Baroncelli, A / Barone, G / Barr, A J / Barreiro, F / Barreiro Guimarães da Costa, J / Bartoldus, R / Barton, A E / Bartos, P / Bassalat, A / Basye, A / Bates, R L / Batista, S J / Batley, J R / Battaglia, M / Bauce, M / Bauer, F / Bawa, H S / Beacham, J B / Beattie, M D / Beau, T / Beauchemin, P H / Beccherle, R / Bechtle, P / Beck, H P / Becker, K / Becker, S / Beckingham, M / Becot, C / Beddall, A J / Beddall, A / Bednyakov, V A / Bee, C P / Beemster, L J / Beermann, T A / Begel, M / Behr, K / Belanger-Champagne, C / Bell, P J / Bell, W H / Bella, G / Bellagamba, L / Bellerive, A / Bellomo, M / Belotskiy, K / Beltramello, O / Benary, O / Benchekroun, D / Bender, M / Bendtz, K / Benekos, N / Benhammou, Y / Benhar Noccioli, E / Benitez Garcia, J A / Benjamin, D P / Bensinger, J R / Bentvelsen, S / Beresford, L / Beretta, M / Berge, D / Bergeaas Kuutmann, E / Berger, N / Berghaus, F / Beringer, J / Bernard, C / Bernard, N R / Bernius, C / Bernlochner, F U / Berry, T / Berta, P / Bertella, C / Bertoli, G / Bertolucci, F / Bertsche, C / Bertsche, D / Besana, M I / Besjes, G J / Bessidskaia Bylund, O / Bessner, M / Besson, N / Betancourt, C / Bethke, S / Bevan, A J / Bhimji, W / Bianchi, R M / Bianchini, L / Bianco, M / Biebel, O / Bieniek, S P / Biglietti, M / Bilbao De Mendizabal, J / Bilokon, H / Bindi, M / Binet, S / Bingul, A / Bini, C / Black, C W / Black, J E / Black, K M / Blackburn, D / Blair, R E / Blanchard, J-B / Blanco, J E / Blazek, T / Bloch, I / Blocker, C / Blum, W / Blumenschein, U / Bobbink, G J / Bobrovnikov, V S / Bocchetta, S S / Bocci, A / Bock, C / Boddy, C R / Boehler, M / Bogaerts, J A / Bogdanchikov, A G / Bohm, C / Boisvert, V / Bold, T / Boldea, V / Boldyrev, A S / Bomben, M / Bona, M / Boonekamp, M / Borisov, A / Borissov, G / Borroni, S / Bortfeldt, J / Bortolotto, V / Bos, K / Boscherini, D / Bosman, M / Boudreau, J / Bouffard, J / Bouhova-Thacker, E V / Boumediene, D / Bourdarios, C / Bousson, N / Boutouil, S / Boveia, A / Boyd, J / Boyko, I R / Bozic, I / Bracinik, J / Brandt, A / Brandt, G / Brandt, O / Bratzler, U / Brau, B / Brau, J E / Braun, H M / Brazzale, S F / Brendlinger, K / Brennan, A J / Brenner, L / Brenner, R / Bressler, S / Bristow, K / Bristow, T M / Britton, D / Brochu, F M / Brock, I / Brock, R / Bronner, J / Brooijmans, G / Brooks, T / Brooks, W K / Brosamer, J / Brost, E / Brown, J / Bruckman de Renstrom, P A / Bruncko, D / Bruneliere, R / Bruni, A / Bruni, G / Bruschi, M / Bryngemark, L / Buanes, T / Buat, Q / Bucci, F / Buchholz, P / Buckley, A G / Buda, S I / Budagov, I A / Buehrer, F / Bugge, L / Bugge, M K / Bulekov, O / Burckhart, H / Burdin, S / Burghgrave, B / Burke, S / Burmeister, I / Busato, E / Büscher, D / Büscher, V / Bussey, P / Buszello, C P / Butler, J M / Butt, A I / Buttar, C M / Butterworth, J M / Butti, P / Buttinger, W / Buzatu, A / Cabrera Urbán, S / Caforio, D / Cakir, O / Calafiura, P / Calandri, A / Calderini, G / Calfayan, P / Caloba, L P / Calvet, D / Calvet, S / Camacho Toro, R / Camarda, S / Cameron, D / Caminada, L M / Caminal Armadans, R / Campana, S / Campanelli, M / Campoverde, A / Canale, V / Canepa, A / Cano Bret, M / Cantero, J / Cantrill, R / Cao, T / Capeans Garrido, M D M / Caprini, I / Caprini, M / Capua, M / Caputo, R / Cardarelli, R / Carli, T / Carlino, G / Carminati, L / Caron, S / Carquin, E / Carrillo-Montoya, G D / Carter, J R / Carvalho, J / Casadei, D / Casado, M P / Casolino, M / Castaneda-Miranda, E / Castelli, A / Castillo Gimenez, V / Castro, N F / Catastini, P / Catinaccio, A / Catmore, J R / Cattai, A / Cattani, G / Caudron, J / Cavaliere, V / Cavalli, D / Cavalli-Sforza, M / Cavasinni, V / Ceradini, F / Cerio, B C / Cerny, K / Cerqueira, A S / Cerri, A / Cerrito, L / Cerutti, F / Cerv, M / Cervelli, A / Cetin, S A / Chafaq, A / Chakraborty, D / Chalupkova, I / Chang, P / Chapleau, B / Chapman, J D / Charfeddine, D / Charlton, D G / Chau, C C / Chavez Barajas, C A / Cheatham, S / Chegwidden, A / Chekanov, S / Chekulaev, S V / Chelkov, G A / Chelstowska, M A / Chen, C / Chen, H / Chen, K / Chen, L / Chen, S / Chen, X / Chen, Y / Cheng, H C / Cheng, Y / Cheplakov, A / Cheremushkina, E / Cherkaoui El Moursli, R / Chernyatin, V / Cheu, E / Chevalier, L / Chiarella, V / Childers, J T / Chilingarov, A / Chiodini, G / Chisholm, A S / Chislett, R T / Chitan, A / Chizhov, M V / Chouridou, S / Chow, B K B / Chromek-Burckhart, D / Chu, M L / Chudoba, J / Chwastowski, J J / Chytka, L / Ciapetti, G / Ciftci, A K / Cinca, D / Cindro, V / Ciocio, A / Citron, Z H / Citterio, M / Ciubancan, M / Clark, A / Clark, P J / Clarke, R N / Cleland, W / Clement, C / Coadou, Y / Cobal, M / Coccaro, A / Cochran, J / Coffey, L / Cogan, J G / Cole, B / Cole, S / Colijn, A P / Collot, J / Colombo, T / Compostella, G / Conde Muiño, P / Coniavitis, E / Connell, S H / Connelly, I A / Consonni, S M / Consorti, V / Constantinescu, S / Conta, C / Conti, G / Conventi, F / Cooke, M / Cooper, B D / Cooper-Sarkar, A M / Copic, K / Cornelissen, T / Corradi, M / Corriveau, F / Corso-Radu, A / Cortes-Gonzalez, A / Cortiana, G / Costa, M J / Costanzo, D / Côté, D / Cottin, G / Cowan, G / Cox, B E / Cranmer, K / Cree, G / Crépé-Renaudin, S / Crescioli, F / Cribbs, W A / Crispin Ortuzar, M / Cristinziani, M / Croft, V / Crosetti, G / Cuhadar Donszelmann, T / Cummings, J / Curatolo, M / Cuthbert, C / Czirr, H / Czodrowski, P / D'Auria, S / D'Onofrio, M / Da Cunha Sargedas De Sousa, M J / Da Via, C / Dabrowski, W / Dafinca, A / Dai, T / Dale, O / Dallaire, F / Dallapiccola, C / Dam, M / Dandoy, J R / Daniells, A C / Danninger, M / Dano Hoffmann, M / Dao, V / Darbo, G / Darmora, S / Dassoulas, J / Dattagupta, A / Davey, W / David, C / Davidek, T / Davies, E / Davies, M / Davignon, O / Davison, P / Davygora, Y / Dawe, E / Dawson, I / Daya-Ishmukhametova, R K / De, K / de Asmundis, R / De Castro, S / De Cecco, S / De Groot, N / de Jong, P / De la Torre, H / De Lorenzi, F / De Nooij, L / De Pedis, D / De Salvo, A / De Sanctis, U / De Santo, A / De Vivie De Regie, J B / Dearnaley, W J / Debbe, R / Debenedetti, C / Dedovich, D V / Deigaard, I / Del Peso, J / Del Prete, T / Delgove, D / Deliot, F / Delitzsch, C M / Deliyergiyev, M / Dell'Acqua, A / Dell'Asta, L / Dell'Orso, M / Della Pietra, M / Della Volpe, D / Delmastro, M / Delsart, P A / Deluca, C / DeMarco, D A / Demers, S / Demichev, M / Demilly, A / Denisov, S P / Derendarz, D / Derkaoui, J E / Derue, F / Dervan, P / Desch, K / Deterre, C / Deviveiros, P O / Dewhurst, A / Dhaliwal, S / Di Ciaccio, A / Di Ciaccio, L / Di Domenico, A / Di Donato, C / Di Girolamo, A / Di Girolamo, B / Di Mattia, A / Di Micco, B / Di Nardo, R / Di Simone, A / Di Sipio, R / Di Valentino, D / Diaconu, C / Diamond, M / Dias, F A / Diaz, M A / Diehl, E B / Dietrich, J / Dietzsch, T A / Diglio, S / Dimitrievska, A / Dingfelder, J / Dittus, F / Djama, F / Djobava, T / Djuvsland, J I / do Vale, M A B / Dobos, D / Dobre, M / Doglioni, C / Doherty, T / Dohmae, T / Dolejsi, J / Dolezal, Z / Dolgoshein, B A / Donadelli, M / Donati, S / Dondero, P / Donini, J / Dopke, J / Doria, A / Dova, M T / Doyle, A T / Dris, M / Dubreuil, E / Duchovni, E / Duckeck, G / Ducu, O A / Duda, D / Dudarev, A / Duflot, L / Duguid, L / Dührssen, M / Dunford, M / Duran Yildiz, H / Düren, M / Durglishvili, A / Duschinger, D / Dwuznik, M / Dyndal, M / Edson, W / Edwards, N C / Ehrenfeld, W / Eifert, T / Eigen, G / Einsweiler, K / Ekelof, T / El Kacimi, M / Ellert, M / Elles, S / Ellinghaus, F / Elliot, A A / Ellis, N / Elmsheuser, J / Elsing, M / Emeliyanov, D / Enari, Y / Endner, O C / Endo, M / Engelmann, R / Erdmann, J / Ereditato, A / Eriksson, D / Ernis, G / Ernst, J / Ernst, M / Errede, S / Ertel, E / Escalier, M / Esch, H / Escobar, C / Esposito, B / Etienvre, A I / Etzion, E / Evans, H / Ezhilov, A / Fabbri, L / Facini, G / Fakhrutdinov, R M / Falciano, S / Falla, R J / Faltova, J / Fang, Y / Fanti, M / Farbin, A / Farilla, A / Farooque, T / Farrell, S / Farrington, S M / Farthouat, P / Fassi, F / Fassnacht, P / Fassouliotis, D / Favareto, A / Fayard, L / Federic, P / Fedin, O L / Fedorko, W / Feigl, S / Feligioni, L / Feng, C 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R M / Nevski, P / Newman, P R / Nguyen, D H / Nickerson, R B / Nicolaidou, R / Nicquevert, B / Nielsen, J / Nikiforou, N / Nikiforov, A / Nikolaenko, V / Nikolic-Audit, I / Nikolopoulos, K / Nilsson, P / Ninomiya, Y / Nisati, A / Nisius, R / Nobe, T / Nomachi, M / Nomidis, I / Nooney, T / Norberg, S / Nordberg, M / Novgorodova, O / Nowak, S / Nozaki, M / Nozka, L / Ntekas, K / Nunes Hanninger, G / Nunnemann, T / Nurse, E / Nuti, F / O'Brien, B J / O'grady, F / O'Neil, D C / O'Shea, V / Oakham, F G / Oberlack, H / Obermann, T / Ocariz, J / Ochi, A / Ochoa, I / Oda, S / Odaka, S / Ogren, H / Oh, A / Oh, S H / Ohm, C C / Ohman, H / Oide, H / Okamura, W / Okawa, H / Okumura, Y / Okuyama, T / Olariu, A / Olchevski, A G / Olivares Pino, S A / Oliveira Damazio, D / Oliver Garcia, E / Olszewski, A / Olszowska, J / Onofre, A / Onyisi, P U E / Oram, C J / Oreglia, M J / Oren, Y / Orestano, D / Orlando, N / Oropeza Barrera, C / Orr, R S / Osculati, B / Ospanov, R / Otero Y Garzon, G / Otono, H / 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Zaitsev, A M / Zaman, A / Zambito, S / Zanello, L / Zanzi, D / Zeitnitz, C / Zeman, M / Zemla, A / Zengel, K / Zenin, O / Ženiš, T / Zerwas, D / Zhang, D / Zhang, F / Zhang, J / Zhang, L / Zhang, R / Zhang, X / Zhang, Z / Zhao, X / Zhao, Y / Zhao, Z / Zhemchugov, A / Zhong, J / Zhou, B / Zhou, C / Zhou, L / Zhou, N / Zhu, C G / Zhu, H / Zhu, J / Zhu, Y / Zhuang, X / Zhukov, K / Zibell, A / Zieminska, D / Zimine, N I / Zimmermann, C / Zimmermann, R / Zimmermann, S / Zinonos, Z / Ziolkowski, M / Živković, L / Zobernig, G / Zoccoli, A / Zur Nedden, M / Zurzolo, G / Zwalinski, L

    Physical review letters

    2015  Volume 114, Issue 12, Page(s) 121801

    Abstract: A search for the decays of the Higgs and Z bosons to J/ψγ and ϒ(nS)γ (n=1,2,3) is performed with pp ... In the J/ψγ final state the limits are 1.5×10^{-3} and 2.6×10^{-6} for the Higgs and Z boson decays ...

    Abstract A search for the decays of the Higgs and Z bosons to J/ψγ and ϒ(nS)γ (n=1,2,3) is performed with pp collision data samples corresponding to integrated luminosities of up to 20.3  fb^{-1} collected at sqrt[s]=8  TeV with the ATLAS detector at the CERN Large Hadron Collider. No significant excess of events is observed above expected backgrounds and 95% C.L. upper limits are placed on the branching fractions. In the J/ψγ final state the limits are 1.5×10^{-3} and 2.6×10^{-6} for the Higgs and Z boson decays, respectively, while in the ϒ(1S,2S,3S)γ final states the limits are (1.3,1.9,1.3)×10^{-3} and (3.4,6.5,5.4)×10^{-6}, respectively.
    Language English
    Publishing date 2015-03-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 208853-8
    ISSN 1079-7114 ; 0031-9007
    ISSN (online) 1079-7114
    ISSN 0031-9007
    DOI 10.1103/PhysRevLett.114.121801
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  6. Article ; Online: Cold adaptation in the environmental bacterium Shewanella oneidensis is controlled by a J-domain co-chaperone protein network

    Nathanael Jean Maillot / Flora Ambre Honoré / Deborah Byrne / Vincent Méjean / Olivier Genest

    Communications Biology, Vol 2, Iss 1, Pp 1-

    2019  Volume 10

    Abstract: ... a previously uncharacterized J‐ domain protein, AtcJ and that its interaction with the target protein AtcC is ...

    Abstract Maillot et al. demonstrate that the environmental bacterium Shewanella oneidensis possesses a previously uncharacterized J‐ domain protein, AtcJ and that its interaction with the target protein AtcC is important for this bacterial adaptation to the cold. This study identifies a protein network that allows bacteria to survive cold stress.
    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2019-08-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase.

    Yu, Zhong / Genest, Paul-André / ter Riet, Bas / Sweeney, Kate / DiPaolo, Courtney / Kieft, Rudo / Christodoulou, Evangelos / Perrakis, Anastassis / Simmons, Jana M / Hausinger, Robert P / van Luenen, Henri G A M / Rigden, Daniel J / Sabatini, Robert / Borst, Piet

    Nucleic acids research

    2007  Volume 35, Issue 7, Page(s) 2107–2115

    Abstract: Trypanosomatids contain an unusual DNA base J (beta-d-glucosylhydroxymethyluracil), which replaces ... a fraction of thymine in telomeric and other DNA repeats. To determine the function of base J, we have ... searched for enzymes that catalyze J biosynthesis. We present evidence that a protein that binds to J ...

    Abstract Trypanosomatids contain an unusual DNA base J (beta-d-glucosylhydroxymethyluracil), which replaces a fraction of thymine in telomeric and other DNA repeats. To determine the function of base J, we have searched for enzymes that catalyze J biosynthesis. We present evidence that a protein that binds to J in DNA, the J-binding protein 1 (JBP1), may also catalyze the first step in J biosynthesis, the conversion of thymine in DNA into hydroxymethyluracil. We show that JBP1 belongs to the family of Fe(2+) and 2-oxoglutarate-dependent dioxygenases and that replacement of conserved residues putatively involved in Fe(2+) and 2-oxoglutarate-binding inactivates the ability of JBP1 to contribute to J synthesis without affecting its ability to bind to J-DNA. We propose that JBP1 is a thymidine hydroxylase responsible for the local amplification of J inserted by JBP2, another putative thymidine hydroxylase.
    MeSH term(s) Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding Sites ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/classification ; DNA-Binding Proteins/metabolism ; Dioxygenases/classification ; Glucosides/biosynthesis ; Glucosides/chemistry ; Glucosides/metabolism ; Leishmania/genetics ; Mixed Function Oxygenases/chemistry ; Mixed Function Oxygenases/classification ; Mixed Function Oxygenases/metabolism ; Molecular Sequence Data ; Protein Structure, Tertiary ; Protozoan Proteins/chemistry ; Protozoan Proteins/classification ; Protozoan Proteins/metabolism ; Uracil/analogs & derivatives ; Uracil/biosynthesis ; Uracil/chemistry ; Uracil/metabolism
    Chemical Substances DNA-Binding Proteins ; Glucosides ; J-specific DNA-binding protein, protozoa ; Protozoan Proteins ; 5-((glucopyranosyloxy)methyl)uracil (53910-96-6) ; Uracil (56HH86ZVCT) ; Mixed Function Oxygenases (EC 1.-) ; Dioxygenases (EC 1.13.11.-) ; thymidine,2-oxoglutarate dioxygenase (EC 1.14.11.3)
    Language English
    Publishing date 2007
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205588-5
    ISSN 1362-4962 ; 1746-8272 ; 0305-1048 ; 0261-3166
    ISSN (online) 1362-4962 ; 1746-8272
    ISSN 0305-1048 ; 0261-3166
    DOI 10.1093/nar/gkm049
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  8. Article: Evidence that J-binding protein 2 is a thymidine hydroxylase catalyzing the first step in the biosynthesis of DNA base J.

    Vainio, Saara / Genest, Paul-André / ter Riet, Bas / van Luenen, Henri / Borst, Piet

    Molecular and biochemical parasitology

    2009  Volume 164, Issue 2, Page(s) 157–161

    Abstract: ... hydroxymethyluracil or base J. We recently reported that two proteins, called J-binding protein (JBP) 1 and 2 ... which regulate the levels of J in the genome, display features of the family of Fe(II)-2-oxoglutarate dependent ... dioxygenases and are likely to be the enzymes catalyzing the first step in J biosynthesis. In this study ...

    Abstract The genomic DNA of kinetoplastid parasites contains a unique modified base, beta-d-glucosyl-hydroxymethyluracil or base J. We recently reported that two proteins, called J-binding protein (JBP) 1 and 2, which regulate the levels of J in the genome, display features of the family of Fe(II)-2-oxoglutarate dependent dioxygenases and are likely to be the enzymes catalyzing the first step in J biosynthesis. In this study, we examine the effects of replacing the four conserved residues critical for the activity of this class of enzymes on the function of Leishmania tarentolae JBP2. The results show that each of these four residues is indispensable for the ability of JBP2 to stimulate J synthesis, while mutating non-conserved residues has no consequences. We conclude that JBP2, like JBP1, is in all probability a thymidine hydroxylase involved in the biosynthesis of base J.
    MeSH term(s) Amino Acid Substitution/genetics ; Animals ; DNA, Protozoan/chemistry ; DNA, Protozoan/genetics ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Glucosides/biosynthesis ; Leishmania/enzymology ; Leishmania/genetics ; Mixed Function Oxygenases/genetics ; Mixed Function Oxygenases/metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Sequence Analysis, DNA ; Thymidine/metabolism ; Uracil/analogs & derivatives ; Uracil/biosynthesis
    Chemical Substances DNA, Protozoan ; DNA-Binding Proteins ; Glucosides ; J-specific DNA-binding protein, protozoa ; Protozoan Proteins ; 5-((glucopyranosyloxy)methyl)uracil (53910-96-6) ; Uracil (56HH86ZVCT) ; Mixed Function Oxygenases (EC 1.-) ; Thymidine (VC2W18DGKR)
    Language English
    Publishing date 2009-04
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 756166-0
    ISSN 1872-9428 ; 0166-6851
    ISSN (online) 1872-9428
    ISSN 0166-6851
    DOI 10.1016/j.molbiopara.2008.12.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Transient very low LDL-C levels: a legacy effect for cardiovascular prevention?

    Genest, Jacques

    European heart journal

    2023  Volume 44, Issue 16, Page(s) 1418–1420

    MeSH term(s) Humans ; Hydroxymethylglutaryl-CoA Reductase Inhibitors ; Cholesterol, LDL ; Cardiovascular Diseases/prevention & control ; Acute Coronary Syndrome ; Risk Factors ; Heart Disease Risk Factors
    Chemical Substances Hydroxymethylglutaryl-CoA Reductase Inhibitors ; Cholesterol, LDL ; alirocumab (PP0SHH6V16)
    Language English
    Publishing date 2023-03-07
    Publishing country England
    Document type Editorial ; Comment
    ZDB-ID 603098-1
    ISSN 1522-9645 ; 0195-668X
    ISSN (online) 1522-9645
    ISSN 0195-668X
    DOI 10.1093/eurheartj/ehad155
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    Zs.MO 640: Show issues

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  10. Article ; Online: Telomeric localization of the modified DNA base J in the genome of the protozoan parasite Leishmania.

    Genest, Paul-André / Ter Riet, Bas / Cijsouw, Tony / van Luenen, Henri G A M / Borst, Piet

    Nucleic acids research

    2007  Volume 35, Issue 7, Page(s) 2116–2124

    Abstract: Base J or beta-d-glucosylhydroxymethyluracil is a DNA modification replacing a fraction of thymine ... in the nuclear DNA of kinetoplastid parasites and of Euglena. J is located in the telomeric sequences ... of Trypanosoma brucei and in other simple repeat DNA sequences. In addition, J was found in the inactive variant ...

    Abstract Base J or beta-d-glucosylhydroxymethyluracil is a DNA modification replacing a fraction of thymine in the nuclear DNA of kinetoplastid parasites and of Euglena. J is located in the telomeric sequences of Trypanosoma brucei and in other simple repeat DNA sequences. In addition, J was found in the inactive variant surface glycoprotein (VSG) expression sites, but not in the active expression site of T. brucei, suggesting that J could play a role in transcription silencing in T. brucei. We have now looked at the distribution of J in the genomes of other kinetoplastid parasites. First, we analyzed the DNA sequences immunoprecipitated with a J-antiserum in Leishmania major Friedlin. Second, we investigated the co-migration of J- and telomeric repeat-containing DNA sequences of various kinetoplastids using J-immunoblots and Southern blots of fragmented DNA. We find only approximately 1% of J outside the telomeric repeat sequences of Leishmania sp. and Crithidia fasciculata, in contrast to the substantial fraction of non-telomeric J found in T. brucei, Trypanosoma equiperdum and Trypanoplasma borreli. Our results suggest that J is a telomeric base modification, recruited for other (unknown) functions in some kinetoplastids and Euglena.
    MeSH term(s) Animals ; Chromatography, Agarose ; Crithidia fasciculata/genetics ; DNA, Protozoan/chemistry ; Genome, Protozoan ; Glucosides/analysis ; Immunoblotting ; Immunoprecipitation ; Leishmania/genetics ; Repetitive Sequences, Nucleic Acid ; Sequence Analysis, DNA ; Telomere/chemistry ; Trypanosoma cruzi/genetics ; Uracil/analogs & derivatives ; Uracil/analysis
    Chemical Substances DNA, Protozoan ; Glucosides ; 5-((glucopyranosyloxy)methyl)uracil (53910-96-6) ; Uracil (56HH86ZVCT)
    Language English
    Publishing date 2007
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205588-5
    ISSN 1362-4962 ; 1746-8272 ; 0305-1048 ; 0261-3166
    ISSN (online) 1362-4962 ; 1746-8272
    ISSN 0305-1048 ; 0261-3166
    DOI 10.1093/nar/gkm050
    Database MEDical Literature Analysis and Retrieval System OnLINE

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