Zobrazeno 1 - 10
of 657
pro vyhledávání: '"Tainer, JA"'
Autor:
WILSON, David, Deacon, AM, Duncton, MAJ, Pellicena, P, Georgiadis, MM, Yeh, AP, Arvai, AS, Moiani, D, Tainer, JA, Das , D
Cancer will directly affect the lives of over one-third of the population. The DNA Damage Response (DDR) is an intricate system involving damage recognition, cell cycle regulation, DNA repair, and ultimately cell fate determination, playing a central
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______105::7068aabd1648daba90c75c8e39e205e6
http://hdl.handle.net/1942/35805
http://hdl.handle.net/1942/35805
Autor:
Tsutakawa, SE, Thompson, MJ, Arvai, AS, Neil, AJ, Shaw, SJ, Algasaier, SI, Kim, JC, Finger, D, Jardine, E, Gotham, VJB, Sarker, AH, Her, MZ, Rashid, F, Hamdan, SM, Mirkin, SM, Grasby, JA, Tainer, JA
Publikováno v:
Tsutakawa, SE; Thompson, MJ; Arvai, AS; Neil, AJ; Shaw, SJ; Algasaier, SI; et al.(2017). Phosphate steering by Flap Endonuclease 1 promotes 5 '-flap specificity and incision to prevent genome instability (vol 8, 15855, 2017). NATURE COMMUNICATIONS, 8. doi: 10.1038/ncomms16145. Lawrence Berkeley National Laboratory: Retrieved from: http://www.escholarship.org/uc/item/447808sk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::8e139ef5e2e6b52bb78d83a6a3d462bb
http://www.escholarship.org/uc/item/447808sk
http://www.escholarship.org/uc/item/447808sk
Publikováno v:
Journal of the American Society for Mass Spectrometry, vol 28, iss 2
Susa, AC; Xia, Z; Tang, HYH; Tainer, JA; & Williams, ER. (2017). Charging of Proteins in Native Mass Spectrometry. Journal of the American Society for Mass Spectrometry, 28(2), 332-340. doi: 10.1007/s13361-016-1517-7. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/7r66h9m4
Susa, AC; Xia, Z; Tang, HYH; Tainer, JA; & Williams, ER. (2017). Charging of Proteins in Native Mass Spectrometry. Journal of the American Society for Mass Spectrometry, 28(2), 332-340. doi: 10.1007/s13361-016-1517-7. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/7r66h9m4
© 2016, American Society for Mass Spectrometry. Factors that influence the charging of protein ions formed by electrospray ionization from aqueous solutions in which proteins have native structures and function were investigated. Protein ions rangin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::047d686cec7e7cf1f9ea8330fd64a1b4
https://escholarship.org/uc/item/7r66h9m4
https://escholarship.org/uc/item/7r66h9m4
Autor:
Daniel Aceytuno, R, Piett, CG, Havali-Shahriari, Z, Edwards, RA, Rey, M, Ye, R, Javed, F, Fang, S, Mani, R, Weinfeld, M, Hammel, M, Tainer, JA, Schriemer, DC, Lees-Miller, SP, Mark Glover, JN
Publikováno v:
Daniel Aceytuno, R; Piett, CG; Havali-Shahriari, Z; Edwards, RA; Rey, M; Ye, R; et al.(2017). Structural and functional characterization of the PNKP-XRCC4-LigIV DNA repair complex. Nucleic Acids Research, 45(10), 6238-6251. doi: 10.1093/nar/gkx275. Lawrence Berkeley National Laboratory: Lawrence Berkeley National Laboratory. Retrieved from: http://www.escholarship.org/uc/item/8vv1h2hs
© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. Non-homologous end joining (NHEJ) repairs DNA double strand breaks in non-cycling eukaryotic cells. NHEJ relies on polynucleotide kinase/phosphatase (PNK
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______325::11460a66b20de394958b302d981018ab
http://www.escholarship.org/uc/item/8vv1h2hs
http://www.escholarship.org/uc/item/8vv1h2hs
Autor:
Brunette, TJ, Parmeggiani, F, Huang, PS, Bhabha, G, Ekiert, DC, Tsutakawa, SE, Hura, GL, Tainer, JA, Baker, D
Publikováno v:
Nature, vol 528, iss 7583
Brunette, TJ; Parmeggiani, F; Huang, PS; Bhabha, G; Ekiert, DC; Tsutakawa, SE; et al.(2015). Exploring the repeat protein universe through computational protein design. Nature, 528(7583), 580-584. doi: 10.1038/nature16162. Lawrence Berkeley National Laboratory: Lawrence Berkeley National Laboratory. Retrieved from: http://www.escholarship.org/uc/item/1pb2b52f
Brunette, TJ; Parmeggiani, F; Huang, PS; Bhabha, G; Ekiert, DC; Tsutakawa, SE; et al.(2015). Exploring the repeat protein universe through computational protein design. Nature, 528(7583), 580-584. doi: 10.1038/nature16162. Lawrence Berkeley National Laboratory: Lawrence Berkeley National Laboratory. Retrieved from: http://www.escholarship.org/uc/item/1pb2b52f
© 2015 Macmillan Publishers Limited. All rights reserved. A central question in protein evolution is the extent to which naturally occurring proteins sample the space of folded structures accessible to the polypeptide chain. Repeat proteins composed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::bae418dc5b9ea176a6fbfc91abe3347f
https://escholarship.org/uc/item/1pb2b52f
https://escholarship.org/uc/item/1pb2b52f
Autor:
Shibata, A, Moiani, D (Davide), Arvai, AS, Perry, J, Harding, SM, Genois, MM, Maity, R, Van Rossum - Fikkert, Sari, Kertokalio, Aryandi, Romoli, F, Ismail, A, Ismalaj, E, Petricci, E, Neale, MJ, Bristow, RG, Masson, JY, Wyman, C.L., Jeggo, PA, Tainer, JA
Publikováno v:
Molecular Cell, 53(2), 361-361. Cell Press
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=narcis______::67a02313e0e51d0ccc9c28c01fe66021
https://pure.eur.nl/en/publications/3d0936c6-008e-449f-9be6-3571d8d42f6a
https://pure.eur.nl/en/publications/3d0936c6-008e-449f-9be6-3571d8d42f6a
Publikováno v:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
r-IIS La Fe. Repositorio Institucional de Producción Científica del Instituto de Investigación Sanitaria La Fe
instname
r-IIS La Fe. Repositorio Institucional de Producción Científica del Instituto de Investigación Sanitaria La Fe
instname
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=RECOLECTA___::16bef6638211ac781d3cd239bbc30554
https://fundanet.iislafe.san.gva.es/publicaciones/ProdCientif/PublicacionFrw.aspx?id=4263
https://fundanet.iislafe.san.gva.es/publicaciones/ProdCientif/PublicacionFrw.aspx?id=4263
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