The DOI matches its Crossref record.
A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae.
Open accessAbstract
A series of yeast shuttle vectors and host strains has been created to allow more efficient manipulation of DNA in Saccharomyces cerevisiae. Transplacement vectors were constructed and used to derive yeast strains containing nonreverting his3, trp1, leu2 and ura3 mutations. A set of YCp and YIp vectors (pRS series) was then made based on the backbone of the multipurpose plasmid pBLUESCRIPT. These pRS vectors are all uniform in structure and differ only in the yeast selectable marker gene used (HIS3, TRP1, LEU2 and URA3). They possess all of the attributes of pBLUESCRIPT and several yeast-specific features as well. Using a pRS vector, one can perform most standard DNA manipulations in the same plasmid that is introduced into yeast.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
Correlation between Protein and mRNA Abundance in Yeast
Gygi, S. P., Rochon, Y., Franza, B. R., & Aebersold, R. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.1720 · Cited by 3,819
Kaeberlein, M., McVey, M., & Guarente, L. (1999) · Genes & Development · doi:10.1101/gad.13.19.2570 · Cited by 2,253
Extrachromosomal rDNA circles—a cause of aging in yeast
Sinclair, D. A., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80493-6 · Cited by 1,500
Bishop, D. K., Park, D., Xu, L., & Kleckner, N. (1992) · Cell · doi:10.1016/0092-8674(92)90446-j · Cited by 1,144
Kihara, A., Noda, T., Ishihara, N., & Ohsumi, Y. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.3.519 · Cited by 1,004
The MKK2 Pathway Mediates Cold and Salt Stress Signaling in Arabidopsis
Teige, M., Scheikl, E., Eulgem, T., Dóczi, R., Ichimura, K., Shinozaki, K., Dangl, J. L., & Hirt, H. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.06.023 · Cited by 1,002
Formation Process of Autophagosome Is Traced with Apg8/Aut7p in Yeast
Kirisako, T., Baba, M., Ishihara, N., Miyazawa, K., Ohsumi, M., Yoshimori, T., Noda, T., & Ohsumi, Y. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.2.435 · Cited by 881
Sequence-specific antimicrobials using efficiently delivered RNA-guided nucleases
Citorik, R. J., Mimee, M., & Lu, T. K. (2014) · Nature Biotechnology · doi:10.1038/nbt.3011 · Cited by 808
Reduced levels of hsp90 compromise steroid receptor action in vivo
Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787
Dever, T. E., Feng, L., Wek, R. C., Cigan, A. M., Donahue, T. F., & Hinnebusch, A. G. (1992) · Cell · doi:10.1016/0092-8674(92)90193-g · Cited by 776
TLC1 : Template RNA Component of Saccharomyces cerevisiae Telomerase
Singer, M. S., & Gottschling, D. E. (1994) · Science · doi:10.1126/science.7545955 · Cited by 736
Disruption of CREB function in brain leads to neurodegeneration
Mantamadiotis, T., Lemberger, T., Bleckmann, S. C., Kern, H., Kretz, O., Villalba, A. M., Tronche, F., Kellendonk, C., Gau, D., Kapfhammer, J., et al. (2002) · Nature Genetics · doi:10.1038/ng882 · Cited by 684
Dancis, A., Yuan, D. S., Haile, D., Askwith, C., Eide, D., Moehle, C., Kaplan, J., & Klausner, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90345-x · Cited by 659
Atg9 vesicles are an important membrane source during early steps of autophagosome formation
Yamamoto, H., Kakuta, S., Watanabe, T. M., Kitamura, A., Sekito, T., Kondo-Kakuta, C., Ichikawa, R., Kinjo, M., & Ohsumi, Y. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201202061 · Cited by 659
Intragenic tandem repeats generate functional variability
Verstrepen, K. J., Jansen, A., Lewitter, F., & Fink, G. R. (2005) · Nature Genetics · doi:10.1038/ng1618 · Cited by 616
Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus
Mochida, K., Oikawa, Y., Kimura, Y., Kirisako, H., Hirano, H., Ohsumi, Y., & Nakatogawa, H. (2015) · Nature · doi:10.1038/nature14506 · Cited by 611
Paeschke, K., Capra, J. A., & Zakian, V. A. (2011) · Cell · doi:10.1016/j.cell.2011.04.015 · Cited by 566
A Genetic Map of the Response to DNA Damage in Human Cells
Olivieri, M., Cho, T., Álvarez-Quilón, A., Li, K., Schellenberg, M. J., Zimmermann, M., Hustedt, N., Rossi, S. E., Adam, S., Melo, H., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.040 · Cited by 551
Calcineurin is required for virulence of Cryptococcus neoformans
Odom, A., Muir, S., Lim, E., Toffaletti, D. L., Perfect, J., & Heitman, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.10.2576 · Cited by 516
Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
Schlicker, C., Gertz, M., Papatheodorou, P., Kachholz, B., Becker, C. F. W., & Steegborn, C. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.048 · Cited by 531
An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis
Mari, M., Griffith, J., Rieter, E., Krishnappa, L., Klionsky, D. J., & Reggiori, F. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200912089 · Cited by 491
Stathopoulos, A. M., & Cyert, M. S. (1997) · Genes & Development · doi:10.1101/gad.11.24.3432 · Cited by 442
The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by the VPS10 gene
Marcusson, E. G., Horazdovsky, B. F., Cereghino, J. L., Gharakhanian, E., & Emr, S. D. (1994) · Cell · doi:10.1016/0092-8674(94)90219-4 · Cited by 439
Xie, Y., & Varshavsky, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.071022298 · Cited by 436
Berger, S. L., Piña, B., Silverman, N., Marcus, G. A., Agapite, J., Regier, J. L., Triezenberg, S. J., & Guarente, L. (1992) · Cell · doi:10.1016/0092-8674(92)90100-q · Cited by 435
Cunningham, K. W., & Fink, G. R. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.5.2226 · Cited by 431
Mutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
Nathan, D. F., & Lindquist, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3917 · Cited by 423
An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function
Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., Cotter, R. J., Felts, S., Toft, D., Karnitz, L., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.008 · Cited by 413
Telomerase-Mediated Telomere Addition In Vivo Requires DNA Primase and DNA Polymerases α and δ
Diede, S. J., & Gottschling, D. E. (1999) · Cell · doi:10.1016/s0092-8674(00)81670-0 · Cited by 379
Kennedy, B. K., Gotta, M., Sinclair, D. A., Mills, K., McNabb, D. S., Murthy, M., Pak, S. M., Laroche, T., Gasser, S. M., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80219-6 · Cited by 375
Rapaport, D., Brunner, M., Neupert, W., & Westermann, B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20150 · Cited by 370
Morrow, D. M., Tagle, D. A., Shiloh, Y., Collins, F. S., & Hieter, P. (1995) · Cell · doi:10.1016/0092-8674(95)90480-8 · Cited by 370
Self-citationIn vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone
Nathan, D. F., Vos, M. H., & Lindquist, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.12949 · Cited by 364
Monitoring disulfide bond formation in the eukaryotic cytosol
Østergaard, H., Tachibana, C., & Winther, J. R. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200402120 · Cited by 333
Matheos, D. P., Kingsbury, T. J., Ahsan, U. S., & Cunningham, K. W. (1997) · Genes & Development · doi:10.1101/gad.11.24.3445 · Cited by 332
Interorganelle signaling is a determinant of longevity in Saccharomyces cerevisiae
Kirchman, P. A., Kim, S., Lai, C.-Y., & Jazwinski, S. M. (1999) · Genetics · doi:10.1093/genetics/152.1.179 · Cited by 328
Sorting of proteins into multivesicular bodies: ubiquitin‐dependent and ‐independent targeting
Reggiori, F., & Pelham, H. R. B. (2001) · The EMBO Journal · doi:10.1093/emboj/20.18.5176 · Cited by 324
Boyd, C., Hughes, T., Pypaert, M., & Novick, P. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200408124 · Cited by 312
Cyert, M. S., Kunisawa, R., Kaim, D., & Thorner, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7376 · Cited by 289
Mutagenic Processing of Ribonucleotides in DNA by Yeast Topoisomerase I
Kim, N., Huang, S.-Y. N., Williams, J. S., Li, Y. C., Clark, A. B., Cho, J.-E., Kunkel, T. A., Pommier, Y., & Jinks-Robertson, S. (2011) · Science · doi:10.1126/science.1205016 · Cited by 291
Friedman, J. R., Mourier, A., Yamada, J., McCaffery, J. M., & Nunnari, J. (2015) · eLife · doi:10.7554/elife.07739 · Cited by 291
Hirst, J., Lui, W. W. Y., Bright, N. A., Totty, N., Seaman, M. N. J., & Robinson, M. S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.1.67 · Cited by 291
Zhou, H., Cheng, J.-S., Wang, B. L., Fink, G. R., & Stephanopoulos, G. (2012) · Metabolic Engineering · doi:10.1016/j.ymben.2012.07.011 · Cited by 287
Upc2p and Ecm22p, Dual Regulators of Sterol Biosynthesis in Saccharomyces cerevisiae
Vik, Å., & Rine, J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.19.6395-6405.2001 · Cited by 277
Cell cycle-regulated histone acetylation required for expression of the yeast HO gene
Krebs, J. E., Kuo, M.-H., Allis, C. D., & Peterson, C. L. (1999) · Genes & Development · doi:10.1101/gad.13.11.1412 · Cited by 275
Marcus, G. A., Silverman, N., Berger, S. L., Horiuchi, J., & Guarente, L. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06806.x · Cited by 276
Hu, J., Dong, L., & Outten, C. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803028200 · Cited by 273
Lickwar, C. R., Mueller, F., Hanlon, S. E., McNally, J. G., & Lieb, J. D. (2012) · Nature · doi:10.1038/nature10985 · Cited by 241
Apg10p, a novel protein‐conjugating enzyme essential for autophagy in yeast
Shintani, T., Mizushima, N., Ogawa, Y., Matsuura, A., Noda, T., & Ohsumi, Y. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5234 · Cited by 269
Atg9 Cycles Between Mitochondria and the Pre-Autophagosomal Structure in Yeasts
Reggiori, F., Shintani, T., Chong, H., Nair, U., & Klionsky, D. J. (2005) · Autophagy · doi:10.4161/auto.1.2.1840 · Cited by 266
Functional Genetic Variants Revealed by Massively Parallel Precise Genome Editing
Sharon, E., Chen, S.-A. A., Khosla, N. M., Smith, J. D., Pritchard, J. K., & Fraser, H. B. (2018) · Cell · doi:10.1016/j.cell.2018.08.057 · Cited by 225
Burgess, S. M., Delannoy, M., & Jensen, R. E. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.6.1375 · Cited by 249
Mitochondrial protein synthesis adapts to influx of nuclear-encoded protein
Richter-Dennerlein, R., Oeljeklaus, S., Lorenzi, I., Ronsör, C., Bareth, B., Schendzielorz, A. B., Wang, C., Warscheid, B., Rehling, P., & Dennerlein, S. (2016) · Cell · doi:10.1016/j.cell.2016.09.003 · Cited by 232
Pif1p Helicase, a Catalytic Inhibitor of Telomerase in Yeast
Zhou, J.-Q., Monson, E. K., Teng, S.-C., Schulz, V. P., & Zakian, V. A. (2000) · Science · doi:10.1126/science.289.5480.771 · Cited by 236
Scholes, D. T., Banerjee, M., Bowen, B., & Curcio, M. J. (2001) · Genetics · doi:10.1093/genetics/159.4.1449 · Cited by 235
Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane
Umebayashi, K., & Nakano, A. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200303088 · Cited by 230
Schweizer, A., Rupp, S., Taylor, B. N., Röllinghoff, M., & Schröppel, K. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02132.x · Cited by 232
Mechanism of Metabolic Control
Komeili, A., Wedaman, K. P., O'Shea, E. K., & Powers, T. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.4.863 · Cited by 230
Nonklang, S., Abdel-Banat, B. M. A., Cha-aim, K., Moonjai, N., Hoshida, H., Limtong, S., Yamada, M., & Akada, R. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.01854-08 · Cited by 215
Finegold, A. A., Shatwell, K. P., Segal, A. W., Klausner, R. D., & Dancis, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.49.31021 · Cited by 213
Merz, S., & Westermann, B. (2009) · Genome Biology · doi:10.1186/gb-2009-10-9-r95 · Cited by 213
A Homolog of Voltage-Gated Ca 2+ Channels Stimulated by Depletion of Secretory Ca 2+ in Yeast
Locke, E. G., Bonilla, M., Liang, L., Takita, Y., & Cunningham, K. W. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.18.6686-6694.2000 · Cited by 212
van de Peppel, J., Kettelarij, N., van Bakel, H., Kockelkorn, T. T. J. P., van Leenen, D., & Holstege, F. C. P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.033 · Cited by 211
Isolation of Hsp90 mutants by screening for decreased steroid receptor function.
Bohen, S. P., & Yamamoto, K. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11424 · Cited by 195
Hallstrom, T. C., & Moye-Rowley, W. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007338200 · Cited by 194
Berger, K. H., Sogo, L. F., & Yaffe, M. P. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.3.545 · Cited by 197
Paidhungat, M., & Garrett, S. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6339 · Cited by 191
Telomere length control and transcriptional regulation of subtelomeric adhesins in Candida glabrata
Castaño, I., Pan, S., Zupancic, M., Hennequin, C., Dujon, B., & Cormack, B. P. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04465.x · Cited by 188
Bungert, J., Davé, U., Lim, K. C., Lieuw, K. H., Shavit, J. A., Liu, Q., & Engel, J. D. (1995) · Genes & Development · doi:10.1101/gad.9.24.3083 · Cited by 183
Suppressors of Superoxide Dismutase (SOD1) Deficiency in Saccharomyces cerevisiae
Strain, J., Lorenz, C. R., Bode, J., Garland, S., Smolen, G. A., Ta, D. T., Vickery, L. E., & Culotta, V. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.47.31138 · Cited by 181
Mediator protein mutations that selectively abolish activated transcription
Myers, L. C., Gustafsson, C. M., Hayashibara, K. C., Brown, P. O., & Kornberg, R. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.1.67 · Cited by 181
Bulawa, C. E. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.4.1764 · Cited by 178
Ramírez, M. A., & Lorenz, M. C. (2007) · Eukaryotic Cell · doi:10.1128/ec.00372-06 · Cited by 174
Arora, C., Kee, K., Maleki, S., & Keeney, S. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00063-2 · Cited by 173
The Saccharomyces cerevisiae Proteome of Oxidized Protein Thiols
Le Moan, N., Clement, G., Le Maout, S., Tacnet, F., & Toledano, M. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513346200 · Cited by 170
HOWE, K. J., KANE, C. M., & ARES, M. (2003) · RNA · doi:10.1261/rna.5390803 · Cited by 169
A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation.
Laloraya, S., Gambill, B. D., & Craig, E. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.14.6481 · Cited by 165
Bardwell, L., Cook, J. G., Chang, E. C., Cairns, B. R., & Thorner, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3637 · Cited by 161
The Ubiquitin-Proteasome System Regulates Mitochondrial Intermembrane Space Proteins
Bragoszewski, P., Gornicka, A., Sztolsztener, M. E., & Chacinska, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01579-12 · Cited by 149
Park, P. U., Defossez, P.-A., & Guarente, L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3848 · Cited by 155
Cruz, M. C., Goldstein, A. L., Blankenship, J., Del Poeta, M., Perfect, J. R., McCusker, J. H., Bennani, Y. L., Cardenas, M. E., & Heitman, J. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.11.3162-3170.2001 · Cited by 159
Shani, N., & Valle, D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11901 · Cited by 157
Clausen, M., Lamb, C. J., Megnet, R., & Doerner, P. W. (1994) · Gene · doi:10.1016/0378-1119(94)90363-8 · Cited by 155
A second iron-regulatory system in yeast independent of Aft1p
Rutherford, J. C., Jaron, S., Ray, E., Brown, P. O., & Winge, D. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.261381198 · Cited by 153
Youngman, M. J., Hobbs, A. E. A., Burgess, S. M., Srinivasan, M., & Jensen, R. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200308012 · Cited by 148
Iron Acquisition from Transferrin by Candida albicans Depends on the Reductive Pathway
Knight, S. A. B., Vilaire, G., Lesuisse, E., & Dancis, A. (2005) · Infection and Immunity · doi:10.1128/iai.73.9.5482-5492.2005 · Cited by 145
Analysis of the oxidative stress regulation of the Candida albicans transcription factor, Cap1p
Zhang, X., De Micheli, M., Coleman, S. T., Sanglard, D., & Moye‐Rowley, W. S. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01877.x · Cited by 146
From Structure to Systems: High-Resolution, Quantitative Genetic Analysis of RNA Polymerase II
Braberg, H., Jin, H., Moehle, E. A., Chan, Y. A., Wang, S., Shales, M., Benschop, J. J., Morris, J. H., Qiu, C., Hu, F., et al. (2013) · Cell · doi:10.1016/j.cell.2013.07.033 · Cited by 143
Self-citationAutophagy supports Candida glabrata survival during phagocytosis
Roetzer, A., Gratz, N., Kovarik, P., & Schüller, C. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2009.01391.x · Cited by 142
A Selective Transport Route from Golgi to Late Endosomes That Requires the Yeast Gga Proteins
Black, M. W., & Pelham, H. R. B. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.3.587 · Cited by 140
Davies, B. S. J., Wang, H. S., & Rine, J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.16.7375-7385.2005 · Cited by 138
Krappmann, S., Bignell, E. M., Reichard, U., Rogers, T., Haynes, K., & Braus, G. H. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04015.x · Cited by 133
Calcineurin is essential in cyclosporin A- and FK506-sensitive yeast strains.
Breuder, T., Hemenway, C. S., Movva, N. R., Cardenas, M. E., & Heitman, J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5372 · Cited by 135
Heat stress-induced life span extension in yeast
Shama, S., Lai, C.-Y., Antoniazzi, J. M., Jiang, J. C., & Jazwinski, S. M. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4279 · Cited by 135
PXA1, a possible Saccharomyces cerevisiae ortholog of the human adrenoleukodystrophy gene.
Shani, N., Watkins, P. A., & Valle, D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.13.6012 · Cited by 129
Roetzer, A., Gregori, C., Jennings, A. M., Quintin, J., Ferrandon, D., Butler, G., Kuchler, K., Ammerer, G., & Schüller, C. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06301.x · Cited by 124
Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin.
Imai, J., & Yahara, I. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9262-9270.2000 · Cited by 123
Crowley, J. H., Leak, F. W., Shianna, K. V., Tove, S., & Parks, L. W. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.16.4177-4183.1998 · Cited by 123
Li, S., Smith, K. D., Davis, J. H., Gordon, P. B., Breaker, R. R., & Strobel, S. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1310439110 · Cited by 122
Metadata
- Authors
- Sikorski, R. S., & Hieter, P.
- Venue
- Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 1989-05-01
- Volume
- 122
- Issue
- 1
- Pages
- 19-27
- ISSN
- 0016-6731 (ISSN-L)
- 1943-2631
- OpenAlex
- W2169333620
- Cited by
- 8,664
- References
- 0
- FWCI
- 43.27
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.