The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The assay was conducted according to Bradford [15].”
From Functional and Bioactive Characterization of Hemp Cake Proteins and Polyphenols from Non-Psychoactive Cannabis sativa (2025) · cites this paper as Bradford [15]
In the citing paper
“The Bradford method for protein determination (Bradford, 1976) is based on the colour change in Coomassie blue G250 when it reacts with proteins.”
From Chemical methods for the characterization of proteolysis in cheese during ripening (1997) · cites this paper as Bradford, 1976
Citations
Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394
DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTION
Gornall, A. G., Bardawill, C. J., & David, M. M. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57021-6 · Cited by 16,164
A rapid, sensitive, and specific method for the determination of protein in dilute solution
Schaffner, W., & Weissmann, C. (1973) · Analytical Biochemistry · doi:10.1016/0003-2697(73)90217-0 · Cited by 2,527
Reisner, A. H., Nemes, P., & Bucholtz, C. A. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90461-3 · Cited by 618
Handbook of Biochemistry. Selected Data for Molecular Biology.
(1969) · Annals of Internal Medicine · doi:10.7326/0003-4819-70-1-239 · Cited by 559
PURIFICATION AND PROPERTIES OF FRUCTOSE-1,6-DIPHOSPHATASE
Mokrasch, L. C., & McGilvery, R. W. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65205-6 · Cited by 282
Phenolic Hydroxyl Ionization in Proteins. I. Bovine Serum Albumin1-3
Tanford, C., & Roberts, G. L. (1952) · Journal of the American Chemical Society · doi:10.1021/ja01130a017 · Cited by 189
Ein einfaches Verfahren zur Analyse der Serumproteine und anderer Proteingemische
Graßmann, W., & HANNIG, K. (1950) · Die Naturwissenschaften · doi:10.1007/bf00623155 · Cited by 175
Determination of proteins in “Tris” buffer by the biuret reaction
Robson, R., Goll, D. E., & Temple, M. J. (1968) · Analytical Biochemistry · doi:10.1016/0003-2697(68)90188-7 · Cited by 145
Simple Microassay of Protein with Membrane Filter
KUNO, H., & Kihara, H. K. (1967) · Nature · doi:10.1038/215974a0 · Cited by 121
Research works printed but not linked: 4
- Kaul, 1970, J. Food Sci. Technol, 7, 11
- Swaminathan, 1973, Indian J. Exp. Biol, 11, 63
- Sherbon, 1974, J. Assoc. Off. Anal. Chem, 57, 1338
- Wetlaufer, 1962, Advan. Prot. Chem, 17, 378
Cited by
Sorted by citations
Items 201–300 of 2,307
Chu, Z.-L., McKinsey, T. A., Liu, L., Gentry, J. J., Malim, M. H., & Ballard, D. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.19.10057 · Cited by 872
Mechanism of antibacterial activity of copper nanoparticles
Chatterjee, A. K., Chakraborty, R., & Basu, T. (2014) · Nanotechnology · doi:10.1088/0957-4484/25/13/135101 · Cited by 890
Reffitt, D. M., Ogston, N., Jugdaohsingh, R., Cheung, H. F. J., Evans, B. A. J., Thompson, R. P. H., Powell, J. J., & Hampson, G. N. (2003) · Bone · doi:10.1016/s8756-3282(02)00950-x · Cited by 876
Mogi, M., Harada, M., Kondo, T., Riederer, P., Inagaki, H., Minami, M., & Nagatsu, T. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90508-8 · Cited by 855
Cohen, S., Carpenter, G., & King, L. E. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85573-4 · Cited by 858
Sgk1-Dependent Stimulation of Cardiac Na+/H+Exchanger Nhe1 by Dexamethasone
Voelkl, J. G. J., Pasham, V., Ahmed, M. S. E., Walker, B., Szteyn, K., Kuhl, D., Metzler, B., Alesutan, I., & Lang, F. J. W. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350120 · Cited by 860
Burgomaster, K. A., Hughes, S. C., Heigenhauser, G. J. F., Bradwel, S. N., & Gibala, M. J. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01095.2004 · Cited by 856
Receptor-mediated in vitro gene transformation by a soluble DNA carrier system.
Wu, G. Y., & Wu, C. H. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61209-8 · Cited by 855
Expression in Escherichia coli of a Chemically Synthesized Gene for the Hormone Somatostatin
Itakura, K., Hirose, T., Crea, R., Riggs, A. D., Heyneker, H. L., Bolívar, F. G., & Boyer, H. W. (1977) · Science · doi:10.1126/science.412251 · Cited by 853
The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae.
Terbush, D. R., Maurice, T. C., Roth, D., & Novick, P. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01039.x · Cited by 843
In vitro toxicity of silica nanoparticles in human lung cancer cells
Lin, W., Huang, Y., Zhou, X., & Ma, Y. (2006) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2006.10.004 · Cited by 852
A 38,000-dalton membrane protein (p38) present in synaptic vesicles.
Jahn, R., SCHIEBLER, W., Ouimet, C. C., & Greengard, P. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4137 · Cited by 851
Belimov, A. A., Hontzeas, N., Сафронова, В. И., Demchinskaya, S. V., Piluzza, G., Bullitta, S., & Glick, B. R. (2004) · Soil Biology and Biochemistry · doi:10.1016/j.soilbio.2004.07.033 · Cited by 850
Silicon alleviates oxidative damage of wheat plants in pots under drought
Gong, H., Zhu, X., Chen, K., Wang, S., & Chenglie, Z. (2005) · Plant Science · doi:10.1016/j.plantsci.2005.02.023 · Cited by 852
Serini, G., Bochaton-Piallat, M.-L., Ropraz, P., Geinoz, A., Borsi, L., Zardi, L., & Gabbiani, G. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.3.873 · Cited by 847
Besufkad, A., Worku, Y., Desalegn, F., & Aragaw, D. (2018) · Zenodo (CERN European Organization for Nuclear Research) · doi:10.4172/2157 · Cited by 848
Göke, R., Fehmann, H. C., Linn, T., Schmidt, H., Krause, M., Eng, J., & Göke, B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36565-2 · Cited by 837
Wardzala, L. J., & Jeanrenaud, B. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68926-x · Cited by 839
Beresford, J. N., Bennett, J. H., Devlin, C., Leboy, P. S., & Owen, M. E. (1992) · Journal of Cell Science · doi:10.1242/jcs.102.2.341 · Cited by 826
Tsang, V. C. W., Brand, J. A., & Boyer, A. E. (1989) · The Journal of Infectious Diseases · doi:10.1093/infdis/159.1.50 · Cited by 836
Glycogen Synthase Kinase‐3 from Rabbit Skeletal Muscle
Noor, E. M. B. I., RYLATT, D. B., & Cohen, P. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb06059.x · Cited by 837
Oehm, A., Behrmann, I., Falk, W., Pawlita, M., Maier, G., Klas, C., Li-Weber, M., Richards, S., Dhein, J., & Trauth, B. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50076-x · Cited by 834
Purification and characterization of a newly identified growth factor specific for epithelial cells.
Rubin, J. S., Osada, H., Finch, P. W., Taylor, W., Rudikoff, S., & Aaronson, S. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.3.802 · Cited by 832
Matthews, J. R., Wakasugi, N., Virelizier, J., Yodoi, J., & Hay, R. T. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.15.3821 · Cited by 836
Boye, J. I., Aksay, S., Roufik, S., Ribéreau, S., Mondor, M., Farnworth, E. R., & Rajamohamed, S. H. (2009) · Food Research International · doi:10.1016/j.foodres.2009.07.021 · Cited by 913
Zero-length crosslinking procedure with the use of active esters
Grabarek, Z., & Gergely, J. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90267-d · Cited by 844
Bose, R., Verheij, M., Haimovitz‐Friedman, A., Scotto, K. W., FUKS, Z. Y., & Kolesnick, R. (1995) · Cell · doi:10.1016/0092-8674(95)90429-8 · Cited by 827
Biological monitoring: lichens as bioindicators of air pollution assessment — a review
Conti, M. E., & Cecchetti, G. (2001) · Environmental Pollution · doi:10.1016/s0269-7491(00)00224-4 · Cited by 823
Encinas, M., Iglesias, M., Liu, Y., Wang, H., Muhaisen, A., Ceña, V., Gallego, C., & Comella, J. X. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750991.x · Cited by 822
Polymeric Chains of SUMO-2 and SUMO-3 Are Conjugated to Protein Substrates by SAE1/SAE2 and Ubc9
Tatham, M. H., Jaffray, E., Vaughan, O. A., Desterro, J. M. P., Botting, C. H., Naismith, J. H., & Hay, R. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104214200 · Cited by 821
Stuehr, D. J., Cho, H. J., Kwon, N. S., Weise, M. F., & Nathan, C. F. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.17.7773 · Cited by 816
Scheinman, R. I., Gualberto, A., Jewell, C. M., Cidlowski, J. A., & Baldwin, A. S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.943 · Cited by 819
Molecular identification and isolation of the Waxy locus in maize
Shure, M., Wessler, S. R., & Fedoroff, N. V. (1983) · Cell · doi:10.1016/0092-8674(83)90225-8 · Cited by 811
Hartl, F. U., Pfanner, N., Nicholson, D. W., & Neupert, W. (1989) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(89)90002-6 · Cited by 801
Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
Kojro, E., Gimpl, G., Lammich, S., März, W., & Fahrenholz, F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081612998 · Cited by 804
Akt/Protein Kinase B Up-regulates Bcl-2 Expression through cAMP-response Element-binding Protein
Pugazhenthi, S., Nesterova, A., Sable, C., Heidenreich, K. A., Boxer, L. M., Heasley, L. E., & Reusch, J. E.-B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.15.10761 · Cited by 679
Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms
Talmadge, R. J., & Roy, R. R. (1993) · Journal of Applied Physiology · doi:10.1152/jappl.1993.75.5.2337 · Cited by 804
Molecular Characterization of a Phospholipase D Generating Anandamide and Its Congeners
Okamoto, Y., Morishita, J., Tsuboi, K., Tonai, T., & Ueda, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306642200 · Cited by 800
Elevated immune response in the brain of autistic patients
Li, X., Chauhan, A., Sheikh, A. M., Patil, S., Chauhan, V., Li, X.-M., Ji, L., Brown, T., & Malik, M. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2008.12.002 · Cited by 786
The p65 subunit is responsible for the strong transcription activating potential of NF‐kappa B.
Schmitz, M. L., & Baeuerle, P. A. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04950.x · Cited by 796
Demiral, T., & Türkan, İ. (2004) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2004.03.017 · Cited by 791
Koschinsky, T., He, C.-J., Mitsuhashi, T., Bucala, R., Liu, C., Buenting, C., Heitmann, K., & Vlassara, H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6474 · Cited by 792
Toward a Human Blood Serum Proteome
Adkins, J., Varnum, S. M., Auberry, K. J., Moore, R. J., Angell, N. H., Smith, R. D., Springer, D. L., & Pounds, J. G. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200066-mcp200 · Cited by 788
Iron fortification of rice seed by the soybean ferritin gene
Goto, F., Yoshihara, T., Shigemoto, N., Toki, S., & Takaiwa, F. (1999) · Nature Biotechnology · doi:10.1038/7029 · Cited by 793
Sharma, V., Anderson, D. C., & Dhawan, A. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0705-6 · Cited by 810
Dey, R., Pal, K. K., Bhatt, D. M., & Chauhan, S. (2004) · Microbiological Research · doi:10.1016/j.micres.2004.08.004 · Cited by 791
Wilden, U., Hall, S. W., & Kühn, H. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.5.1174 · Cited by 791
Cationic liposome-mediated RNA transfection.
Malone, R. W., Felgner, P. L., & Verma, I. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.16.6077 · Cited by 911
Regulation of Flowering by Trehalose-6-Phosphate Signaling in Arabidopsis thaliana
Wahl, V., Ponnu, J., Schlereth, A., Arrivault, S., Langenecker, T., Franke, A., Feil, R., Lunn, J. E., Stitt, M., & Schmid, M. (2013) · Science · doi:10.1126/science.1230406 · Cited by 785
Metal–Organic Framework-Based Enzyme Biocomposites
Liang, W., Wied, P., Carraro, F., Sumby, C. J., Nidetzky, B., Tsung, C., Falcaro, P., & Doonan, C. J. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01029 · Cited by 801
Cho, A.-S., Jeon, S.-M., Kim, M., Yeo, J., Seo, K., Choi, M., & Lee, M. (2010) · Food and Chemical Toxicology · doi:10.1016/j.fct.2010.01.003 · 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
Zsebo, K. M., Wypych, J., McNiece, I., Lu, H. S., Smith, K. A., Karkare, S. B., Sachdev, R. K., Yuschenkoff, V. N., Birkett, N. C., Williams, L. R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90300-4 · Cited by 786
Heme oxygenase: A novel target for the modulation of inflammatory response
Willis, D., Moore, A., Frederick, R., & Willoughby, D. A. (1996) · Nature Medicine · doi:10.1038/nm0196-87 · Cited by 782
Ethoxyresorufin-O-deethylase (EROD) Activity in Fish as a Biomarker of Chemical Exposure
Whyte, J. J., Jung, R. E., Schmitt, C. J., & Tillitt, D. E. (2000) · Critical Reviews in Toxicology · doi:10.1080/10408440091159239 · Cited by 782
Devys, D., Lutz, Y., Rouyer, N., Bellocq, J., & Mandel, J. (1993) · Nature Genetics · doi:10.1038/ng0893-335 · Cited by 781
Fukao, T., Xu, K., Ronald, P. C., & Bailey-Serres, J. N. (2006) · The Plant Cell · doi:10.1105/tpc.106.043000 · Cited by 781
Doxycycline-mediated quantitative and tissue-specific control of gene expression in transgenic mice.
Kistner, A., Gossen, M., Zimmermann, F., Jerecic, J., Ullmer, C., Lübbert, H., & Bujard, H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.10933 · Cited by 785
The Bradford Method For Protein Quantitation
Kruger, N. J. (2009) · Springer protocols handbooks/Springer protocols · doi:10.1007/978-1-59745-198-7_4 · Cited by 779
Microtubule assembly nucleated by isolated centrosomes
Mitchison, T. J., & Kirschner, M. W. (1984) · Nature · doi:10.1038/312232a0 · Cited by 779
A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles.
Cohen, S., Ushiro, H., Stoscheck, C. M., & Chinkers, M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68224-4 · Cited by 776
Flint, A. J., Tiganis, T., Barford, D., & Tonks, N. K. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.5.1680 · Cited by 775
Draetta, G. F., & Beach, D. (1988) · Cell · doi:10.1016/0092-8674(88)90175-4 · Cited by 775
Use of Cells Expressing γ Subunit Variants to Identify Diverse Mechanisms of AMPK Activation
Hawley, S. A., Ross, F. A., Chevtzoff, C., Green, K. A., Evans, A., Fogarty, S., Towler, M. C., Brown, L. J., Ogunbayo, O. A., Evans, A. M., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.04.001 · Cited by 773
Jasmonic acid carboxyl methyltransferase: A key enzyme for jasmonate-regulated plant responses
Seo, H. S., Song, J. T., Cheong, J., Lee, Y., Lee, Y., Hwang, I., Lee, J. S., & Choi, Y. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081557298 · Cited by 774
Shieh, F., Wang, S., Yen, C.-I., Wu, C.-C., Dutta, S., Chou, L., Morabito, J. V., Hu, P., Hsu, M.-H., Wu, K. C. ‐., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/ja513058h · Cited by 774
The target of ezetimibe is Niemann-Pick C1-Like 1 (NPC1L1)
Garcia-Calvo, M., Lisnock, J., Bull, H. G., Hawes, B. E., Burnett, D. A., Braun, M. P., Crona, J. H., Davis, H. R., Dean, D. C., Detmers, P. A., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500269102 · Cited by 670
Ichinose, H., Ohye, T., Takahashi, E.-I., Seki, N., Hori, T.-A., Segawa, M., Nomura, Y., Endo, K., Tanaka, H., Tsuji, S., et al. (1994) · Nature Genetics · doi:10.1038/ng1194-236 · Cited by 770
Chaoui, A., Mazhoudi, S., Ghorbal, M. H., & Ferjani, E. E. (1997) · Plant Science · doi:10.1016/s0168-9452(97)00115-5 · Cited by 769
[16] Protein determination in membrane and lipoprotein samples: Manual and automated procedures
Markwell, M. A. K., Haas, S. M., Tolbert, N. E., & BIEBER, L. L. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)72018-4 · Cited by 769
Duh, E. J., Maury, W. J., Folks, T. M., Fauci, A. S., & Rabson, A. B. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5974 · Cited by 767
Mack, D., Fischer, W., Krokotsch, A., Leopold, K., Hartmann, R., Egge, H., & Laufs, R. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.1.175-183.1996 · Cited by 885
Barboza, L. G. A., Vieira, L. R., Branco, V., Figueiredo, N., Carvalho, F., Carvalho, C., & Guilhermino, L. (2018) · Aquatic Toxicology · doi:10.1016/j.aquatox.2017.12.008 · Cited by 766
REVIEW: Biofortification of Durum Wheat with Zinc and Iron
Çakmak, İ., Pfeiffer, W., & McClafferty, B. (2010) · Cereal Chemistry · doi:10.1094/cchem-87-1-0010 · Cited by 765
Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins
Kascsak, R., Rubenstein, R., MERZ, P. A., Tonna-DeMasi, M., Fersko, R., Carp, R. I., Wisniewski, H. M., & Diringer, H. (1987) · Journal of Virology · doi:10.1128/jvi.61.12.3688-3693.1987 · Cited by 765
Herbivory-induced volatiles elicit defence genes in lima bean leaves
Arimura, G., Ozawa, R., Shimoda, T., Nishioka, T., Boland, W., & Takabayashi, J. (2000) · Nature · doi:10.1038/35020072 · Cited by 763
Effects of Calmodulin Antagonists on Radiation-induced Lipid Peroxidation in Microsomes
Varshney, R. K., & Kale, R. K. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552121 · Cited by 763
The Rel/NF-κB Family Directly Activates Expression of the Apoptosis Inhibitor Bcl-x L
Chen, C., Edelstein, L. C., & Gélinas, C. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2687-2695.2000 · Cited by 771
Li, Z., Agellon, L., Allen, T., Umeda, M., Jewell, L. S., Mason, A., & Vance, D. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.03.007 · Cited by 739
Mechanism of action of cytochalasin B on actin
MacLean-Fletcher, S. (1980) · Cell · doi:10.1016/0092-8674(80)90619-4 · Cited by 755
Regulated internalization of caveolae.
Parton, R. G., Joggerst, B., & Simons, K. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.5.1199 · Cited by 755
Eggert, C., Temp, U., & Eriksson, K. ‐. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.4.1151-1158.1996 · Cited by 755
Kong, X., Onrust, R., O’Donnell, M. E., & Kuriyan, J. (1992) · Cell · doi:10.1016/0092-8674(92)90445-i · Cited by 757
Multiple promoters direct tissue-specific expression of the rat BDNF gene
Timmusk, T., Palm, K., Metsis, M., Reintam, T., Paalme, V., Saarma, M., & Persson, H. (1993) · Neuron · doi:10.1016/0896-6273(93)90335-o · Cited by 858
Generation of superoxide by purified brain nitric oxide synthase
Pou, S., Pou, W. S., Bredt, D. S., Snyder, S. H., & Rosen, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35745-4 · Cited by 750
Liang, Y., Chen, Q. I. N., Liu, Q., Zhang, W., & Ding, R. (2003) · Journal of Plant Physiology · doi:10.1078/0176-1617-01065 · Cited by 749
PARP-2, A Novel Mammalian DNA Damage-dependent Poly(ADP-ribose) Polymerase
Amé, J., Rolli, V., Schreiber, V., Niedergang, C., Apiou, F., Decker, P., Muller, S., Höger, T. H., Murcia, J. M., & de MURCIA, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17860 · Cited by 744
Antioxidant activity of sulfated polysaccharide fractions extracted from Laminaria japonica
Wang, J., Zhang, Q., Zhang, Z., & Li, Z. (2007) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2007.10.003 · Cited by 745
Vistica, D. T., Skehan, P., Scudiero, D. A., Monks, A. P., Pittman, A. F., & Boyd, M. R. (1991) · PubMed · Cited by 745
Hernández, J. A., Ferrer, M. Á., Jiménez, A., Barceló, A. R., & Sevilla, F. (2001) · PLANT PHYSIOLOGY · doi:10.1104/pp.010188 · Cited by 744
Kessler, M., Terramani, T., Lynch, G., & Baudry, M. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb01881.x · Cited by 649
Inoguchi, T., Battan, R., Handler, E., Sportsman, J. R., Heath, W., & King, G. L. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.11059 · Cited by 739
Enhanced Myocardial Function in Transgenic Mice Overexpressing the β 2 -Adrenergic Receptor
Milano, C. A., Allen, L. F., Rockman, H. A., Dolber, P. C., McMinn, T. R., Chien, K. R., Johnson, T. D., Bond, R. A., & Lefkowitz, R. J. (1994) · Science · doi:10.1126/science.8160017 · Cited by 739
Frataxin is Reduced in Friedreich Ataxia Patients and is Associated with Mitochondrial Membranes
Campuzano, V., Montermini, L., Lutz, Y., Cova, L., Hindelang, C., Jiralerspong, S., Trottier, Y., Kish, S. J., Faucheux, B. A., Trouillas, P., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.11.1771 · Cited by 739
Flow of information in the light-triggered cyclic nucleotide cascade of vision.
Fung, B. K.-K., Hurley, J. B., & Stryer, L. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.1.152 · Cited by 738
Lin, K.-H., Huang, M.-Y., Huang, W.-D., Hsu, M.-H., Yang, Z.-W., & Yang, C.-M. (2013) · Scientia Horticulturae · doi:10.1016/j.scienta.2012.10.002 · Cited by 740
Arnold, R. S., Sun, Q., Sun, C. Q., Richards, J. C., O’Hearn, S. F., Osunkoya, A. O., Wallace, D. C., & Petros, J. A. (2012) · BioMed Research International · doi:10.1155/2013/239257 · Cited by 737
Mercury Methylation by Novel Microorganisms from New Environments
Gilmour, C. C., Podar, M., Bullock, A. L., Graham, A. M., Brown, S. D., Somenahally, A., Johs, A., Hurt, R. A., Bailey, K. L., & Elias, D. A. (2013) · Environmental Science & Technology · doi:10.1021/es403075t · Cited by 780
Cellular responses induced by silver nanoparticles: In vitro studies
Arora, S., Jain, J., Rajwade, J. M., & Paknikar, K. M. (2008) · Toxicology Letters · doi:10.1016/j.toxlet.2008.04.009 · Cited by 736
Sun, P., Enslen, H., Myung, P. S., & Maurer, R. A. (1994) · Genes & Development · doi:10.1101/gad.8.21.2527 · Cited by 744
Metadata
- Authors
- Bradford, M. M.
- Affiliations
- University of Georgia (US)
- Corresponding author
- Bradford, Marion M.
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 1976-05
- Volume
- 72
- Issue
- 1-2
- Pages
- 248-254
- ISSN
- 0003-2697 (ISSN-L)
- OpenAlex
- W2128635872
- Cited by
- 255,302
- References
- 20
- Citations by year
- 2026: 4653 · 2025: 6079 · 2024: 6445 · 2023: 6652 · 2022: 7284 · 2021: 7677 · 2020: 7719 · 2019: 7373 · 2018: 7128 · 2017: 6899 · 2016: 7250 · 2015: 7450 · 2014: 7796 · 2013: 7638 · 2012: 7600
- FWCI
- 124.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Analytical Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- protein quantification, Coomassie Brilliant Blue G-250, dye-protein binding, colorimetric assay, absorption maximum shift, detergent interference, sodium dodecyl sulfate, Triton X-100
- MeSH terms
- Binding Sites, Colorimetry, Methods, Microchemistry, Protein Binding, Proteins, Rosaniline Dyes, Time Factors
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