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 101–200 of 2,307
Harrison, J. K., Jiang, Y., Chen, S., Xia, Y., Maciejewski, D., McNamara, R. K., Streit, W. J., Salafranca, M. N., Adhikari, S., Thompson, D. A., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10896 · Cited by 1,176
bcl-2 inhibits multiple forms of apoptosis but not negative selection in thymocytes
Sentman, C. L., Shutter, J. R., Hockenbery, D. M., Kanagawa, O., & Korsmeyer, S. J. (1991) · Cell · doi:10.1016/0092-8674(91)90361-2 · Cited by 1,188
Cho, K.-O., Hunt, C. A., & Kennedy, M. B. (1992) · Neuron · doi:10.1016/0896-6273(92)90245-9 · Cited by 1,188
Drake, T. A., Morrissey, J. H., & Edgington, T. S. (1989) · Europe PMC (PubMed Central) · Cited by 1,192
Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane
Eskes, R., Desagher, S., Antonsson, B. E., & Martinou, J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.929-935.2000 · Cited by 1,212
The Novel Anticonvulsant Drug, Gabapentin (Neurontin), Binds to the α2δ Subunit of a Calcium Channel
GEE, N. S., Brown, J. P., Dissanayake, V. U. K., Offord, J., Thurlow, R. J., & Woodruff, G. N. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5768 · Cited by 1,182
Brown adipose tissue regulates glucose homeostasis and insulin sensitivity
Stanford, K. I., Middelbeek, R. J. W., Townsend, K. L., An, D., Nygaard, E. B., Hitchcox, K. M., Markan, K. R., Nakano, K., Hirshman, M. F., Tseng, Y.-H., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci62308 · Cited by 1,180
Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones
Luo, Y., Raible, D. W., & Raper, J. A. (1993) · Cell · doi:10.1016/0092-8674(93)80064-l · Cited by 1,177
Clark, B. J., Wells, J., King, S. R., & Stocco, D. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)46930-x · Cited by 1,168
Meloni, D. A., Oliva, M. A., Martínez, C. A., & Cambraia, J. (2002) · Environmental and Experimental Botany · doi:10.1016/s0098-8472(02)00058-8 · Cited by 1,173
Sawadogo, M., & Roeder, R. (1985) · Cell · doi:10.1016/0092-8674(85)90021-2 · Cited by 925
Diorio, D., Viau, V, & Meaney, M. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-09-03839.1993 · Cited by 1,151
Review of the folin phenol protein quantitation method of lowry, rosebrough, farr and randall
Peterson, G. L. (1979) · Analytical Biochemistry · doi:10.1016/0003-2697(79)90222-7 · Cited by 1,147
Aminoguanidine Prevents Diabetes-Induced Arterial Wall Protein Cross-Linking
Brownlee, M., Vlassara, H., Kooney, A., Ulrich, P. C., & Cerami, A. (1986) · Science · doi:10.1126/science.3487117 · Cited by 1,146
Natarajan, K., Singh, S., Burke, T. R., Grünberger, D., & Aggarwal, B. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.17.9090 · Cited by 1,144
Isolation and characterization of plant cell walls and cell wall components
York, W. S., Darvill, A. G., McNeil, M., Stevenson, T. T., & Albersheim, P. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)18062-1 · Cited by 1,129
Stuehr, D. J., & Marletta, M. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.22.7738 · Cited by 1,126
Cramton, S. E., Gerke, C., Schnell, N. F., Nichols, W. W., & Götz, F. (1999) · Infection and Immunity · doi:10.1128/iai.67.10.5427-5433.1999 · Cited by 1,126
c-Myc transactivation of LDH-A : Implications for tumor metabolism and growth
Shim, H., Dolde, C., Lewis, B. C., Wu, C.-S., Dang, G., Jungmann, R. A., Dalla-Favera, R., & Dang, C. V. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6658 · Cited by 1,092
Xie, Q. W., Whisnant, R., & Nathan, C. F. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.177.6.1779 · Cited by 1,118
Galactinol and Raffinose Constitute a Novel Function to Protect Plants from Oxidative Damage
Nishizawa‐Yokoi, A., Yabuta, Y., & Shigeoka, S. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.122465 · Cited by 1,118
Dubbels, R., Reiter, R. J., Klenke, E., Goebel, A., Schnakenberg, E., Ehlers, C., SCHIWARA, H. W., & Schloot, W. (1995) · Journal of Pineal Research · doi:10.1111/j.1600-079x.1995.tb00136.x · Cited by 1,104
rab5 controls early endosome fusion in vitro
Gorvel, J., Chavrier, P., Zerial, M., & Gruenberg, J. E. (1991) · Cell · doi:10.1016/0092-8674(91)90316-q · Cited by 1,094
Van Cauwenberghe, L., Claessens, M., Vandegehuchte, M. B., & Janssen, C. R. (2015) · Environmental Pollution · doi:10.1016/j.envpol.2015.01.008 · Cited by 1,084
Gilmour, S. J., Sebolt, A. M., Salazar, M. P., Everard, J. D., & Thomashow, M. F. (2000) · PLANT PHYSIOLOGY · doi:10.1104/pp.124.4.1854 · Cited by 1,081
Marui, N., Offermann, M. K., Swerlick, R., Kunsch, C., Rosen, C. A., Ahmad, M., Alexander, R. W., & Medford, R. M. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116778 · Cited by 1,072
Matsui, T., Amano, M., Yamamoto, T., Chihara, K., Nakafuku, M., Ito, M., Nakano, T., Okawa, K., Iwamatsu, A., & Kaibuchi, K. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00574.x · Cited by 1,062
T cell growth factor receptors. Quantitation, specificity, and biological relevance
Robb, R., Munck, A. U., & Smith, K. (1981) · The Journal of Experimental Medicine · doi:10.1084/jem.154.5.1455 · Cited by 1,062
Creely, S. J., McTernan, P. G., Kusminski, C. M., Fisher, F. M., Da Silva, N. F., Khanolkar, M., Evans, M., Harte, A. L., & Kumar, S. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00302.2006 · Cited by 1,043
Penninckx, I. A. M. A., Thomma, B. P. H. J., Buchala, A. J., Métraux, J., & Broekaert, W. F. (1998) · The Plant Cell · doi:10.1105/tpc.10.12.2103 · Cited by 1,038
Inducible isoforms of cyclooxygenase and nitric-oxide synthase in inflammation.
Vane, J. R., Mitchell, J. A., Appleton, I., Tomlinson, A., Bishop‐Bailey, D., Croxtall, J. D., & Willoughby, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.6.2046 · Cited by 1,035
Xu, D., Duan, X., Wang, B., Hong, B., Ho, T., & Wu, R. (1996) · PLANT PHYSIOLOGY · doi:10.1104/pp.110.1.249 · Cited by 1,034
The retinoblastoma protein is phosphorylated during specific phases of the cell cycle
Buchkovich, K., Duffy, L. A., & Harlow, E. (1989) · Cell · doi:10.1016/0092-8674(89)90508-4 · Cited by 995
Abel, T., Nguyen, P. V., Barad, M., Deuel, T. A. S., Kandel, E. R., & Bourtchouladze, R. (1997) · Cell · doi:10.1016/s0092-8674(00)81904-2 · Cited by 1,217
Subcellular Distribution of Superoxide Dismutases (SOD) in Rat Liver
Okado‐Matsumoto, A., & Fridovich, I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105395200 · Cited by 1,036
Siekierka, J. J., Hung, S. H. Y., Poe, M., Lin, C. S., & SIGAL, N. H. (1989) · Nature · doi:10.1038/341755a0 · Cited by 1,016
Kieffer, B. L., Befort, K., Gavériaux‐Ruff, C., & HIRTH, C. G. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.12048 · Cited by 994
Ram�rez-Zacar�as, J. L., Castro‐Muñozledo, F., & Kuri‐Harcuch, W. (1992) · Histochemistry and Cell Biology · doi:10.1007/bf00316069 · Cited by 1,009
Feys, B. J., Benedetti, C. E., Penfold, C. N., & Turner, J. G. (1994) · The Plant Cell · doi:10.1105/tpc.6.5.751 · Cited by 1,007
Mogi, M., Harada, M., Riederer, P., Narabayashi, H., Fujita, K., & Nagatsu, T. (1994) · Neuroscience Letters · doi:10.1016/0304-3940(94)90746-3 · Cited by 986
beta-Glucuronidase from Escherichia coli as a gene-fusion marker.
Jefferson, R., Burgess, S. M., & Hirsh, D. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.22.8447 · Cited by 992
Deák, M., Clifton, A. D., Lucocq, J. M., & Alessi, D. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4426 · Cited by 1,004
Frumento, G., Rotondo, R., Tonetti, M., Damonte, G., Benatti, U., & Ferrara, G. B. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020121 · Cited by 1,133
Assessment of mitochondrial respiratory chain enzymatic activities on tissues and cultured cells
Spinazzi, M., Casarin, A., Pertegato, V., Salviati, L., & Angelini, C. I. (2012) · Nature Protocols · doi:10.1038/nprot.2012.058 · Cited by 1,007
Xynos, I. D., Edgar, A. J., Buttery, L. D. K., Hench, L. L., & Polak, J. M. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3503 · Cited by 983
Yokoyama, C., Wang, X., Briggs, M. R., Admon, A., Wu, J., Hua, X., Goldstein, J. L., & Brown, M. S. (1993) · Cell · doi:10.1016/s0092-8674(05)80095-9 · Cited by 979
Pollock, J. S., Förstermann, U., Mitchell, J. A., Warner, T. D., Schmidt, H. H. H. W., Nakane, M., & Murad, F. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.23.10480 · Cited by 979
Identification of a protein required for disulfide bond formation in vivo.
Bardwell, J., McGovern, K., & Beckwith, J. (1991) · Cell · doi:10.1016/0092-8674(91)90532-4 · Cited by 961
Koelle, M. R., Talbot, W. S., Segraves, W. A., Bender, M. T., Cherbas, P. T., & Hogness, D. S. (1991) · Cell · doi:10.1016/0092-8674(91)90572-g · Cited by 966
The Genetic Basis for Bacterial Mercury Methylation
Parks, J. M., Johs, A., Podar, M., Bridou, R., Hurt, R. A., Smith, S. D., Tomanicek, S. J., Qian, Y., Brown, S. D., Brandt, C. C., et al. (2013) · Science · doi:10.1126/science.1230667 · Cited by 966
Feedback control of mitosis in budding yeast
Li, R., & Murray, A. W. (1991) · Cell · doi:10.1016/0092-8674(81)90015-5 · Cited by 1,174
Penninckx, I. A. M. A., Eggermont, K., Terras, F. R. G., Thomma, B. P. H. J., Samblanx, G. W. D., Buchala, A. J., Métraux, J., Manners, J. M., & Broekaert, W. F. (1996) · The Plant Cell · doi:10.1105/tpc.8.12.2309 · Cited by 958
Nilin, J., Pestana, J. L. T., Ferreira, N. G. C., Loureiro, S., Costa-Lotufo, L. V., & Soares, A. M. V. M. (2012) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2012.06.107 · Cited by 956
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
Langer, T., Lu, C. Z., Echols, H., Flanagan, J. M., Hayer-Hartl, M. K., & Hartl, F. U. (1992) · Nature · doi:10.1038/356683a0 · Cited by 953
Alt, V., Bechert, T., Steinrücke, P., Wagener, M., SEIDEL, P. R., Dingeldein, E., Domann, E., & Schnettler, R. (2003) · Biomaterials · doi:10.1016/j.biomaterials.2003.10.078 · Cited by 952
Barboza, L. G. A., Lopes, C., Oliveira, P., Bessa, F., Otero, V., Henriques, B., Raimundo, J., Caetano, M., Vale, C., & Guilhermino, L. (2020) · Science of The Total Environment · doi:10.1016/j.scitotenv.2019.134625 · Cited by 951
Membrane fouling in membrane bioreactors—Characterisation, contradictions, cause and cures
Drews, A. (2010) · Journal of Membrane Science · doi:10.1016/j.memsci.2010.06.046 · Cited by 950
Field, J. M., Nikawa, J., Broek, D., MACDONALD, B. S., Rodgers, L., Wilson, I. A., Lerner, R. A., & Wigler, M. H. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.5.2159 · Cited by 949
Hämäläinen, M., Nieminen, R. M., Vuorela, P. M., Heinonen, M., & Moilanen, E. (2007) · Mediators of Inflammation · doi:10.1155/2007/45673 · Cited by 971
Jiang, M., & Zhang, J. (2001) · Plant and Cell Physiology · doi:10.1093/pcp/pce162 · Cited by 944
Zhang, Y., Liu, X., Wang, Y., Jiang, P., & Quek, S. Y. (2015) · Food Control · doi:10.1016/j.foodcont.2015.05.032 · Cited by 943
T lymphocytes from human atherosclerotic plaques recognize oxidized low density lipoprotein.
Stemme, S., Faber, B., Holm, J., Wiklund, O., Witztum, J. L., & Hansson, G. K. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.9.3893 · Cited by 943
[21] Thioredoxin and thioredoxin reductase
Holmgren, A., & Björnstedt, M. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)52023-6 · Cited by 941
Kase, H., Iwahashi, K., Nakanishi, S., Matsuda, Y., Yamada, K., Takahashi, M., Murakata, C., Sato, A., & Kaneko, M. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90293-2 · Cited by 939
Chen, S.-C., Wu, Y.-C., Mi, F., Lin, Y.-H., Yu, L.-C., & Sung, H. (2004) · Journal of Controlled Release · doi:10.1016/j.jconrel.2004.02.002 · Cited by 935
Godwin, A. K., Meister, A., O'Dwyer, P. J., Huang, C. S., Hamilton, T. C., & Anderson, M. E. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.3070 · Cited by 926
Burris, K. D., Molski, T. F. P., Xu, C., Ryan, E., Tottori, K., Kikuchi, T., Yocca, F. D., & Molinoff, P. B. (2002) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.102.033175 · Cited by 924
Isolation and characterization of angiogenin, an angiogenic protein from human carcinoma cells
Fett, J. W., Strydom, D. J., Lobb, R. R., Alderman, E. M., Bethune, J. L., Riordan, J. F., & Vallée, B. L. (1985) · Biochemistry · doi:10.1021/bi00341a030 · Cited by 923
Human tumor necrosis factor. Production, purification, and characterization.
Aggarwal, B. B., Kohr, W. J., Hass, P. E., Moffat, B., Spencer, S. A., Henzel, W. J., Bringman, T. S., Nedwin, G. E., Goeddel, D. V., & Harkins, R. N. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89560-6 · Cited by 917
Protein production and purification
Biologiques, A. E. F. D. M., Facility, O. P. P., Initiative, R. S. G., & SPINE2-Complexes (2008) · Nature Methods · doi:10.1038/nmeth.f.202 · Cited by 919
Roberts, A. B., Anzano, M. A., Lamb, L. C., Smith, J. M., & Sporn, M. B. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.9.5339 · Cited by 919
phot1 and phot2 mediate blue light regulation of stomatal opening
Kinoshita, T., Doi, M., Suetsugu, N., Kagawa, T., Wada, M., & Shimazaki, K.-I. (2001) · Nature · doi:10.1038/414656a · Cited by 899
Purification, molecular cloning, and expression of the mammalian sigma1-binding site.
Hanner, M., Moebius, F. F., Flandorfer, A., Knaus, H. G., Striessnig, J., Kempner, E. S., & Glossmann, H. H. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.8072 · Cited by 914
Advanced Glycosylation End Products in Patients with Diabetic Nephropathy
Makita, Z., Radoff, S., Rayfield, E. J., Yang, Z. H., Skolnik, E. Y., DELANEY, V. B., Friedman, E. A., Cerami, A., & Vlassara, H. (1991) · New England Journal of Medicine · doi:10.1056/nejm199109193251202 · Cited by 922
Hiesberger, T., Trommsdorff, M., Howell, B. W., Goffinet, A., Mumby, M. C., Cooper, J. A., & Herz, J. (1999) · Neuron · doi:10.1016/s0896-6273(00)80861-2 · Cited by 916
Ziche, M., Morbidelli, L., Choudhuri, R., Zhang, H. T., Donnini, S., Granger, H. J., & Bicknell, R. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119451 · Cited by 909
Embi, N., Rylatt, D. B., & Cohen, P. (1980) · PubMed · Cited by 911
Plant growth-promoting bacteria that decrease heavy metal toxicity in plants
Burd, G. I., Dixon, D. G., & Glick, B. R. (2000) · Canadian Journal of Microbiology · doi:10.1139/w99-143 · Cited by 903
Sugasawa, K., Ng, J. M. Y., Masutani, C., Iwai, S., van der Spek, P. J., Eker, A. P. M., Hanaoka, F., Bootsma, D., & Hoeijmakers, J. H. J. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80132-x · Cited by 899
Meerts, I. A. T. M. (2000) · Toxicological Sciences · doi:10.1093/toxsci/56.1.95 · Cited by 904
Sutherland, C., Leighton, I. A., & Cohen, P. (1993) · Biochemical Journal · doi:10.1042/bj2960015 · Cited by 903
Jiang, M. (2002) · Journal of Experimental Botany · doi:10.1093/jxb/erf090 · Cited by 898
Thymidine Phosphorylase Gene Mutations in MNGIE, a Human Mitochondrial Disorder
Nishino, I., Spinazzola, A., & Hirano, M. (1999) · Science · doi:10.1126/science.283.5402.689 · Cited by 899
DeCaprio, J. A., Ludlow, J. W., Lynch, D., Furukawa, Y., Griffin, J., Piwnica-Worms, H., Huang, C.-M., & Livingston, D. M. (1989) · Cell · doi:10.1016/0092-8674(89)90507-2 · Cited by 897
Delayed leaf senescence induces extreme drought tolerance in a flowering plant
Rivero, R. M., Kojima, M., Gepstein, A., Sakakibara, H., Mittler, R., Gepstein, S., & Blumwald, E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709453104 · Cited by 896
MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
Maki, H., & Sekiguchi, M. (1992) · Nature · doi:10.1038/355273a0 · Cited by 901
Interleukin-6 induces cellular insulin resistance in hepatocytes.
Senn, J. J., Klover, P. J., Nowak, I. A., & Mooney, R. A. (2002) · Diabetes · doi:10.2337/diabetes.51.12.3391 · Cited by 883
Deregulation of Glucose Transporter 1 and Glycolytic Gene Expression by c-Myc
Osthus, R. C., Shim, H., Kim, S., Li, Q., Reddy, R., Mukherjee, M., Xu, Y., Wonsey, D. R., Lee, L. A., & Dang, C. V. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000023200 · Cited by 876
Browne, S. E., Bowling, A. C., Macgarvey, U., Baik, M. J., Berger, S. C., Muquit, M. M. K., Bird, E. D., & Beal, M. F. (1997) · Annals of Neurology · doi:10.1002/ana.410410514 · Cited by 885
Reppert, S. M., Godson, C., Mahle, C. D., Weaver, D. R., Slaugenhaupt, S. A., & Gusella, J. F. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.19.8734 · Cited by 882
Posas, F., Wurgler‐Murphy, S. M., Maeda, T., Witten, E. A., Thai, T. C., & Saito, H. (1996) · Cell · doi:10.1016/s0092-8674(00)80162-2 · Cited by 881
Agonistic properties of cannabidiol at 5-HT1a receptors
Russo, E. B., Burnett, A., Hall, B., & Parker, K. K. (2005) · Neurochemical Research · doi:10.1007/s11064-005-6978-1 · Cited by 878
Ungerer, M., Böhm, M., Elce, J. S., Erdmann, E., & Lohse, M. J. (1993) · Circulation · doi:10.1161/01.cir.87.2.454 · Cited by 878
Ishiguro, S., Kawai-Oda, A., Ueda, J., Nishida, I., & Okada, K. (2001) · The Plant Cell · doi:10.1105/tpc.010192 · Cited by 878
Zhu, Z., Wei, G., Li, J., Qian, Q., & Yu, J. (2004) · Plant Science · doi:10.1016/j.plantsci.2004.04.020 · Cited by 911
Traverse, S., Gómez, N., Paterson, H., Marshall, C. J., & Cohen, P. (1992) · Biochemical Journal · doi:10.1042/bj2880351 · Cited by 874
Transcriptional Regulator of Oxidative Stress-Inducible Genes: Direct Activation by Oxidation
Storz, G., Tartaglia, L. A., & Ames, B. N. (1990) · Science · doi:10.1126/science.2183352 · Cited by 864
Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
de Ruyter, P. G. G. A., Kuipers, O. P., & de Vos, W. M. (1996) · Applied and Environmental Microbiology · doi:10.1128/aem.62.10.3662-3667.1996 · Cited by 859
Nuclear localization of unoccupied oestrogen receptors
Welshons, W. V., Lieberman, M. E., & Gorski, J. (1984) · Nature · doi:10.1038/307747a0 · Cited by 870
Vancanneyt, G., Schmidt, R., O’Connor-Sánchez, A., Willmitzer, L., & Rocha‐Sosa, M. (1990) · Molecular and General Genetics MGG · doi:10.1007/bf00260489 · Cited by 866
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