Differential distribution of follistatin isoforms: application of a new FS315-specific immunoassay

Activin-Binding Protein from Rat Ovary Is Follistatin

Nakamura, T., Takio, K., Eto, Y., Shibai, H., Titani, K., & Sugino, H. (1990) · Science · doi:10.1126/science.2106159 · Cited by 883 · see citing works

Multiple defects and perinatal death in mice deficient in follistatin

Matzuk, M. M., Lu, N., Vogel, H. S., Sellheyer, K., Roop, D. R., & Bradley, A. (1995) · Nature · doi:10.1038/374360a0 · Cited by 584 · see citing works

Isolation and partial characterization of follistatin: a single-chain Mr 35,000 monomeric protein that inhibits the release of follicle-stimulating hormone.

Ueno, N., LING, N. C., Ying, S. Y., Esch, F. S., Shimasaki, S., & Guillemin, R. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8282 · Cited by 445 · see citing works

The isolation of polypeptides with FSH suppressing activity from bovine follicular fluid which are structurally different to inhibin

Robertson, D. M., Klein, R., de Vos, F. L., McLachlan, R. I., Wettenhall, R. E. H., Hearn, M. T. W., Burger, H., & de Kretser, D. M. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)90430-x · Cited by 345 · see citing works

Activins, Inhibins, and Follistatins: From Endocrinology to Signaling. A Paradigm for the New Millennium

Welt, C. K., Sidis, Y., Keutmann, H. T., & Schneyer, A. L. (2002) · Experimental Biology and Medicine · doi:10.1177/153537020222700905 · Cited by 324 · see citing works

Primary structure of the human follistatin precursor and its genomic organization

Shimasaki, S., Koga, M., Esch, F., Cooksey, K., Mercado, M., Koba, A., Ueno, N., Ying, S. Y., Ling, N., & Guillemin, R. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4218 · Cited by 232 · see citing works

Molecular heterogeneity of follistatin, an activin-binding protein. Higher affinity of the carboxyl-terminal truncated forms for heparan sulfate proteoglycans on the ovarian granulosa cell

Sugino, K., Kurosawa, N., Nakamura, T., Takio, K., Shimasaki, S., LING, N. C., Titani, K., & Sugino, H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82296-7 · Cited by 228 · see citing works

Follistatin, an activin-binding protein, associates with heparan sulfate chains of proteoglycans on follicular granulosa cells.

Nakamura, T., Sugino, K., Titani, K., & Sugino, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55015-8 · Cited by 166 · see citing works

Human Follistatin-Related Protein: A Structural Homologue of Follistatin with Nuclear Localization

Tortoriello, D. V., Sidis, Y., Holtzman, D. A., Holmes, W. E., & Schneyer, A. L. (2001) · Endocrinology · doi:10.1210/endo.142.8.8319 · Cited by 152 · see citing works

Rat follistatin: Gonadal and extragonadal expression and evidence for alternative splicing

Michel, U., Albiston, A. L., & Findlay, J. K. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)81072-1 · Cited by 150 · see citing works

Characterization of unique binding kinetics of follistatin and activin or inhibin in serum

Schneyer, A. L., Rzucidlo, D. A., Sluss, P. M., & Crowley, W. F. (1994) · Endocrinology · doi:10.1210/endo.135.2.8033815 · Cited by 143 · see citing works

Dynamic Changes in the Intrafollicular Inhibin/Activin/Follistatin Axis during Human Follicular Development: Relationship to Circulating Hormone Concentrations

Schneyer, A. L., Fujiwara, T., Fox, J. H., Welt, C. K., Adams, J., Lambert-Messerlian, G. M., & Taylor, A. E. (2000) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.85.9.6767 · Cited by 119 · see citing works

Identification and characterization of binding proteins for inhibin and activin in human serum and follicular fluids

KRUMMEN, L. A., Woodruff, T. K., DeGuzman, G. G., Cox, E. T., Baly, D. L., Mann, E. A., Garg, S., Wong, W. L., Cossum, P. A., & Mather, J. P. (1993) · Endocrinology · doi:10.1210/endo.132.1.7678220 · Cited by 118 · see citing works

Evidence for activin A and follistatin involvement in the systemic inflammatory response

Phillips, D. J., Jones, K. L., Scheerlinck, J. Y., Hedger, M. P., & de Kretser, D. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(01)00516-0 · Cited by 108 · see citing works

Alpha 2-macroglobulin is a binding protein of inhibin and activin.

Vaughan, J. M., & Vale, W. (1993) · Endocrinology · doi:10.1210/endo.132.5.7682939 · Cited by 83 · see citing works

Control of pelage hair follicle development and cycling by complex interactions between follistatin and activin

Nakamura, M., Matzuk, M. M., Gerstmayer, B., Bosio, A., Lauster, R., Miyachi, Y., Werner, S., & Paus, R. (2003) · The FASEB Journal · doi:10.1096/fj.02-0247fje · Cited by 81 · see citing works

Development, validation and application of an ultra-sensitive two-site enzyme immunoassay for human follistatin

Evans, L., Muttukrishna, S., & Groome, N. (1998) · Journal of Endocrinology · doi:10.1677/joe.0.1560275 · Cited by 77 · see citing works

Differential Binding and Neutralization of Activins A and B by Follistatin and Follistatin Like-3 (FSTL-3/FSRP/FLRG)

Schneyer, A. L., Schoen, A., Quigg, A., & Sidis, Y. (2003) · Endocrinology · doi:10.1210/en.2002-0203 · Cited by 71 · see citing works

Follistatin-Related Protein and Follistatin Differentially Neutralize Endogenous vs. Exogenous Activin

Sidis, Y., Tortoriello, D. V., Holmes, W. E., Pan, Y., Keutmann, H. T., & Schneyer, A. L. (2002) · Endocrinology · doi:10.1210/endo.143.5.8805 · Cited by 67 · see citing works

A Two-Site Chemiluminescent Assay for Activin-Free Follistatin Reveals That Most Follistatin Circulating in Men and Normal Cycling Women Is in an Activin-Bound State1

McConnell, D. S., Wang, Q., Sluss, P. M., Bolf, N., Khoury, R. H., Schneyer, A. L., MIDGLEY, A. R., Reame, N. E., Crowley, W. F., & Padmanabhan, V. (1998) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.83.3.4651 · Cited by 65 · see citing works

Serum follistatin levels in women: evidence against an endocrine function of ovarian follistatin

Khoury, R. H., Wang, Q. F., Crowley, W. F., Hall, J. E., Schneyer, A. L., Toth, T. L., MIDGLEY, A. R., & Sluss, P. M. (1995) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.80.4.7714112 · Cited by 63 · see citing works

Follistatin-activin complexes in human serum and follicular fluid differ immunologically and biochemically

Schneyer, A. L., Hall, H. A., Lambert-Messerlian, G. M., Wang, Q. F., Sluss, P., & Crowley, W. F. (1996) · Endocrinology · doi:10.1210/endo.137.1.8536619 · Cited by 59 · see citing works

Localization of the heparin binding site of follistatin

Inouye, S., LING, N. C., & Shimasaki, S. (1992) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(92)90094-m · Cited by 52 · see citing works

Production of follistatin in porcine endothelial cells: differential regulation by bacterial compounds and the synthetic glucocorticoid RU 28362

Michel, U., Schneider, O., Kirchhof, C., Meisel, S., Av, S., Wiltfang, J., & Rieckmann, P. (1996) · Endocrinology · doi:10.1210/endo.137.11.8895365 · Cited by 49 · see citing works

Activin-binding proteins in human serum and follicular fluid.

Schneyer, A. L., O'Neil, D. A., & Crowley, W. F. (1992) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.74.6.1592877 · Cited by 41 · see citing works

Analysis of Human Follistatin Structure: Identification of Two Discontinuous N-Terminal Sequences Coding for Activin A Binding and Structural Consequences of Activin Binding to Native Proteins*

Qifa, W., Keutmann, H. T., Schneyer, A. L., & Sluss, P. M. (2000) · Endocrinology · doi:10.1210/endo.141.9.7675 · Cited by 40 · see citing works

Analysis of follicular fluid hormone concentrations and granulosa cell mRNA levels for the inhibin-activin-follistatin system: relation to oocyte and embryo characteristics

Fujiwara, T., Lambert-Messerlian, G. M., Sidis, Y., Leykin, L., Isaacson, K., Toth, T. L., & Schneyer, A. L. (2000) · Fertility and Sterility · doi:10.1016/s0015-0282(00)00652-x · Cited by 37 · see citing works

Differential Response to Exogenous and Endogenous Activin in a Human Ovarian Teratocarcinoma-Derived Cell Line (PA-1): Regulation by Cell Surface Follistatin*

Delbaere, A., Sidis, Y., & Schneyer, A. L. (1999) · Endocrinology · doi:10.1210/endo.140.6.6824 · Cited by 31 · see citing works

A two-site monoclonal antibody immunoradiometric assay for human follistatin: secretion by a human ovarian teratocarcinoma-derived cell line (PA-1)

Wang, Q. F., Khoury, R. H., Smith, P. C., McConnell, D. S., Padmanahban, V., MIDGLEY, A. R., Schneyer, A. L., Crowley, W. F., & Sluss, P. M. (1996) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.81.4.8636347 · Cited by 26 · see citing works

Isolation of Drosophila Activin and Follistatin cDNAs using novel MACH amplification protocols

Haerry, T. E., & O’Connor, M. B. (2002) · Gene · doi:10.1016/s0378-1119(02)00463-8 · Cited by 17 · see citing works

Follistatin Physiology and Potential Mechanisms of Action in the Human

Schneyer, A. L., Wang, Q. F., Weiss, J., Boepple, P. A., Hall, J. E., Khoury, R. H., Taylor, A. E., Pralong, F. P., Sluss, P., & Crowley, W. F. (1997) · Springer eBooks · doi:10.1007/978-1-4612-1874-6_3 · Cited by 9 · see citing works

Activins and Inhibins: Roles in Development, Physiology, and Disease

Namwanje, M., & Brown, C. W. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a021881 · Cited by 294 · see citing works

The Structure of the Follistatin:Activin Complex Reveals Antagonism of Both Type I and Type II Receptor Binding

Thompson, T. B., Lerch, T. F., Cook, R. W., Woodruff, T. K., & Jardetzky, T. S. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.09.008 · Cited by 288 · see citing works

The role of hepatokines in NAFLD

Stefan, N., Schick, F., Birkenfeld, A. L., Häring, H., & White, M. F. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.01.006 · Cited by 282 · see citing works

Hepatokines and metabolism: Deciphering communication from the liver

Jensen-Cody, S. O., & Potthoff, M. J. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101138 · Cited by 252 · see citing works

The biology of activin: recent advances in structure, regulation and function

Xia, Y. Y., & Schneyer, A. L. (2009) · Journal of Endocrinology · doi:10.1677/joe-08-0549 · Cited by 233 · see citing works

Biological activity of follistatin isoforms and follistatin-like-3 is dependent on differential cell surface binding and specificity for activin, myostatin, and bone morphogenetic proteins

Sidis, Y., Mukherjee, A., Keutmann, H., Delbaere, A., Sadatsuki, M., & Schneyer, A. (2006) · Endocrinology · doi:10.1210/en.2006-0089 · Cited by 211 · see citing works

Activin A in Mammalian Physiology

Bloise, E., Ciarmela, P., Cruz, C. D., Luisi, S. V., Petraglia, F., & dos Reis, F. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00002.2018 · Cited by 196 · see citing works

Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease

Rodino‐Klapac, L. R., Haidet, A. M., Kota, J., Handy, C., Kaspar, B. K., & Mendell, J. R. (2009) · Muscle & Nerve · doi:10.1002/mus.21244 · Cited by 194 · see citing works

Inhibin at 90: From Discovery to Clinical Application, a Historical Review

Makanji, Y., Zhu, J., Mishra, R. K., Holmquist, C., Wong, W. P. S., Schwartz, N. B., Mayo, K. E., & Woodruff, T. K. (2014) · Endocrine Reviews · doi:10.1210/er.2014-1003 · Cited by 187 · see citing works

Follistatin Gene Delivery Enhances Muscle Growth and Strength in Nonhuman Primates

Kota, J., Handy, C. R., Haidet, A. M., Montgomery, C. L., Eagle, A., Rodino‐Klapac, L. R., Tucker, D., Shilling, C. J., Therlfall, W. R., Walker, C. M., et al. (2009) · Science Translational Medicine · doi:10.1126/scitranslmed.3000112 · Cited by 166 · see citing works

The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding

Cash, J. N., Rejon, C. A., McPherron, A. C., Bernard, D. J., & Thompson, T. B. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.205 · Cited by 159 · see citing works

FSTL3 deletion reveals roles for TGF-β family ligands in glucose and fat homeostasis in adults

Mukherjee, A., Sidis, Y., Mahan, A. L., Raher, M. J., Xia, Y. Y., Rosen, E. D., Bloch, K. D., Thomas, M. K., & Schneyer, A. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607966104 · Cited by 157 · see citing works

Intertwining of Activin A and TGFβ Signaling: Dual Roles in Cancer Progression and Cancer Cell Invasion

Loomans-Kropp, H. A., & Andl, C. D. (2014) · Cancers · doi:10.3390/cancers7010070 · Cited by 148 · see citing works

The structural basis of TGF-β, bone morphogenetic protein, and activin ligand binding

Lin, S. J., Lerch, T. F., Cook, R. W., Jardetzky, T. S., & Woodruff, T. K. (2006) · Reproduction · doi:10.1530/rep.1.01072 · Cited by 138 · see citing works

Pituitary actions of ligands of the TGF-β family: activins and inhibins

Bilezikjian, L. M., Blount, A. L., Donaldson, C., & Vale, W. (2006) · Reproduction · doi:10.1530/rep.1.01073 · Cited by 128 · see citing works

Circulating follistatin is liver-derived and regulated by the glucagon-to-insulin ratio

Hansen, J. S., Rutti, S., Arous, C., Clemmesen, J. O., Secher, N. H., Drescher, A., Gonelle-Gispert, C., Halban, P. A., Pedersen, B. K., Weigert, C., et al. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-3668 · Cited by 125 · see citing works

Inactivating hepatic follistatin alleviates hyperglycemia

Tao, R., Wang, C., Stöhr, O., Qiu, W., Hu, Y., Miao, J., Dong, X. C., Leng, S., Stefater, M., Stylopoulos, N., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0048-0 · Cited by 104 · see citing works

Myostatin Inhibitors: Panacea or Predicament for Musculoskeletal Disorders?

Suh, J., & Lee, Y. (2020) · Journal of Bone Metabolism · doi:10.11005/jbm.2020.27.3.151 · Cited by 86 · see citing works

Effect of Various Exercise Regimens on Selected Exercise-Induced Cytokines in Healthy People

Domin, R., Dadej, D., Pytka, M., Zybek-Kocik, A., Ruchała, M., & Guzik, P. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph18031261 · Cited by 79 · see citing works

Advances in research on pharmacotherapy of sarcopenia

Feike, Y., Liu, Z., & Chen, W. (2021) · Aging Medicine · doi:10.1002/agm2.12168 · Cited by 67 · see citing works

Structural and Biophysical Coupling of Heparin and Activin Binding to Follistatin Isoform Functions

Lerch, T. F., Shimasaki, S., Woodruff, T. K., & Jardetzky, T. S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700737200 · Cited by 66 · see citing works

Circulating follistatin in relation to energy metabolism

Hansen, J. S., & Plomgaard, P. (2016) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2016.06.002 · Cited by 62 · see citing works

The Structure of FSTL3·Activin A Complex

Stamler, R., Keutmann, H. T., Sidis, Y., Kattamuri, C., Schneyer, A. L., & Thompson, T. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801266200 · Cited by 63 · see citing works

Follistatin and follistatin like-3 differentially regulate adiposity and glucose homeostasis

Brown, M. L., Bonomi, L., Ungerleider, N., Zina, J., Kimura, F., Mukherjee, A., Sidis, Y., & Schneyer, A. (2011) · Obesity · doi:10.1038/oby.2011.97 · Cited by 55 · see citing works

Follistatin-based ligand trap ACE-083 induces localized hypertrophy of skeletal muscle with functional improvement in models of neuromuscular disease

Pearsall, R. S., Davies, M. V., Cannell, M., Li, J., Widrick, J. J., Mulivor, A. W., Wallner, S., Troy, M., Spaits, M. S., Liharska, K., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-47818-w · Cited by 53 · see citing works

Follistatin Regulates Germ Cell Nest Breakdown and Primordial Follicle Formation

Kimura, F., Bonomi, L. M., & Schneyer, A. L. (2010) · Endocrinology · doi:10.1210/en.2010-0950 · Cited by 52 · see citing works

High serum follistatin levels in women with ovarian endometriosis

Florio, P., Reis, F. M., Torres, P. B., Calonaci, F., Abrao, M. S., Nascimento, L. L., Franchini, M., Cianferoni, L., & Petraglia, F. (2009) · Human Reproduction · doi:10.1093/humrep/dep195 · Cited by 51 · see citing works

Clinical and therapeutic implications of follistatin in solid tumours

SHI, L., RESAUL, J., OWEN, S., YE, L., & JIANG, W. G. (2016) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20005 · Cited by 47 · see citing works

Female Infertility and Disrupted Angiogenesis Are Actions of Specific Follistatin Isoforms

Lin, S.-Y., Craythorn, R. G., O’Connor, A. E., Matzuk, M. M., Girling, J. E., Morrison, J. R., & de Kretser, D. M. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0529 · Cited by 46 · see citing works

The Follistatin-288 Isoform Alone Is Sufficient for Survival But Not for Normal Fertility in Mice

Kimura, F., Sidis, Y., Bonomi, L. M., Xia, Y. Y., & Schneyer, A. L. (2009) · Endocrinology · doi:10.1210/en.2009-1176 · Cited by 42 · see citing works

Activins and Related Proteins in the Establishment of Pregnancy

Florio, P., Gabbanini, M., Borges, L. E., Bonaccorsi, L., Pinzauti, S., dos Reis, F. M., Torres, P. B., Rago, G., Litta, P., & Petraglia, F. (2010) · Reproductive Sciences · doi:10.1177/1933719109353205 · Cited by 38 · see citing works

Follistatin as potential therapeutic target in prostate cancer

Sepporta, M. V., Tumminello, F. M., Flandina, C., Crescimanno, M., Giammanco, M., Guardia, M. L., Majo, D. D., & Leto, G. (2013) · Targeted Oncology · doi:10.1007/s11523-013-0268-7 · Cited by 30 · see citing works

Increased Expression of Follistatin in Breast Cancer Reduces Invasiveness and Clinically Correlates with Better Survival

Zabkiewicz, C., Resaul, J., Hargest, R., Jiang, W. G., & Ye, L. (2017) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20035 · Cited by 30 · see citing works

Follistatin-288-Fc Fusion Protein Promotes Localized Growth of Skeletal Muscle

Castonguay, R., Lachey, J. L., Wallner, S., Strand, J., Liharska, K., Watanabe, A. E., Cannell, M., Davies, M. V., Sako, D., Troy, M., et al. (2018) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.118.252304 · Cited by 29 · see citing works

Follistatin Effects in Migration, Vascularization, and Osteogenesis in vitro and Bone Repair in vivo

Fahmy‐Garcia, S., Farrell, E., Witte‐Bouma, J., den Berge, I. J. R.-V., Muñoz, M. S., Mumcuoglu, D., Walles, H., Kluijtmans, S. G. J. M., van der Eerden, B. C. J., van Osch, G. J. V. M., et al. (2019) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00038 · Cited by 25 · see citing works

Systemic administration of Follistatin288 increases muscle mass and reduces fat accumulation in mice

Gangopadhyay, S. S. (2013) · Scientific Reports · doi:10.1038/srep02441 · Cited by 25 · see citing works

Combinatory effects of siRNA-induced myostatin inhibition and exercise on skeletal muscle homeostasis and body composition

Mosler, S., Relizani, K., Mouisel, É., Amthor, H., & Diel, P. R. (2014) · Physiological Reports · doi:10.1002/phy2.262 · Cited by 24 · see citing works

The influence of follistatin on mechanical properties of bone tissue in growing mice with overexpression of follistatin

Gajos-Michniewicz, A., Pawłowska, E., Ochędalski, T., & Piastowska‐Ciesielska, A. W. (2012) · Journal of Bone and Mineral Metabolism · doi:10.1007/s00774-011-0347-8 · Cited by 22 · see citing works

Follistatin Is an Early Player in Rainbow Trout Ovarian Differentiation and Is Both Colocalized with Aromatase and Regulated by the Wnt Pathway

Nicol, B., Yano, A., Jouanno, E., Guérin, A., Fostier, A., & Guiguen, Y. (2013) · Sexual Development · doi:10.1159/000350687 · Cited by 21 · see citing works

Follistatin N terminus differentially regulates muscle size and fat in vivo

Zheng, H., Qiao, C., Tang, R., Li, J., Bulaklak, K., Huang, Z., Zhao, C., Dai, Y. L., Li, J., & Xiao, X. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.135 · Cited by 20 · see citing works

Bone Geometry Is Altered by Follistatin‐Induced Muscle Growth in Young Adult Male Mice

Chan, A. S. M., McGregor, N. E., Poulton, I. J., Hardee, J. P., Cho, H., Martin, T. J., Gregorevic, P., Sims, N. A., & Lynch, G. S. (2021) · JBMR Plus · doi:10.1002/jbm4.10477 · Cited by 19 · see citing works

Imbalance of Amniotic Fluid Activin-A and Follistatin in Intraamniotic Infection, Inflammation, and Preterm Birth

Hardy, J. T., Buhimschi, I. A., McCarthy, M. E., Zhao, G., Laky, C. A., Shook, L. L., & Buhimschi, C. S. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-4147 · Cited by 17 · see citing works

The Effects of Transforming Growth Factor-β2 on the Expression of Follistatin and Activin A in Normal and Glaucomatous Human Trabecular Meshwork Cells and Tissues

Fitzgerald, A. M., Benz, C. L., Clark, A. F., & Wordinger, R. J. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-10292 · Cited by 17 · see citing works

The transgenic expression of human follistatin-344 increases skeletal muscle mass in pigs

Chang, F., Fang, R., Wang, M., Zhao, X., Chang, W., Zhang, Z., Li, N., & Meng, Q. (2016) · Transgenic Research · doi:10.1007/s11248-016-9985-x · Cited by 16 · see citing works

Drosophila Follistatin exhibits unique structural modifications and interacts with several TGF-β family members

Bickel, D., Shah, R., Gesualdi, S. C., & Haerry, T. E. (2007) · Mechanisms of Development · doi:10.1016/j.mod.2007.09.013 · Cited by 16 · see citing works

Activin-related proteins in bovine mammary gland: Localization and differential expression during gestational development and differentiation

Bloise, E., Cassali, G. D., Ferreira, M. C. F., Ciarmela, P., Petraglia, F., & dos Reis, F. M. (2010) · Journal of Dairy Science · doi:10.3168/jds.jds.2009-2981 · Cited by 15 · see citing works

Protein Engineering on Human Recombinant Follistatin: Enhancing Pharmacokinetic Characteristics for Therapeutic Application

Shen, C., Iskenderian, A., Lundberg, D. M., He, T., Palmieri, K. J., Crooker, R., Deng, Q., Traylor, M. J., Gu, S., Rong, H., et al. (2018) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.118.248195 · Cited by 15 · see citing works

Hepatic follistatin increases basal metabolic rate and attenuates diet-induced obesity during hepatic insulin resistance

Tao, R., Stöhr, O., Wang, C., Qiu, W., Copps, K. D., & White, M. F. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101703 · Cited by 14 · see citing works

Detection of follistatin‐based inhibitors of the TGF‐β signaling pathways in serum/plasma by means of LC‐HRMS/MS and Western blotting

Walpurgis, K., Weigand, T., Knoop, A., Thomas, A., Reichel, C., Dellanna, F., & Thevis, M. (2020) · Drug Testing and Analysis · doi:10.1002/dta.2925 · Cited by 14 · see citing works

Too Many Follistatins: Racing Inside and Getting Out of the Cell

Kumar, T. R. (2005) · Endocrinology · doi:10.1210/en.2005-1210 · Cited by 13 · see citing works

Anti‐Müllerian hormone signaling is influenced by Follistatin 288, but not 14 other transforming growth factor beta superfamily regulators

Kawagishi, Y., Pankhurst, M. W., Nakatani, Y., & McLennan, I. S. (2017) · Molecular Reproduction and Development · doi:10.1002/mrd.22828 · Cited by 11 · see citing works

The Role of TGF-β, Activin and Follistatin in Inflammatory Bowel Disease

Esfahani, N. H., & Day, A. S. (2023) · Gastrointestinal Disorders · doi:10.3390/gidisord5020015 · Cited by 10 · see citing works

Detection of black market follistatin 344

Reichel, C., Gmeiner, G., & Thevis, M. (2019) · Drug Testing and Analysis · doi:10.1002/dta.2741 · Cited by 9 · see citing works

Activin-inhibitory action on lactotrophs is decreased in lactotroph hyperplasia

Faraoni, E. Y., Abeledo-Machado, A., Pérez, P. A., López, C. A. M., Camilletti, M. A., Peña‐Zanoni, M., Rulli, S. B., Gutiérrez, S., & Dı́az-Torga, G. (2019) · Journal of Endocrinology · doi:10.1530/joe-19-0326 · Cited by 8 · see citing works

Inhibition of DNA methylation increases follistatin expression and secretion in the human adrenocortical cell line NCI-H295R

Utriainen, P., Liu, J., Kuulasmaa, T., & Voutilainen, R. (2006) · Journal of Endocrinology · doi:10.1677/joe.1.06392 · Cited by 8 · see citing works

Production of bioactive chicken (Gallus gallus) follistatin-type proteins in E. coli

Lee, S. B., Park, S., & Kim, Y. (2015) · AMB Express · doi:10.1186/s13568-015-0142-3 · Cited by 8 · see citing works

The Reign of Follistatin in Tumors and Their Microenvironment: Implications for Drug Resistance

Sosa, J., Oyelakin, A., & Sinha, S. (2024) · Biology · doi:10.3390/biology13020130 · Cited by 7 · see citing works

Fructose and follistatin potentiate acute MASLD during complete hepatic insulin resistance

Tao, R., Stöhr, O., Tok, O., Andrés-Hernando, A., Qiu, W., He, B., Wang, C., Grøntved, L., Burant, C., Hui, S. T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66296-5 · Cited by 6 · see citing works

FSTL3-Neutralizing Antibodies Enhance Glucose-Responsive Insulin Secretion in Dysfunctional Male Mouse and Human Islets

Brown, M., Lopez, A., Meyer, N., Richter, A., & Thompson, T. B. (2021) · Endocrinology · doi:10.1210/endocr/bqab019 · Cited by 6 · see citing works

Activin Actions in Adipocytes

Ongaro, L., & Bernard, D. J. (2025) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaf233 · Cited by 5 · see citing works

Sarcopenia in chronic obstructive pulmonary disease: mechanisms, diagnosis, and management strategies

Khan, M. H., Fatima, M., Adnan, A. B., Jawaid, A., Hassan, S. M., Talal, M., Rahim, S., Mughal, Z. U. N., Patel, A. O., & Singh, A. K. (2025) · Annals of Medicine and Surgery · doi:10.1097/ms9.0000000000003584 · Cited by 6 · see citing works

Inhibin, Activin, and Follistatin in Ovarian Physiology

Welt, C. K., & Schneyer, A. L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-813209-8.00006-6 · Cited by 5 · see citing works

Screening and confirmation of recombinant human follistatin in equine plasma for doping control purposes

Wong, K., Cheung, H. W., Choi, Y., To, N. S., Wan, T. S. M., & Ho, E. N. M. (2023) · Drug Testing and Analysis · doi:10.1002/dta.3540 · Cited by 4 · see citing works

Circulating plasma follistatin follows a 24-hour rhythm in healthy young males

Zilstorff, D. B., Sennels, H. P., Jørgensen, H. L., Albrechtsen, N. J. W., & Richter, M. M. (2026) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgag121 · Cited by 1 · see citing works

Central serous chorioretinopathy associated with high-dose follistatin-344: a retrospective case series

Dağ, U., Çağlayan, M., Öncül, H., & Alakuş, M. F. (2020) · International Ophthalmology · doi:10.1007/s10792-020-01501-6 · Cited by 2 · see citing works

Cloning of Japanese Quail (Coturnix japonica) Follistatin and Production of Bioactive Quail Follistatin288 in Escherichia coli

Maaeni, Y. M. A., Lee, S. B., Choi, D. H., Mozdziak, P. E., & Kim, Y. (2017) · International Journal of Poultry Science · doi:10.3923/ijps.2018.8.21 · Cited by 1 · see citing works

Folistatina, resistencia a la insulina y composición corporal en adultos colombianos

Toloza, F. J. K., Ricardo-Silgado, M. L., Mantilla-Rivas, J. O., Morales-Álvarez, M. C., Pérez-Matos, M. C., Pinzón-Cortés, J. A., Pérez-Mayorga, M., & Mendivil, C. O. (2018) · Revista Colombiana de Endocrinología Diabetes & Metabolismo · doi:10.53853/encr.5.1.336 · Cited by 1 · see citing works

CANDIDATE GENES ASSOCIATED WITH POLYCYSTIC OVARY SYNDROME IN ASIAN POPULATIONS: A RESEARCH REVIEW

Vg, A. (2016) · Asian Journal of Pharmaceutical and Clinical Research · doi:10.22159/ajpcr.2016.v9i5.12432 · Cited by 1 · see citing works

Feedback regulation loop between bone morphogenetic proteins and their antagonists in prostate cancer and the implication in bone metastasis

Resaul, J. (2018) · ORCA Online Research @Cardiff (Cardiff University)

Molecular Characterization of the Follistatin (FST) Gene in Quail and its Modulation through Natural Agonists

Hassan, F., Aftab, S., Rehman, M. S.-U., Arif, S., Safdar, M., Ahmed, S., Ahmad, K., Cerbo, A. D., Azzam, M. M., & Alagawany, M. M. (2025) · Brazilian Journal of Poultry Science · doi:10.1590/1806-9061-2024-2004

Implication des Bone Morphogenetic Proteins (BMPs) hypophysaires dans la régulation de la synthèse et de la libération de l'hormone folliculo-stimulante (FSH) ?

Sallon, C. (2010) · theses.fr (ABES) · doi:10.70675/2ccb2882z4155z4240zb98cz58eef2b4158d

Molecular heterogeneity of follistatin, an activin-binding protein. Higher affinity of the carboxyl-terminal truncated forms for heparan sulfate proteoglycans on the ovarian granulosa cell

Sugino, K., Kurosawa, N., Nakamura, T., Takio, K., Shimasaki, S., LING, N. C., Titani, K., & Sugino, H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82296-7 · Cited by 228 · see citing works

Comparison of bioactivities, binding properties and intrafollicular levels of bovine follistatins

Glister, C., Sunderland, S. J., Boland, M. P., Ireland, J. J., & Knight, P. G. (2015) · Reproduction · doi:10.1530/rep-15-0086 · Cited by 3 · see citing works

Follistatin-activin complexes in human serum and follicular fluid differ immunologically and biochemically

Schneyer, A. L., Hall, H. A., Lambert-Messerlian, G. M., Wang, Q. F., Sluss, P., & Crowley, W. F. (1996) · Endocrinology · doi:10.1210/endo.137.1.8536619 · Cited by 59 · see citing works

Biological activity of follistatin isoforms and follistatin-like-3 is dependent on differential cell surface binding and specificity for activin, myostatin, and bone morphogenetic proteins

Sidis, Y., Mukherjee, A., Keutmann, H., Delbaere, A., Sadatsuki, M., & Schneyer, A. (2006) · Endocrinology · doi:10.1210/en.2006-0089 · Cited by 211 · see citing works

Follistatin and its role as an activin-binding protein.

Sugino, H., Sugino, K., Hashimoto, O., Shoji, H., & Nakamura, T. (1997) · PubMed · Cited by 61 · see citing works