Kinases as targets for chemical modulators: Structural aspects and their role in spermatogenesis

References

• Russell L. Movement of spermatocytes from the basal to the adluminal compartment of the rat testis. Am J Anat 1977; 148:313-28; PMID:857632
   PubMedGoogle Scholar
• Wong CH, Cheng CY. Mitogen-activated protein kinases, adherens junction dynamics, and spermatogenesis: a review of recent data. Dev Biol 2005; 286:1-15; PMID:16153630; http://dx.doi.org/10.1016/j.ydbio.2005.08.001
   PubMed Web of Science ®Google Scholar
• Almog T, Naor Z. Mitogen activated protein kinases (MAPKs) as regulators of spermatogenesis and spermatozoa functions. Mol Cell Endocrinol 2008; 282:39-44; PMID:18177996; http://dx.doi.org/10.1016/j.mce.2007.11.011
   PubMed Web of Science ®Google Scholar
• Li MW, Mruk DD, Cheng CY. Mitogen-activated protein kinases in male reproductive function. Trends Mol Med 2009; 15:159-68; PMID:19303360; http://dx.doi.org/10.1016/j.molmed.2009.02.002
   PubMed Web of Science ®Google Scholar
• Almog T, Naor Z. The role of mitogen activated protein kinase (MAPK) in sperm functions. Mol Cell Endocrinol 2010; 314:239-43; PMID:19467295; http://dx.doi.org/10.1016/j.mce.2009.05.009
   PubMed Web of Science ®Google Scholar
• Ijiri TW, Mahbub Hasan AK, Sato K. Protein-tyrosine kinase signaling in the biological functions associated with sperm. J Signal Transduct 2012; 2012:181560; PMID:23209895; http://dx.doi.org/10.1155/2012/181560
   PubMedGoogle Scholar
• Page ST, Amory JK, Bremner WJ. Advances in male contraception. Endocr Rev 2008; 29:465-93; PMID:18436704; http://dx.doi.org/10.1210/er.2007-0041
   PubMed Web of Science ®Google Scholar
• Wang C, Swerdloff RS. Hormonal approaches to male contraception. Curr Opin Urol 2010; 20:520-4; PMID:20808223; http://dx.doi.org/10.1097/MOU.0b013e32833f1b4a
   PubMed Web of Science ®Google Scholar
• Roth MY. Male hormonal contraception. Virtual Mentor 2012; 14:126-32; PMID:23116954
   PubMedGoogle Scholar
• Nya-Ngatchou JJ, Amory JK. New approaches to male non-hormonal contraception. Contraception 2013; 87:296-9; PMID:22995542; http://dx.doi.org/10.1016/j.contraception.2012.08.016
   PubMed Web of Science ®Google Scholar
• Mathur PP, D'Cruz SC. The effect of environmental contaminants on testicular function. Asian J Androl 2011; 13:585-91; PMID:21706039; http://dx.doi.org/10.1038/aja.2011.40
   PubMed Web of Science ®Google Scholar
• D'Cruz SC, Jubendradass R, Jayakanthan M, Rani SJ, Mathur PP. Bisphenol a impairs insulin signaling and glucose homeostasis and decreases steroidogenesis in rat testis: an in vivo and in silico study. Food Chem Toxicol 2012; 50:1124-33; PMID:22142692; http://dx.doi.org/10.1016/j.fct.2011.11.041
   PubMed Web of Science ®Google Scholar
• Cheng CY, Wong EW, Lie PP, Li MW, Su L, Siu ER, Yan HH, Mannu J, Mathur PP, Bonanomi M, et al. Environmental toxicants and male reproductive function. Spermatogenesis 2011; 1:2-13; PMID:21866273; http://dx.doi.org/10.4161/spmg.1.1.13971
   PubMedGoogle Scholar
• Li X, Zhang S, Safe S. Activation of kinase pathways in MCF-7 cells by 17beta-estradiol and structurally diverse estrogenic compounds. J Steroid Biochem Mol Biol 2006; 98:122-32; PMID:16413991; http://dx.doi.org/10.1016/j.jsbmb.2005.08.018
   PubMed Web of Science ®Google Scholar
• Bian Q, Qian J, Xu L, Chen J, Song L, Wang X. The toxic effects of 4-tert-octylphenol on the reproductive system of male rats. Food Chem Toxicol 2006; 44:1355-61; PMID:16631297; http://dx.doi.org/10.1016/j.fct.2006.02.014
   PubMed Web of Science ®Google Scholar
• Boockfor FR, Blake CA. Chronic administration of 4-tert-octylphenol to adult male rats causes shrinkage of the testes and male accessory sex organs, disrupts spermatogenesis, and increases the incidence of sperm deformities. Biol Reproduct 1997; 57:267-77; PMID:9241039; http://dx.doi.org/10.1095/biolreprod57.2.267
   PubMed Web of Science ®Google Scholar
• Sebolt-Leopold JS. Development of anticancer drugs targeting the MAP kinase pathway. Oncogene 2000; 19:6594-9; PMID:11426644
   PubMed Web of Science ®Google Scholar
• Dunn KB, Heffler M, Golubovskaya VM. Evolving therapies and FAK inhibitors for the treatment of cancer. Anticancer Agents Med Chem 2010; 10:722-34; PMID:21291406; http://dx.doi.org/10.2174/187152010794728657
   PubMed Web of Science ®Google Scholar
• Tang EI, Xiao X, Mruk DD, Qian XJ, Mok KW, Jenardhanan P, Lee WM, Mathur PP, Cheng CY. Microtubule affinity-regulating kinase 4 (MARK4) is a component of the ectoplasmic specialization in the rat testis. Spermatogenesis 2012; 2:117-26; PMID:22670221; http://dx.doi.org/10.4161/spmg.20724
   PubMedGoogle Scholar
• Li Y, Sosnik J, Brassard L, Reese M, Spiridonov NA, Bates TC, Johnson GR, Anguita J, Visconti PE, Salicioni AM. Expression and localization of five members of the testis-specific serine kinase (Tssk) family in mouse and human sperm and testis. Mol Hum Reproduct 2011; 17:42-56; PMID:20729278; http://dx.doi.org/10.1093/molehr/gaq071
   PubMed Web of Science ®Google Scholar
• de Lamirande E, O'Flaherty C. Sperm activation: role of reactive oxygen species and kinases. Biochim Biophys Acta 2008; 1784:106-15; PMID:17920343; http://dx.doi.org/10.1016/j.bbapap.2007.08.024
   PubMed Web of Science ®Google Scholar
• Burton KA, McKnight GS. PKA, germ cells, and fertility. Physiology 2007; 22:40-6; PMID:17289929; http://dx.doi.org/10.1152/physiol.00034.2006
   PubMed Web of Science ®Google Scholar
• Breitbart H, Naor Z. Protein kinases in mammalian sperm capacitation and the acrosome reaction. Rev Reproduct 1999; 4:151-9; PMID:10521152; http://dx.doi.org/10.1530/ror.0.0040151
   PubMedGoogle Scholar
• Breitbart H, Rotman T, Rubinstein S, Etkovitz N. Role and regulation of PI3K in sperm capacitation and the acrosome reaction. Mol Cell Endocrinol 2010; 314:234-8; PMID:19560510; http://dx.doi.org/10.1016/j.mce.2009.06.009
   PubMed Web of Science ®Google Scholar
• Ickowicz D, Finkelstein M, Breitbart H. Mechanism of sperm capacitation and the acrosome reaction: role of protein kinases. Asian J Androl 2012; 14:816-21; PMID:23001443; http://dx.doi.org/10.1038/aja.2012.81
   PubMed Web of Science ®Google Scholar
• Ikebe C, Ohashi K, Mizuno K. Identification of testis-specific (Limk2t) and brain-specific (Limk2c) isoforms of mouse LIM-kinase 2 gene transcripts. Biochem Biophys Res Commun 1998; 246:307-12; PMID:9610354; http://dx.doi.org/10.1006/bbrc.1998.8609
   PubMed Web of Science ®Google Scholar
• Jaffer ZM, Chernoff J. p21-activated kinases: three more join the Pak. Int J Biochem Cell Biol 2002; 34:713-7; PMID:11950587; http://dx.doi.org/10.1016/S1357-2725(01)00158-3
   PubMed Web of Science ®Google Scholar
• Molli PR, Li DQ, Murray BW, Rayala SK, Kumar R. PAK signaling in oncogenesis. Oncogene 2009; 28:2545-55; PMID:19465939; http://dx.doi.org/10.1038/onc.2009.119
   PubMed Web of Science ®Google Scholar
• Baskaran Y, Ng YW, Selamat W, Ling FT, Manser E. Group I and II mammalian PAKs have different modes of activation by Cdc42. EMBO Rep 2012; 13:653-9; PMID:22653441; http://dx.doi.org/10.1038/embor.2012.75
   PubMed Web of Science ®Google Scholar
• Yang F, Li X, Sharma M, Zarnegar M, Lim B, Sun Z. Androgen receptor specifically interacts with a novel p21-activated kinase, PAK6. J Biol Chem 2001; 276:15345-53; PMID:11278661; http://dx.doi.org/10.1074/jbc.M010311200
   PubMed Web of Science ®Google Scholar
• Lee SR, Ramos SM, Ko A, Masiello D, Swanson KD, Lu ML, Balk SP. AR and ER interaction with a p21-activated kinase (PAK6). Mol Endocrinol 2002; 16:85-99; PMID:11773441; http://dx.doi.org/10.1210/mend.16.1.0753
   PubMed Web of Science ®Google Scholar
• Liu T, Li Y, Gu H, Zhu G, Li J, Cao L, Li F. p21-Activated kinase 6 (PAK6) inhibits prostate cancer growth via phosphorylation of androgen receptor and tumorigenic E3 ligase murine double minute-2 (Mdm2). J Biol Chem 2013; 288:3359-69; PMID:23132866; http://dx.doi.org/10.1074/jbc.M112.384289
   PubMed Web of Science ®Google Scholar
• Anastassiadis T, Deacon SW, Devarajan K, Ma H, Peterson JR. Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. Nat Biotechnol 2011; 29:1039-45; PMID:22037377; http://dx.doi.org/10.1038/nbt.2017
   PubMed Web of Science ®Google Scholar
• Gao J, Ha BH, Lou HJ, Morse EM, Zhang R, Calderwood DA, Turk BE, Boggon TJ. Substrate and inhibitor specificity of the type II p21-activated kinase, PAK6. PloS One 2013; 8:e77818; PMID:24204982; http://dx.doi.org/10.1371/journal.pone.0077818
   PubMed Web of Science ®Google Scholar
• Coburn AM, Cappon GD, Bowman CJ, Stedman DB, Patyna S. Reproductive toxicity assessment of sunitinib, a multitargeted receptor tyrosine kinase inhibitor, in male and female rats. Birth Defects Res B Dev Reprod Toxicol 2012; 95:267-75; PMID:22499257; http://dx.doi.org/10.1002/bdrb.21012
   PubMedGoogle Scholar
• Trinczek B, Brajenovic M, Ebneth A, Drewes G. MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes. J Biol Chem 2004; 279:5915-23; PMID:14594945; http://dx.doi.org/10.1074/jbc.M304528200
   PubMed Web of Science ®Google Scholar
• Gabrovska PN, Smith RA, Haupt LM, Griffiths LR. Investigation of two Wnt signalling pathway single nucleotide polymorphisms in a breast cancer-affected Australian population. Twin Res Hum Genet 2011; 14:562-7; PMID:22506312; http://dx.doi.org/10.1375/twin.14.6.562
   PubMed Web of Science ®Google Scholar
• Timm T, von Kries JP, Li X, Zempel H, Mandelkow E, Mandelkow EM. Microtubule affinity regulating kinase activity in living neurons was examined by a genetically encoded fluorescence resonance energy transfer/fluorescence lifetime imaging-based biosensor: inhibitors with therapeutic potential. J Biol Chem 2011; 286:41711-22; PMID:21984823; http://dx.doi.org/10.1074/jbc.M111.257865
   PubMed Web of Science ®Google Scholar
• Jenardhanan P, Mannu J, Mathur PP. The structural analysis of MARK4 and the exploration of specific inhibitors for the MARK family: a computational approach to obstruct the role of MARK4 in prostate cancer progression. Mol BioSyst 2014; 10:1845-68; PMID:24763618; http://dx.doi.org/10.1039/c3mb70591a
   PubMedGoogle Scholar
• Bucko-Justyna M, Lipinski L, Burgering BM, Trzeciak L. Characterization of testis-specific serine-threonine kinase 3 and its activation by phosphoinositide-dependent kinase-1-dependent signalling. FEBS J 2005; 272:6310-23; PMID:16336268; http://dx.doi.org/10.1111/j.1742-4658.2005.05018.x
   PubMed Web of Science ®Google Scholar
• Kueng P, Nikolova Z, Djonov V, Hemphill A, Rohrbach V, Boehlen D, Zuercher G, Andres AC, Ziemiecki A. A novel family of serine/threonine kinases participating in spermiogenesis. J Cell Biol 1997; 139:1851-9; PMID:9412477; http://dx.doi.org/10.1083/jcb.139.7.1851
   PubMed Web of Science ®Google Scholar
• Zuercher G, Rohrbach V, Andres AC, Ziemiecki A. A novel member of the testis specific serine kinase family, tssk-3, expressed in the Leydig cells of sexually mature mice. Mech Dev 2000; 93:175-7; PMID:10781952; http://dx.doi.org/10.1016/S0925-4773(00)00255-0
   PubMed Web of Science ®Google Scholar
• Spiridonov NA, Wong L, Zerfas PM, Starost MF, Pack SD, Paweletz CP, Johnson GR. Identification and characterization of SSTK, a serine/threonine protein kinase essential for male fertility. Mol Cell Biol 2005; 25:4250-61; PMID:15870294; http://dx.doi.org/10.1128/MCB.25.10.4250-4261.2005
   PubMed Web of Science ®Google Scholar
• Shang P, Baarends WM, Hoogerbrugge J, Ooms MP, van Cappellen WA, de Jong AA, Dohle GR, van Eenennaam H, Gossen JA, Grootegoed JA. Functional transformation of the chromatoid body in mouse spermatids requires testis-specific serine/threonine kinases. J Cell Sci 2010; 123:331-9; PMID:20053632; http://dx.doi.org/10.1242/jcs.059949
   PubMed Web of Science ®Google Scholar
• Xu B, Hao Z, Jha KN, Zhang Z, Urekar C, Digilio L, Pulido S, Strauss JF, 3rd, Flickinger CJ, Herr JC. Targeted deletion of Tssk1 and 2 causes male infertility due to haploinsufficiency. Dev Biol 2008; 319:211-22; PMID:18533145; http://dx.doi.org/10.1016/j.ydbio.2008.03.047
   PubMed Web of Science ®Google Scholar
• Jaleel M, McBride A, Lizcano JM, Deak M, Toth R, Morrice NA, Alessi DR. Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate. FEBS Lett 2005; 579:1417-23; PMID:15733851 http://dx.doi.org/10.1016/j.febslet.2005.01.042
   PubMed Web of Science ®Google Scholar
• Thomas SM, Brugge JS. Cellular functions regulated by Src family kinases. Annu Rev Cell Dev Biol 1997; 13:513-609; PMID:9442882; http://dx.doi.org/10.1146/annurev.cellbio.13.1.513
   PubMed Web of Science ®Google Scholar
• Siu ER, Wong EW, Mruk DD, Porto CS, Cheng CY. Focal adhesion kinase is a blood-testis barrier regulator. Proc Natl Acad Sci USA. 2009; 106:9298-303; PMID:19470647; http://dx.doi.org/10.1073/pnas.0813113106
   PubMed Web of Science ®Google Scholar
• Siu ER, Wong EW, Mruk DD, Sze KL, Porto CS, Cheng CY. An occludin-focal adhesion kinase protein complex at the blood-testis barrier: a study using the cadmium model. Endocrinology 2009; 150:3336-44; PMID:19213829; http://dx.doi.org/10.1210/en.2008-1741
   PubMed Web of Science ®Google Scholar
• Wan HT, Mruk DD, Tang EI, Xiao X, Cheng YH, Wong EW, Wong CK, Cheng CY. Role of non-receptor protein tyrosine kinases in spermatid transport during spermatogenesis. Semin Cell Dev Biol 2014; PMID:24727349
   PubMed Web of Science ®Google Scholar
• Siu MK, Mruk DD, Lee WM, Cheng CY. Adhering junction dynamics in the testis are regulated by an interplay of β 1-integrin and focal adhesion complex-associated proteins. Endocrinology 2003; 144:2141-63; PMID:12697723; http://dx.doi.org/10.1210/en.2002-221035
   PubMed Web of Science ®Google Scholar
• Cheng CY, Lie PP, Wong EW, Mruk DD. Focal adhesion kinase and actin regulatory/binding proteins that modulate F-actin organization at the tissue barrier: lesson from the testis. Tissue Barriers 2013; 1:e24252; PMID:24665388; http://dx.doi.org/10.4161/tisb.24252
   PubMedGoogle Scholar
• Li SY, Mruk DD, Cheng CY. Focal adhesion kinase is a regulator of F-actin dynamics: new insights from studies in the testis. Spermatogenesis 2013; 3:e25385; PMID:24381802
   PubMedGoogle Scholar
• Schaller MD. Cellular functions of FAK kinases: insight into molecular mechanisms and novel functions. J Cell Sci 2010; 123:1007-13; PMID:20332118; http://dx.doi.org/10.1242/jcs.045112
   PubMed Web of Science ®Google Scholar
• Slack-Davis JK, Martin KH, Tilghman RW, Iwanicki M, Ung EJ, Autry C, Luzzio MJ, Cooper B, Kath JC, Roberts WG, et al. Cellular characterization of a novel focal adhesion kinase inhibitor. J Biol Chem 2007; 282:14845-52; PMID:17395594; http://dx.doi.org/10.1074/jbc.M606695200
   PubMed Web of Science ®Google Scholar
• Roberts WG, Ung E, Whalen P, Cooper B, Hulford C, Autry C, Richter D, Emerson E, Lin J, Kath J, et al. Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271. Cancer Res 2008; 68:1935-44; PMID:18339875; http://dx.doi.org/10.1158/0008-5472.CAN-07-5155
   PubMed Web of Science ®Google Scholar
• Shi Q, Hjelmeland AB, Keir ST, Song L, Wickman S, Jackson D, Ohmori O, Bigner DD, Friedman HS, Rich JN. A novel low-molecular weight inhibitor of focal adhesion kinase, TAE226, inhibits glioma growth. Mol Carcinog 2007; 46:488-96; PMID:17219439; http://dx.doi.org/10.1002/mc.20297
   PubMed Web of Science ®Google Scholar
• Golubovskaya VM, Virnig C, Cance WG. TAE226-induced apoptosis in breast cancer cells with overexpressed Src or EGFR. Mol Carcinog 2008; 47:222-34; PMID:17849451; http://dx.doi.org/10.1002/mc.20380
   PubMed Web of Science ®Google Scholar
• Liu TJ, LaFortune T, Honda T, Ohmori O, Hatakeyama S, Meyer T, Jackson D, de Groot J, Yung WK. Inhibition of both focal adhesion kinase and insulin-like growth factor-I receptor kinase suppresses glioma proliferation in vitro and in vivo. Mol Cancer Ther 2007; 6:1357-67; PMID:17431114; http://dx.doi.org/10.1158/1535-7163.MCT-06-0476
   PubMed Web of Science ®Google Scholar
• Walsh C, Tanjoni I, Uryu S, Tomar A, Nam JO, Luo H, Phillips A, Patel N, Kwok C, McMahon G, et al. Oral delivery of PND-1186 FAK inhibitor decreases tumor growth and spontaneous breast to lung metastasis in pre-clinical models. Cancer Biol Ther 2010; 9:778-90; PMID:20234193; http://dx.doi.org/10.4161/cbt.9.10.11433
   PubMed Web of Science ®Google Scholar
• Lietha D, Eck MJ. Crystal structures of the FAK kinase in complex with TAE226 and related bis-anilino pyrimidine inhibitors reveal a helical DFG conformation. PloS One 2008; 3:e3800; PMID:19030106
   PubMed Web of Science ®Google Scholar
• Iwatani M, Iwata H, Okabe A, Skene RJ, Tomita N, Hayashi Y, Aramaki Y, Hosfield DJ, Hori A, Baba A, et al. Discovery and characterization of novel allosteric FAK inhibitors. Eur J Med Chem 2013; 61:49-60; PMID:22819505; http://dx.doi.org/10.1016/j.ejmech.2012.06.035
   PubMed Web of Science ®Google Scholar
• Maekawa M, Toyama Y, Yasuda M, Yagi T, Yuasa S. Fyn tyrosine kinase in Sertoli cells is involved in mouse spermatogenesis. Biol Reprod 2002; 66:211-21; PMID:11751285; http://dx.doi.org/10.1095/biolreprod66.1.211
   PubMed Web of Science ®Google Scholar
• Kierszenbaum AL, Rivkin E, Talmor-Cohen A, Shalgi R, Tres LL. Expression of full-length and truncated Fyn tyrosine kinase transcripts and encoded proteins during spermatogenesis and localization during acrosome biogenesis and fertilization. Mol Reprod Dev 2009; 76:832-43; PMID:19441121; http://dx.doi.org/10.1002/mrd.21049
   PubMed Web of Science ®Google Scholar
• Luo J, Gupta V, Kern B, Tash JS, Sanchez G, Blanco G, Kinsey WH. Role of FYN kinase in spermatogenesis: defects characteristic of Fyn-null sperm in mice. Biol Reprod 2012; 86:1-8; PMID:21918125; http://dx.doi.org/10.1095/biolreprod.111.093864
   PubMed Web of Science ®Google Scholar
• Kinoshita T, Matsubara M, Ishiguro H, Okita K, Tada T. Structure of human Fyn kinase domain complexed with staurosporine. Biochem Biophys Res Commun 2006; 346:840-4; PMID:16782058; http://dx.doi.org/10.1016/j.bbrc.2006.05.212
   PubMed Web of Science ®Google Scholar
• Poli G, Tuccinardi T, Rizzolio F, Caligiuri I, Botta L, Granchi C, Ortore G, Minutolo F, Schenone S, Martinelli A. Identification of new Fyn kinase inhibitors using a FLAP-based approach. J Chem Inf Model 2013; 53:2538-47; PMID:24001328; http://dx.doi.org/10.1021/ci4002553
   PubMed Web of Science ®Google Scholar
• Bordeleau LJ, Leclerc P. Expression of hck-tr, a truncated form of the src-related tyrosine kinase hck, in bovine spermatozoa and testis. Mol Reprod Dev 2008; 75:828-37; PMID:17926339; http://dx.doi.org/10.1002/mrd.20814
   PubMed Web of Science ®Google Scholar
• Schindler T, Sicheri F, Pico A, Gazit A, Levitzki A, Kuriyan J. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol Cell 1999; 3:639-48; PMID:10360180; http://dx.doi.org/10.1016/S1097-2765(00)80357-3
   PubMed Web of Science ®Google Scholar
• Hao Z, Jha KN, Kim YH, Vemuganti S, Westbrook VA, Chertihin O, Markgraf K, Flickinger CJ, Coppola M, Herr JC, et al. Expression analysis of the human testis-specific serine/threonine kinase (TSSK) homologues. A TSSK member is present in the equatorial segment of human sperm. Mol Hum Reprod 2004; 10:433-44; PMID:15044604; http://dx.doi.org/10.1093/molehr/gah052
   PubMed Web of Science ®Google Scholar
• Chapin RE, Wine RN, Harris MW, Borchers CH, Haseman JK. Structure and control of a cell-cell adhesion complex associated with spermiation in rat seminiferous epithelium. J Androl 2001; 22:1030-52; PMID:11700851
   PubMed Web of Science ®Google Scholar
• Abe MK, Kuo WL, Hershenson MB, Rosner MR. Extracellular signal-regulated kinase 7 (ERK7), a novel ERK with a C-terminal domain that regulates its activity, its cellular localization, and cell growth. Mol Cell Biol 1999; 19:1301-12; PMID:9891064
   PubMed Web of Science ®Google Scholar
• Shiraishi K, Yoshida K, Fujimiya T, Naito K. Activation of mitogen activated protein kinases and apoptosis of germ cells after vasectomy in the rat. J Urol 2002; 168:1273-8; PMID:12187281; http://dx.doi.org/10.1016/S0022-5347(05)64639-3
   PubMed Web of Science ®Google Scholar
• Gupta S, Barrett T, Whitmarsh AJ, Cavanagh J, Sluss HK, Derijard B, Davis RJ. Selective interaction of JNK protein kinase isoforms with transcription factors. EMBO J 1996; 15:2760; PMID:8654373
   PubMed Web of Science ®Google Scholar
• Wong CH, Mruk DD, Siu MK, Cheng CY. Blood-testis barrier dynamics are regulated by 2-macroglobulin via the c-Jun N-terminal protein kinase pathway. Endocrinology 2005; 146:1893-908; PMID:15618353; http://dx.doi.org/10.1210/en.2004-1464
   PubMed Web of Science ®Google Scholar
• Ikebe C, Ohashi K, Mizuno K. Identification of testis-specific (Limk2t) and brain-specific (Limk2c) isoforms of mouse LIM-kinase 2 gene transcripts. Biochem Biophys Res Commun 1998; 246:307-12; PMID:9610354; http://dx.doi.org/10.1006/bbrc.1998.8609
   PubMed Web of Science ®Google Scholar
• Karn T, Holtrich U, Wolf G, Hock B, Strebhardt K, Rubsamenwaigmann H. Human SAK related to the PLK/polo family of cell cycle kinases shows high mRNA expression in testis. Oncol Rep 1997; 4:505-10; PMID:21590086
   PubMed Web of Science ®Google Scholar
• Xia L, Robinson D, Ma AH, Chen HC, Wu F, Qiu Y, Kung HJ. Identification of human male germ cell-associated kinase, a kinase transcriptionally activated by androgen in prostate cancer cells. J Biol Chem 2002; 277:35422-33; PMID:12084720; http://dx.doi.org/10.1074/jbc.M203940200
   PubMed Web of Science ®Google Scholar
• Unni SK, Modi DN, Pathak SG, Dhabalia JV, Bhartiya D. Stage-specific localization and expression of c-kit in the adult human testis. J Histochem Cytochem 2009; 57:861-9; PMID:19435714; http://dx.doi.org/10.1369/jhc.2009.953737
   PubMed Web of Science ®Google Scholar
• Oatley JM, Avarbock MR, Brinster RL. Glial cell line-derived neurotrophic factor regulation of genes essential for self-renewal of mouse spermatogonial stem cells is dependent on Src family kinase signaling. J Biol Chem 2007; 282:25842-51; PMID:17597063; http://dx.doi.org/10.1074/jbc.M703474200
   PubMed Web of Science ®Google Scholar
• Chen YM, Lee NP, Mruk DD, Lee WM, Cheng CY. Fer kinase/FerT and adherens junction dynamics in the testis: an in vitro and in vivo study. Biol Reprod 2003; 69:656-72; PMID:12700184; http://dx.doi.org/10.1095/biolreprod.103.016881
   PubMed Web of Science ®Google Scholar
• Goupil S, La Salle S, Trasler JM, Bordeleau LJ, Leclerc P. Developmental expression of SRC-related tyrosine kinases in the mouse testis. J Androl 2011; 32:95-110; PMID:20798388; http://dx.doi.org/10.2164/jandrol.110.010462
   PubMedGoogle Scholar
• Somanath PR, Jack SL, Vijayaraghavan S. Changes in sperm glycogen synthase kinase-3 serine phosphorylation and activity accompany motility initiation and stimulation. J Androl 2004; 25:605-17; PMID:15223849
   PubMed Web of Science ®Google Scholar
• Nesic D, Miller MC, Quinkert ZT, Stein M, Chait BT, Stebbins CE. Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nat Struct Mol Biol 2010; 17:130-2; PMID:19966800; http://dx.doi.org/10.1038/nsmb.1705
   PubMed Web of Science ®Google Scholar
• Eswar N, Webb B, Marti-Renom MA, Madhusudhan MS, Eramian D, Shen MY, Pieper U, Sali A. Comparative protein structure modeling using MODELLER. Curr Protoc Protein Sci, John E Coligan [et al] 2007; Chapter 2:Unit 2.9; PMID:18429317; http://dx.doi.org/10.1002/0471140864.ps0209s50
   PubMedGoogle Scholar
• Halgren TA, Murphy RB, Friesner RA, Beard HS, Frye LL, Pollard WT, Banks JL. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. J Med Chem 2004; 47:1750-9; PMID:15027866; http://dx.doi.org/10.1021/jm030644s
   PubMed Web of Science ®Google Scholar