Urokinase-type plasminogen activator

Details

Name
Urokinase-type plasminogen activator
Synonyms
  • 3.4.21.73
  • U-plasminogen activator
Gene Name
PLAU
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037097|Urokinase-type plasminogen activator
MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQ
HCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHN
YCRNPDNRRRPWCYVQVGLKPLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKII
GGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLG
RSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICL
PSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKML
CAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIR
SHTKEENGLAL
Number of residues
431
Molecular Weight
48507.09
Theoretical pI
8.48
GO Classification
Functions
serine-type endopeptidase activity
Processes
angiogenesis / blood coagulation / cellular response to fluid shear stress / cellular response to glucose stimulus / cellular response to hepatocyte growth factor stimulus / cellular response to hypoxia / cellular response to lipopolysaccharide / cellular response to staurosporine / chemotaxis / embryo implantation / fibrinolysis / neuron death / plasminogen activation / positive regulation of cell proliferation / positive regulation of ovulation / positive regulation of reactive oxygen species metabolic process / positive regulation of smooth muscle cell migration / proteolysis / regulation of cell adhesion mediated by integrin / regulation of hepatocyte proliferation / regulation of receptor activity / regulation of smooth muscle cell migration / regulation of smooth muscle cell-matrix adhesion / regulation of wound healing / response to activity / response to hyperoxia / signal transduction / skeletal muscle tissue regeneration / smooth muscle cell migration / spermatogenesis
Components
cell surface / extracellular exosome / extracellular region / extracellular space / focal adhesion / plasma membrane
General Function
Serine-type endopeptidase activity
Specific Function
Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0021654|Urokinase-type plasminogen activator (PLAU)
ATGGTCTTCCATTTGAGAACTAGATACGAACAGGCGAACTGTGACTGTCTAAATGGAGGA
ACATGTGTGTCCAACAAGTACTTCTCCAACATTCACTGGTGCAACTGCCCAAAGAAATTC
GGAGGGCAGCACTGTGAAATAGATAAGTCAAAAACCTGCTATGAGGGGAATGGTCACTTT
TACCGAGGAAAGGCCAGCACTGACACCATGGGCCGGCCCTGCCTGCCCTGGAACTCTGCC
ACTGTCCTTCAGCAAACGTACCATGCCCACAGATCTGATGCTCTTCAGCTGGGCCTGGGG
AAACATAATTACTGCAGGAACCCAGACAACCGGAGGCGACCCTGGTGCTATGTGCAGGTG
GGCCTAAAGCCGCTTGTCCAAGAGTGCATGGTGCATGACTGCGCAGATGGAAAAAAGCCC
TCCTCTCCTCCAGAAGAATTAAAATTTCAGTGTGGCCAAAAGACTCTGAGGCCCCGCTTT
AAGATTATTGGGGGAGAATTCACCACCATCGAGAACCAGCCCTGGTTTGCGGCCATCTAC
AGGAGGCACCGGGGGGGCTCTGTCACCTACGTGTGTGGAGGCAGCCTCATCAGCCCTTGC
TGGGTGATCAGCGCCACACACTGCTTCATTGATTACCCAAAGAAGGAGGACTACATCGTC
TACCTGGGTCGCTCAAGGCTTAACTCCAACACGCAAGGGGAGATGAAGTTTGAGGTGGAA
AACCTCATCCTACACAAGGACTACAGCGCTGACACGCTTGCTCACCACAACGACATTGCC
TTGCTGAAGATCCGTTCCAAGGAGGGCAGGTGTGCGCAGCCATCCCGGACTATACAGACC
ATCTGCCTGCCCTCGATGTATAACGATCCCCAGTTTGGCACAAGCTGTGAGATCACTGGC
TTTGGAAAAGAGAATTCTACCGACTATCTCTATCCGGAGCAGCTGAAAATGACTGTTGTG
AAGCTGATTTCCCACCGGGAGTGTCAGCAGCCCCACTACTACGGCTCTGAAGTCACCACC
AAAATGCTGTGTGCTGCTGACCCACAGTGGAAAACAGATTCCTGCCAGGGAGACTCAGGG
GGACCCCTCGTCTGTTCCCTCCAAGGCCGCATGACTTTGACTGGAATTGTGAGCTGGGGC
CGTGGATGTGCCCTGAAGGACAAGCCAGGCGTCTACACGAGAGTCTCACACTTCTTACCC
TGGATCCGCAGTCACACCAAGGAAGAGAATGGCCTGGCCCTCTGA
Chromosome Location
10
Locus
10q24
External Identifiers
ResourceLink
UniProtKB IDP00749
UniProtKB Entry NameUROK_HUMAN
GenBank Protein ID1834524
GenBank Gene IDX02419
GenAtlas IDPLAU
HGNC IDHGNC:9052
General References
  1. Jacobs P, Cravador A, Loriau R, Brockly F, Colau B, Chuchana P, van Elsen A, Herzog A, Bollen A: Molecular cloning, sequencing, and expression in Escherichia coli of human preprourokinase cDNA. DNA. 1985 Apr;4(2):139-46. [PubMed:3888571]
  2. Nagai M, Hiramatsu R, Kaneda T, Hayasuke N, Arimura H, Nishida M, Suyama T: Molecular cloning of cDNA coding for human preprourokinase. Gene. 1985;36(1-2):183-8. [PubMed:2415429]
  3. Riccio A, Grimaldi G, Verde P, Sebastio G, Boast S, Blasi F: The human urokinase-plasminogen activator gene and its promoter. Nucleic Acids Res. 1985 Apr 25;13(8):2759-71. [PubMed:2987867]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed:15164054]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  7. Yoshimoto M, Ushiyama Y, Sakai M, Tamaki S, Hara H, Takahashi K, Sawasaki Y, Hanada K: Characterization of single chain urokinase-type plasminogen activator with a novel amino-acid substitution in the kringle structure. Biochim Biophys Acta. 1996 Mar 7;1293(1):83-9. [PubMed:8652631]
  8. Buko AM, Kentzer EJ, Petros A, Menon G, Zuiderweg ER, Sarin VK: Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3992-6. [PubMed:2023947]
  9. Verde P, Stoppelli MP, Galeffi P, Di Nocera P, Blasi F: Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4727-31. [PubMed:6589620]
  10. Gunzler WA, Steffens GJ, Otting F, Kim SM, Frankus E, Flohe L: The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain. Hoppe Seylers Z Physiol Chem. 1982 Oct;363(10):1155-65. [PubMed:6754569]
  11. Schaller J, Nick H, Rickli EE, Gillessen D, Lergier W, Studer RO: Human low-molecular-weight urinary urokinase. Partial characterization and preliminary sequence data of the two polypeptide chains. Eur J Biochem. 1982 Jul;125(2):251-7. [PubMed:6749491]
  12. Steffens GJ, Gunzler WA, Otting F, Frankus E, Flohe L: The complete amino acid sequence of low molecular mass urokinase from human urine. Hoppe Seylers Z Physiol Chem. 1982 Sep;363(9):1043-58. [PubMed:6754572]
  13. Stief TW, Radtke KP, Heimburger N: Inhibition of urokinase by protein C-inhibitor (PCI). Evidence for identity of PCI and plasminogen activator inhibitor 3. Biol Chem Hoppe Seyler. 1987 Oct;368(10):1427-33. [PubMed:3501295]
  14. Franco P, Iaccarino C, Chiaradonna F, Brandazza A, Iavarone C, Mastronicola MR, Nolli ML, Stoppelli MP: Phosphorylation of human pro-urokinase on Ser138/303 impairs its receptor-dependent ability to promote myelomonocytic adherence and motility. J Cell Biol. 1997 May 5;137(3):779-91. [PubMed:9151681]
  15. He S, Lin YL, Liu YX: Functionally inactive protein C inhibitor in seminal plasma may be associated with infertility. Mol Hum Reprod. 1999 Jun;5(6):513-9. [PubMed:10340997]
  16. Behrendt N, Jensen ON, Engelholm LH, Mortz E, Mann M, Dano K: A urokinase receptor-associated protein with specific collagen binding properties. J Biol Chem. 2000 Jan 21;275(3):1993-2002. [PubMed:10636902]
  17. Liu CX, Li Y, Obermoeller-McCormick LM, Schwartz AL, Bu G: The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein. J Biol Chem. 2001 Aug 3;276(31):28889-96. Epub 2001 May 30. [PubMed:11384978]
  18. Wakita T, Hayashi T, Nishioka J, Tamaru H, Akita N, Asanuma K, Kamada H, Gabazza EC, Ido M, Kawamura J, Suzuki K: Regulation of carcinoma cell invasion by protein C inhibitor whose expression is decreased in renal cell carcinoma. Int J Cancer. 2004 Feb 10;108(4):516-23. [PubMed:14696115]
  19. Ustach CV, Kim HR: Platelet-derived growth factor D is activated by urokinase plasminogen activator in prostate carcinoma cells. Mol Cell Biol. 2005 Jul;25(14):6279-88. [PubMed:15988036]
  20. Paterson AD, Rommens JM, Bharaj B, Blavignac J, Wong I, Diamandis M, Waye JS, Rivard GE, Hayward CP: Persons with Quebec platelet disorder have a tandem duplication of PLAU, the urokinase plasminogen activator gene. Blood. 2010 Feb 11;115(6):1264-6. doi: 10.1182/blood-2009-07-233965. Epub 2009 Dec 9. [PubMed:20007542]
  21. Oswald RE, Bogusky MJ, Bamberger M, Smith RA, Dobson CM: Dynamics of the multidomain fibrinolytic protein urokinase from two-dimensional NMR. Nature. 1989 Feb 9;337(6207):579-82. [PubMed:2536903]
  22. Li X, Smith RA, Dobson CM: Sequential 1H NMR assignments and secondary structure of the kringle domain from urokinase. Biochemistry. 1992 Oct 13;31(40):9562-71. [PubMed:1327118]
  23. Li X, Bokman AM, Llinas M, Smith RA, Dobson CM: Solution structure of the kringle domain from urokinase-type plasminogen activator. J Mol Biol. 1994 Feb 4;235(5):1548-59. [PubMed:8107091]
  24. Spraggon G, Phillips C, Nowak UK, Ponting CP, Saunders D, Dobson CM, Stuart DI, Jones EY: The crystal structure of the catalytic domain of human urokinase-type plasminogen activator. Structure. 1995 Jul 15;3(7):681-91. [PubMed:8591045]
  25. Sperl S, Jacob U, Arroyo de Prada N, Sturzebecher J, Wilhelm OG, Bode W, Magdolen V, Huber R, Moroder L: (4-aminomethyl)phenylguanidine derivatives as nonpeptidic highly selective inhibitors of human urokinase. Proc Natl Acad Sci U S A. 2000 May 9;97(10):5113-8. [PubMed:10805774]
  26. Huai Q, Mazar AP, Kuo A, Parry GC, Shaw DE, Callahan J, Li Y, Yuan C, Bian C, Chen L, Furie B, Furie BC, Cines DB, Huang M: Structure of human urokinase plasminogen activator in complex with its receptor. Science. 2006 Feb 3;311(5761):656-9. [PubMed:16456079]
  27. Conne B, Berczy M, Belin D: Detection of polymorphisms in the human urokinase-type plasminogen activator gene. Thromb Haemost. 1997 Mar;77(3):434-5. [PubMed:9065988]
  28. Turkmen B, Schmitt M, Schmalfeldt B, Trommler P, Hell W, Creutzburg S, Graeff H, Magdolen V: Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer. Electrophoresis. 1997 May;18(5):686-9. [PubMed:9194591]
  29. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. doi: 10.1038/nature07485. [PubMed:18987736]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00013Urokinaseapproved, investigational, withdrawnyesDetails
DB00594AmilorideapprovedunknowninhibitorDetails
DB019776-(N-Phenylcarbamyl)-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB023986-[N-(4-(Aminomethyl)Phenyl)Carbamyl]-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB024736-[N-(1-Isopropyl-3,4-Dihydro-7-Isoquinolinyl)Carbamyl]-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB025516-[N-(4-Ethyl-1,2,3,4-Tetrahydro-6-Isoquinolinyl)Carbamyl]-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB027056-[N-(1-Isopropyl-1,2,3,4-Tetrahydro-7-Isoquinolinyl)Carbamyl]-2-NaphthalenecarboxamidineexperimentalunknownDetails
DB030467-Methoxy-8-[1-(Methylsulfonyl)-1h-Pyrazol-4-Yl]Naphthalene-2-CarboximidamideexperimentalunknownDetails
DB030826-[(Z)-Amino(Imino)Methyl]-N-[4-(Aminomethyl)Phenyl]-4-(Pyrimidin-2-Ylamino)-2-NaphthamideexperimentalunknownDetails
DB03127BenzamidineexperimentalunknownDetails
DB03476Trans-6-(2-Phenylcyclopropyl)-Naphthalene-2-CarboxamidineexperimentalunknownDetails
DB037292-Amino-5-Hydroxy-BenzimidazoleexperimentalunknownDetails
DB03782N-(1-Adamantyl)-N'-(4-Guanidinobenzyl)UreaexperimentalunknownDetails
DB040598-(Pyrimidin-2-Ylamino)Naphthalene-2-CarboximidamideexperimentalunknownDetails
DB04172[2,4,6-Triisopropyl-Phenylsulfonyl-L-[3-Amidino-Phenylalanine]]-Piperazine-N'-Beta-AlanineexperimentalunknownDetails
DB05254FibrinolysininvestigationalunknownDetails
DB019052-(2-Hydroxy-5-Methoxy-Phenyl)-1h-Benzoimidazole-5-CarboxamidineexperimentalunknownDetails
DB017252-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamideexperimentalunknownDetails
DB038656-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-CarboxamidineexperimentalunknownDetails
DB068556-fluoro-2-(2-hydroxy-3-isobutoxy-phenyl)-1H-benzoimidazole-5-carboxamidineexperimentalunknownDetails
DB068566-FLUORO-2-[2-HYDROXY-3-(2-METHYL-CYCLOHEXYLOXY)-PHENYL]-1H-INDOLE-5-CARBOXAMIDINEexperimentalunknownDetails
DB06857N-(4-CARBAMIMIDOYL-3-CHORO-PHENYL)-2-HYDROXY-3-IODO-5-METHYL-BENZAMIDEexperimentalunknownDetails
DB070766-[(Z)-AMINO(IMINO)METHYL]-N-[3-(CYCLOPENTYLOXY)PHENYL]-2-NAPHTHAMIDEexperimentalunknownDetails
DB071221-[4-(2-oxo-2-phenylethyl)phenyl]guanidineexperimentalunknownDetails
DB07129(2R)-1-(2,6-dimethylphenoxy)propan-2-amineexperimentalunknownDetails
DB02526CRA_10655experimentalunknownDetails
DB03159CRA_8696experimentalunknownDetails
DB022872-(2-Hydroxy-Phenyl)-3h-Benzoimidazole-5-CarboxamidineexperimentalunknownDetails
DB076254-(2-aminoethoxy)-N-(2,5-diethoxyphenyl)-3,5-dimethylbenzamideexperimentalunknownDetails
DB076264-(2-aminoethoxy)-N-(3-chloro-2-ethoxy-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamideexperimentalunknownDetails
DB031364-Iodobenzo[B]Thiophene-2-CarboxamidineexperimentalunknownDetails
DB03876Thieno[2,3-B]Pyridine-2-CarboxamidineexperimentalunknownDetails
DB080724-(2-AMINOETHOXY)-3,5-DICHLORO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDEexperimentalunknownDetails
DB086974-(2-aminoethoxy)-N-(3-chloro-5-piperidin-1-ylphenyl)-3,5-dimethylbenzamideexperimentalunknownDetails