Glycogen phosphorylase, muscle form

Details

Name
Glycogen phosphorylase, muscle form
Kind
protein
Synonyms
  • 2.4.1.1
  • Myophosphorylase
Gene Name
PYGM
UniProtKB Entry
P11217Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0001824|Glycogen phosphorylase, muscle form
MSRPLSDQEKRKQISVRGLAGVENVTELKKNFNRHLHFTLVKDRNVATPRDYYFALAHTV
RDHLVGRWIRTQQHYYEKDPKRIYYLSLEFYMGRTLQNTMVNLALENACDEATYQLGLDM
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKISGGWQMEEA
DDWLRYGNPWEKARPEFTLPVHFYGHVEHTSQGAKWVDTQVVLAMPYDTPVPGYRNNVVN
TMRLWSAKAPNDFNLKDFNVGGYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTNFDAFPDKVAIQLNDTHPSLAIPELMRILVDLERM
DWDKAWDVTVRTCAYTNHTVLPEALERWPVHLLETLLPRHLQIIYEINQRFLNRVAAAFP
GDVDRLRRMSLVEEGAVKRINMAHLCIAGSHAVNGVARIHSEILKKTIFKDFYELEPHKF
QNKTNGITPRRWLVLCNPGLAEVIAERIGEDFISDLDQLRKLLSFVDDEAFIRDVAKVKQ
ENKLKFAAYLEREYKVHINPNSLFDIQVKRIHEYKRQLLNCLHVITLYNRIKREPNKFFV
PRTVMIGGKAAPGYHMAKMIIRLVTAIGDVVNHDPAVGDRLRVIFLENYRVSLAEKVIPA
ADLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENFFIFGMRVEDVD
KLDQRGYNAQEYYDRIPELRQVIEQLSSGFFSPKQPDLFKDIVNMLMHHDRFKVFADYED
YIKCQEKVSALYKNPREWTRMVIRNIATSGKFSSDRTIAQYAREIWGVEPSRQRLPAPDE
AI
Number of residues
842
Molecular Weight
97091.265
Theoretical pI
7.03
GO Classification
Functions
linear malto-oligosaccharide phosphorylase activity / nucleotide binding / SHG alpha-glucan phosphorylase activity
General Function
Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis
Specific Function
Glycogen phosphorylase activity
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0010645|Glycogen phosphorylase, muscle form (PYGM)
ATGTCCCGGCCCCTGTCAGACCAAGAGAAAAGAAAGCAAATCAGTGTGCGTGGCCTGGCC
GGCGTGGAGAACGTGACTGAGCTGAAAAAGAACTTCAACCGGCACCTGCATTTCACACTC
GTAAAGGACCGCAATGTGGCCACCCCACGAGACTACTACTTTGCTCTGGCCCATACCGTG
CGCGACCACCTCGTGGGGCGCTGGATCCGCACGCAGCAGCACTACTATGAGAAGGACCCC
AAGAAGATCTCCGGGGGCTGGCAGATGGAGGAGGCCGATGACTGGCTTCGCTACGGCAAC
CCCTGGGAGAAGGCCCGGCCCGAGTTCACGCTACCTGTGCACTTCTACGGCCATGTGGAG
CACACCAGCCAGGGTGCCAAGTGGGTGGACACACAGGTGGTACTGGCCATGCCCTACGAT
ACGCCCGTGCCTGGCTATCGCAACAATGTTGTCAACACCATGCGCCTCTGGTCTGCCAAG
GCTCCCAATGACTTCAACCTCAAGGACTTCAATGTCGGTGGCTACATCCAGGCTGTGTTG
GACCGAAACCTGGCGGAGAACATCTCTCGTGTCCTGTACCCCAATGATAATTTCTTCGAA
GGGAAGGAGCTGCGGCTGAAGCAGGAGTATTTCGTGGTGGCTGCCACCCTCCAGGACATC
ATCCGTCGCTTCAAGTCTTCCAAGTTCGGCTGCCGTGATCCCGTGCGCACGAACTTCGAT
GCCTTCCCAGATAAGGTGGCCATCCAGCTCAATGACACCCACCCCTCCCTGGCCATCCCC
GAGCTGATGAGGATCCTGGTGGACCTGGAACGGATGGACTGGGACAAGGCGTGGGATGTG
ACAGTGAGGACCTGTGCCTACACCAACCACACGGTGCTGCCCGAGGCCCTGGAGCGCTGG
CCGGTGCACCTCTTGGAGACGCTGCTGCCGCGGCACCTCCAGATCATCTACGAGATCAAC
CAGCGCTTCCTCAACCGGGTGGCGGCCGCATTCCCAGGGGACGTAGACCGGCTGCGGCGC
ATGTCGCTGGTGGAGGAGGGCGCAGTGAAGCGCATCAACATGGCACACCTGTGCATCGCG
GGGTCGCACGCCGTCAACGGCGTGGCGCGCATCCACTCCGAGATCCTCAAGAAGACCATC
TTCAAAGACTTCTATGAGCTGGAGCCTCATAAGTTCCAGAATAAGACCAACGGCATCACC
CCTCGGCGCTGGCTGGTTCTGTGTAACCCCGGGCTGGCAGAGGTCATTGCTGAGCGCATC
GGGGAGGACTTCATCTCTGACCTGGACCAGCTGCGCAAACTGCTCTCCTTTGTGGATGAT
GAAGCTTTCATTCGGGATGTGGCCAAAGTGAAGCAGGAAAACAAGTTGAAGTTTGCTGCC
TACCTAGAGAGGGAATACAAAGTCCACATCAACCCCAACTCACTCTTCGACATCCAGGTG
AAGCGGATTCACGAATATAAACGACAGCTCCTCAACTGCCTCCATGTCATCACCCTGTAC
AACCGCATCAAGAGGGAGCCCAATAAGTTTTTTGTGCCTCGGACTGTGATGATTGGAGGG
AAGGCTGCACCTGGGTACCACATGGCCAAGATGATCATCAGACTCGTCACAGCCATCGGG
GATGTGGTCAACCATGACCCGGCAGTGGGTGACCGCCTCCGTGTCATCTTCCTGGAGAAC
TACCGAGTCTCACTGGCCGAGAAAGTGATCCCAGCTGCAGACCTCTCTGAGCAGATCTCC
ACTGCGGGCACTGAAGCCTCAGGCACCGGCAACATGAAGTTCATGCTCAACGGGGCTCTG
ACCATTGGCACCATGGACGGGGCCAATGTGGAGATGGCAGAAGAGGCGGGAGAGGAAAAC
TTCTTCATCTTTGGCATGCGGGTGGAGGATGTGGATAAGCTTGACCAAAGAGGGTACAAT
GCCCAGGAGTACTACGATCGCATTCCTGAGCTTCGGCAGGTCATTGAGCAGCTGAGCAGT
GGCTTCTTCTCCCCCAAACAGCCCGACCTGTTCAAGGACATTGTCAATATGCTCATGCAC
CATGACCGGTTTAAAGTCTTCGCAGATTATGAAGACTACATTAAATGCCAGGAGAAAGTC
AGCGCCTTGTACAAGAACCCAAGAGAGTGGACGCGGATGGTGATCCGGAACATAGCCACC
TCTGGCAAGTTCTCCAGTGACCGCACCATTGCCCAGTATGCCCGGGAGATCTGGGGTGTG
GAGCCTTCCCGCCAGCGCCTGCCAGCCCCGGATGAGGCCATCTGA
Chromosome Location
11
Locus
11q13.1
External Identifiers
ResourceLink
UniProtKB IDP11217
UniProtKB Entry NamePYGM_HUMAN
GenBank Protein ID190784
GenBank Gene IDM32598
GeneCard IDPYGM
GenAtlas IDPYGM
HGNC IDHGNC:9726
PDB ID(s)1Z8D
KEGG IDhsa:5837
NCBI Gene ID5837
General References
  1. Burke J, Hwang P, Anderson L, Lebo R, Gorin F, Fletterick R: Intron/exon structure of the human gene for the muscle isozyme of glycogen phosphorylase. Proteins. 1987;2(3):177-87. [Article]
  2. Kubisch C, Wicklein EM, Jentsch TJ: Molecular diagnosis of McArdle disease: revised genomic structure of the myophosphorylase gene and identification of a novel mutation. Hum Mutat. 1998;12(1):27-32. [Article]
  3. 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. [Article]
  4. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [Article]
  5. 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. [Article]
  6. Hwang PK, See YP, Vincentini AM, Powers MA, Fletterick RJ, Crerar MM: Comparative sequence analysis of rat, rabbit, and human muscle glycogen phosphorylase cDNAs. Eur J Biochem. 1985 Oct 15;152(2):267-74. [Article]
  7. Gautron S, Daegelen D, Mennecier F, Dubocq D, Kahn A, Dreyfus JC: Molecular mechanisms of McArdle's disease (muscle glycogen phosphorylase deficiency). RNA and DNA analysis. J Clin Invest. 1987 Jan;79(1):275-81. [Article]
  8. Carty TJ, Tu J-I, Graves DJ: Regulation of glycogen phosphorylase. Role of the peptide region surrounding the phosphoserine residue in determining enzyme properties. J Biol Chem. 1975 Jul 10;250(13):4980-5. [Article]
  9. Tsujino S, Shanske S, DiMauro S: Molecular genetic heterogeneity of myophosphorylase deficiency (McArdle's disease). N Engl J Med. 1993 Jul 22;329(4):241-5. [Article]
  10. Tsujino S, Shanske S, Martinuzzi A, Heiman-Patterson T, DiMauro S: Two novel missense mutations (E654K, L396P) in Caucasian patients with myophosphorylase deficiency (McArdle's disease). Hum Mutat. 1995;6(3):276-7. [Article]
  11. Tsujino S, Shanske S, Nonaka I, DiMauro S: The molecular genetic basis of myophosphorylase deficiency (McArdle's disease). Muscle Nerve Suppl. 1995;3:S23-7. [Article]
  12. Vorgerd M, Kubisch C, Burwinkel B, Reichmann H, Mortier W, Tettenborn B, Pongratz D, Lindemuth R, Tegenthoff M, Malin JP, Kilimann MW: Mutation analysis in myophosphorylase deficiency (McArdle's disease). Ann Neurol. 1998 Mar;43(3):326-31. [Article]
  13. Gamez J, Fernandez R, Bruno C, Andreu AL, Cervera C, Navarro C, Schwartz S, Dimauro S: A new mutation in the regulatory domain of the myophosphorylase gene affecting protein dimer contact. Muscle Nerve. 1999 Aug;22(8):1136-8. [Article]
  14. Andreu AL, Bruno C, Tamburino L, Gamez J, Shanske S, Cervera C, Navarro C, DiMauro S: A new mutation in the myophosphorylase gene (Asn684Tyr) in a Spanish patient with McArdle's disease. Neuromuscul Disord. 1999 May;9(3):171-3. [Article]
  15. Rubio JC, Martin MA, Garcia A, Campos Y, Cabello A, Culebras JM, Arenas J: McArdle's disease associated with homozygosity for the missense mutation Gly204Ser of the myophosphorylase gene in a Spanish patient. Neuromuscul Disord. 1999 May;9(3):174-5. [Article]
  16. Fernandez R, Navarro C, Andreu AL, Bruno C, Shanske S, Gamez J, Teijeira S, Hernandez I, Teijeiro A, Fernandez JM, Musumeci O, DiMauro S: A novel missense mutation (W797R) in the myophosphorylase gene in Spanish patients with McArdle disease. Arch Neurol. 2000 Feb;57(2):217-9. [Article]
  17. Rubio JC, Martin MA, Campos Y, Auciello R, Cabello A, Arenas J: A missense mutation W797R in the myophosphorylase gene in a Spanish patient with McArdle's disease. Muscle Nerve. 2000 Jan;23(1):129-31. [Article]
  18. Rubio JC, Martin MA, Campos Y, Cabello A, Arenas J: A missense mutation T487N in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Feb;10(2):138-40. [Article]
  19. Martin MA, Rubio JC, Campos Y, Ricoy JR, Cabello A, Arenas J: A homozygous missense mutation (A659D) in the myophosphorylase gene in a Spanish patient with McArdle's disease. Neuromuscul Disord. 2000 Aug;10(6):447-9. [Article]
  20. Martin MA, Rubio JC, Buchbinder J, Fernandez-Hojas R, del Hoyo P, Teijeira S, Gamez J, Navarro C, Fernandez JM, Cabello A, Campos Y, Cervera C, Culebras JM, Andreu AL, Fletterick R, Arenas J: Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study. Ann Neurol. 2001 Nov;50(5):574-81. [Article]
  21. Bruno C, Lanzillo R, Biedi C, Iadicicco L, Minetti C, Santoro L: Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease. Neuromuscul Disord. 2002 Jun;12(5):498-500. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Beta-D-Glucopyranose SpirohydantoinexperimentalunknowntargetDetails
(5S,7R,8S,9S,10R)-3-Amino-8,9,10-trihydroxy-7-(hydroxymethyl)-6-oxa-1,3-diazaspiro[4.5]decane-2,4-dioneexperimentalunknowntargetDetails
alpha-D-glucose 6-phosphateexperimentalyestargetinhibitorDetails
N-beta-D-glucopyranosylacetamideexperimentalyestargetinhibitorDetails
Monofluorophosphate ionexperimentalyestargetinhibitorDetails
3,8,9,10-tetrahydroxy-7-hydroxymethyl-6-oxa-1,3-diaza-spiro[4.5]decane-2,4-dioneexperimentalunknowntargetDetails
Nojirimycine TetrazoleexperimentalyestargetinhibitorDetails
Indirubin-5-sulphonateexperimentalunknowntargetDetails
2-Deoxy-Glucose-6-PhosphateexperimentalyestargetinhibitorDetails
C-(1-hydrogyl-beta-D-glucopyranosyl) formamideexperimentalyestargetinhibitorDetails
alpha-D-glucopyranosyl-2-carboxylic acid amideexperimentalyestargetinhibitorDetails
alpha-D-glucose-1-phosphateexperimentalyestargetinhibitorDetails
Beta-D-GlucoseexperimentalyestargetinhibitorDetails
8,9,10-Trihydroxy-7-hydroxymethyl-2-thioxo-6-oxa-1,3-diaza-spiro[4.5]decan-4-oneexperimentalunknowntargetDetails
4-{2,4-Bis[(3-Nitrobenzoyl)Amino]Phenoxy}Phthalic AcidexperimentalunknowntargetDetails
2-(Beta-D-Glucopyranosyl)-5-Methyl-1,2,3-BenzimidazoleexperimentalunknowntargetDetails
N-acetyl-N'-beta-D-glucopyranosyl ureaexperimentalyestargetinhibitorDetails
C-(1-Azido-Alpha-D-Glucopyranosyl) FormamideexperimentalunknowntargetDetails
2-(Beta-D-Glucopyranosyl)-5-Methyl-1,3,4-OxadiazoleexperimentalunknowntargetDetails
(3,4,5-Trihydroxy-6-Hydroxymethyl-Tetrahydro-Pyran-2-Yl)-Phosphoramidic Acid Dimethyl EsterexperimentalunknowntargetDetails
8,9,10-trihydroxy-7-hydroxymethyl-3-methyl-6-oxa-1,3-diaza-spiro[4.5]decane-2,4-dioneexperimentalunknowntargetDetails
Alvocidibexperimental, investigationalyestargetinhibitorDetails
1-deoxy-1-methoxycarbamido-beta-D-glucopyranoseexperimentalyestargetinhibitorDetails
N-[(5S,7R,8S,9S,10R)-8,9,10-Trihydroxy-7-(hydroxymethyl)-2,4-dioxo-6-oxa-1,3-diazaspiro[4.5]dec-3-yl]acetamideexperimentalunknowntargetDetails
1-Deoxy-1-methoxycarbamido-beta-D-gluco-2-heptulopyranosonamideexperimentalunknowntargetDetails
2,3-Dicarboxy-4-(2-Chloro-Phenyl)-1-Ethyl-5-Isopropoxycarbonyl-6-Methyl-PyridiniumexperimentalunknowntargetDetails
N(6)-(pyridoxal phosphate)-L-lysineexperimentalunknowntargetDetails
Heptulose-2-PhosphateexperimentalyestargetinhibitorDetails
N-(Benzoylcarbamoyl)-beta-D-glucopyranosylamineexperimentalyestargetinhibitorDetails
DexfosfoserineexperimentalyestargetinhibitorDetails
1-Deoxy-1-acetylamino-beta-D-gluco-2-heptulopyranosonamideexperimentalunknowntargetDetails
Inosinic AcidexperimentalyestargetinhibitorDetails
Pyridoxal phosphateapproved, investigational, nutraceuticalunknowntargetcofactorDetails
7-{2,6-DICHLORO-4-[3-(2-CHLORO-BENZOYL)-UREIDO]-PHENOXY}-HEPTANOIC ACIDexperimentalunknowntargetDetails
4-{2-[(3-Nitrobenzoyl)Amino]Phenoxy}Phthalic AcidexperimentalyestargetinhibitorDetails
2-CHLORO-N-[(1R,2R)-1-HYDROXY-2,3-DIHYDRO-1H-INDEN-2-YL]-6H-THIENO[2,3-B]PYRROLE-5-CARBOXAMIDEexperimentalunknowntargetDetails
2-CHLORO-N-[(3R)-2-OXO-1,2,3,4-TETRAHYDROQUINOLIN-3-YL]-6H-THIENO[2,3-B]PYRROLE-5-CARBOXAMIDEexperimentalunknowntargetDetails
4-{3-CHLORO-4-[3-(2,4-DICHLORO-BENZOYL)-UREIDO]-PHENOXY}-BUTYRIC ACIDexperimentalunknowntargetDetails
4-{4-[3-(2,4-DICHLORO-BENZOYL)-UREIDO]-2,3-DIMETHYL-PHENOXY}-BUTYRIC ACIDexperimentalunknowntargetDetails
5-{3-[3-(2,4-DICHLORO-BENZOYL)-UREIDO]-2-METHYL-PHENOXY}-PENTANOIC ACIDexperimentalunknowntargetDetails
CP-320626experimentalunknowntargetDetails
(S)-2-CHLORO-N-(1-(2-(2-HYDROXYETHYLAMINO)-2-OXOETHYL)-2-OXO-1,2,3,4-TETRAHYDROQUINOLIN-3-YL)-6H-THIENO[2,3-B]PYRROLE-5-CARBOXAMIDEexperimentalunknowntargetDetails
(2S)-N-[(3S)-1-(2-AMINO-2-OXOETHYL)-2-OXO-1,2,3,4-TETRAHYDROQUINOLIN-3-YL]-2-CHLORO-2H-THIENO[2,3-B]PYRROLE-5-CARBOXAMIDEexperimentalunknowntargetDetails
(3R,4R,5R)-5-(HYDROXYMETHYL)-1-(3-PHENYLPROPYL)PIPERIDINE-3,4-DIOLexperimentalunknowntargetDetails
({[(3E)-2'-Oxo-2',7'-dihydro-2,3'-biindol-3(7H)-ylidene]amino}oxy)acetic acidexperimentalunknowntargetDetails
(5R,7R,8S,9S,10R)-7-(hydroxymethyl)-3-phenyl-1,6-dioxa-2-azaspiro[4.5]dec-2-ene-8,9,10-triolexperimentalunknowntargetDetails
2-DEOXY-3,4-BIS-O-[3-(4-HYDROXYPHENYL)PROPANOYL]-L-THREO-PENTARIC ACIDexperimentalunknowntargetDetails
(3S,5R,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(2-naphthyl)-1,6-dioxa-2-azaspiro[4.5]decane-8,9,10-triolexperimentalunknowntargetDetails
(3S,5R,7R,8S,9S,10R)-7-(hydroxymethyl)-3-(4-methylphenyl)-1,6-dioxa-2-azaspiro[4.5]decane-8,9,10-triolexperimentalunknowntargetDetails
2-(Beta-D-Glucopyranosyl)-5-Methyl-1,3,4-BenzothiazoleexperimentalunknowntargetDetails
BetulininvestigationalyestargetinhibitorDetails
Asiatic acidexperimentalyestargetinhibitorDetails
Ursolic acidexperimentalyestargetinhibitorDetails