| Year |
Citation |
Score |
| 2014 |
Keiffer TR, Bond JS. Meprin metalloproteases inactivate interleukin 6 Journal of Biological Chemistry. 289: 7580-7588. PMID 24474695 DOI: 10.1074/Jbc.M113.546309 |
0.746 |
|
| 2013 |
Bao J, Yura RE, Matters GL, Bradley SG, Shi P, Tian F, Bond JS. Meprin A impairs epithelial barrier function, enhances monocyte migration, and cleaves the tight junction protein occludin American Journal of Physiology - Renal Physiology. 305: F714-F726. PMID 23804454 DOI: 10.1152/Ajprenal.00179.2012 |
0.588 |
|
| 2013 |
Roff AN, Panganiban RP, Bond JS, Ishmael FT. Post-transcriptional regulation of meprin α by the RNA-binding proteins Hu antigen R (HuR) and tristetraprolin (TTP) Journal of Biological Chemistry. 288: 4733-4743. PMID 23269677 DOI: 10.1074/Jbc.M112.444208 |
0.594 |
|
| 2013 |
Jefferson T, Auf Dem Keller U, Bellac C, Metz VV, Broder C, Hedrich J, Ohler A, Maier W, Magdolen V, Sterchi E, Bond JS, Jayakumar A, Traupe H, Chalaris A, Rose-John S, et al. The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10 Cellular and Molecular Life Sciences. 70: 309-333. PMID 22940918 DOI: 10.1007/S00018-012-1106-2 |
0.378 |
|
| 2013 |
Bertenshaw GP, Bond JS. Meprin B Handbook of Proteolytic Enzymes. 1: 910-916. DOI: 10.1016/B978-0-12-382219-2.00190-3 |
0.694 |
|
| 2013 |
Bertenshaw GP, Bond JS. Meprin A Handbook of Proteolytic Enzymes. 1: 900-910. DOI: 10.1016/B978-0-12-382219-2.00189-7 |
0.685 |
|
| 2011 |
Ongeri EM, Anyanwu O, Reeves WB, Bond JS. Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusion American Journal of Physiology - Renal Physiology. 301: F871-F882. PMID 21795642 DOI: 10.1152/Ajprenal.00703.2010 |
0.328 |
|
| 2011 |
Jefferson T, Čaušević M, auf dem Keller U, Schilling O, Isbert S, Geyer R, Maier W, Tschickardt S, Jumpertz T, Weggen S, Bond JS, Overall CM, Pietrzik CU, Becker-Pauly C. Metalloprotease meprin beta generates nontoxic N-terminal amyloid precursor protein fragments in vivo. The Journal of Biological Chemistry. 286: 27741-50. PMID 21646356 DOI: 10.1074/Jbc.M111.252718 |
0.353 |
|
| 2011 |
Garcia-Caballero A, Ishmael SS, Dang Y, Gillie D, Bond JS, Milgram SL, Stutts MJ. Activation of the epithelial sodium channel by the metalloprotease meprin β subunit. Channels (Austin, Tex.). 5: 14-22. PMID 20953144 DOI: 10.4161/Chan.5.1.13759 |
0.783 |
|
| 2009 |
Banerjee S, Oneda B, Yap LM, Jewell DP, Matters GL, Fitzpatrick LR, Seibold F, Sterchi EE, Ahmad T, Lottaz D, Bond JS. MEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel disease Mucosal Immunology. 2: 220-231. PMID 19262505 DOI: 10.1038/Mi.2009.3 |
0.328 |
|
| 2009 |
Sun Q, Jin HJ, Bond JS. Disruption of the meprin α and β genes in mice alters homeostasis of monocytes and natural killer cells Experimental Hematology. 37: 346-356. PMID 19110362 DOI: 10.1016/J.Exphem.2008.10.016 |
0.334 |
|
| 2009 |
Yura RE, Bradley SG, Ramesh G, Reeves WB, Bond JS. Meprin A metalloproteases enhance renal damage and bladder inflammation after LPS challenge American Journal of Physiology - Renal Physiology. 296: F135-F144. PMID 18971209 DOI: 10.1152/Ajprenal.90524.2008 |
0.335 |
|
| 2009 |
Sterchi EE, Stöcker W, Bond JS. Meprins, membrane-bound and secreted astacin metalloproteinases Molecular Aspects of Medicine. 29: 309-328. PMID 18783725 DOI: 10.1016/J.Mam.2008.08.002 |
0.378 |
|
| 2008 |
Banerjee S, Bond JS. Prointerleukin-18 is activated by meprin β in vitro and in vivo in intestinal inflammation Journal of Biological Chemistry. 283: 31371-31377. PMID 18786924 DOI: 10.1074/Jbc.M802814200 |
0.4 |
|
| 2008 |
López-Otín C, Bond JS. Proteases: Multifunctional enzymes in life and disease Journal of Biological Chemistry. 283: 30433-30437. PMID 18650443 DOI: 10.1074/Jbc.R800035200 |
0.369 |
|
| 2008 |
Bylander J, Li Q, Ramesh G, Zhang B, Reeves WB, Bond JS. Targeted disruption of the meprin metalloproteinase β gene protects against renal ischemia-reperfusion injury in mice American Journal of Physiology - Renal Physiology. 294: F480-F490. PMID 18172000 DOI: 10.1152/Ajprenal.00214.2007 |
0.349 |
|
| 2007 |
Bylander JE, Bertenshaw GP, Matters GL, Hubbard SJ, Bond JS. Human and mouse homo-oligomeric meprin A metalloendopeptidase: Substrate and inhibitor specificities Biological Chemistry. 388: 1163-1172. PMID 17976009 DOI: 10.1515/Bc.2007.156 |
0.748 |
|
| 2006 |
Ishmael SS, Ishmael FT, Jones AD, Bond JS. Protease domain glycans affect oligomerization, disulfide bond formation, and stability of the meprin A metalloprotease homo-oligomer Journal of Biological Chemistry. 281: 37404-37415. PMID 17040911 DOI: 10.1074/Jbc.M602769200 |
0.784 |
|
| 2005 |
Matters GL, Manni A, Bond JS. Inhibitors of polyamine biosynthesis decrease the expression of the metalloproteases meprin α and MMP-7 in hormone-independent human breast cancer cells Clinical and Experimental Metastasis. 22: 331-339. PMID 16170669 DOI: 10.1007/S10585-005-0660-5 |
0.343 |
|
| 2005 |
Bond JS, Matters GL, Banerjee S, Dusheck RE. Meprin metalloprotease expression and regulation in kidney, intestine, urinary tract infections and cancer Febs Letters. 579: 3317-3322. PMID 15943977 DOI: 10.1016/J.Febslet.2005.03.045 |
0.35 |
|
| 2005 |
Mathew R, Futterweit S, Valderrama E, Tarectecan AA, Bylander JE, Bond JS, Trachtman H. Meprin-α in chronic diabetic nephropathy: Interaction with, the renin-angiotensin axis American Journal of Physiology - Renal Physiology. 289: F911-F921. PMID 15942051 DOI: 10.1152/Ajprenal.00037.2005 |
0.352 |
|
| 2005 |
Ishmael FT, Shier VK, Ishmael SS, Bond JS. Intersubunit and domain interactions of the meprin B metalloproteinase: Disulfide bonds and protein-protein interactions in the MAM and TRAF domains Journal of Biological Chemistry. 280: 13895-13901. PMID 15695509 DOI: 10.1074/Jbc.M414218200 |
0.777 |
|
| 2004 |
Hengst JA, Bond JS. Transport of meprin subunits through the secretory pathway: Role of the transmembrane and cytoplasmic domains and oligomerization Journal of Biological Chemistry. 279: 34856-34864. PMID 15187079 DOI: 10.1074/Jbc.M405774200 |
0.715 |
|
| 2004 |
Crisman JM, Zhang B, Norman LP, Bond JS. Deletion of the mouse meprin beta metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix. Journal of Immunology (Baltimore, Md. : 1950). 172: 4510-9. PMID 15034068 DOI: 10.4049/Jimmunol.172.7.4510 |
0.331 |
|
| 2003 |
Villa JP, Bertenshaw GP, Bylander JE, Bond JS. Meprin proteolytic complexes at the cell surface and in extracellular spaces Biochemical Society Symposium. 53-63. PMID 14587282 DOI: 10.1042/Bss0700053 |
0.773 |
|
| 2003 |
Villa JP, Bertenshaw GP, Bond JS. Critical Amino Acids in the Active Site of Meprin Metalloproteinases for Substrate and Peptide Bond Specificity Journal of Biological Chemistry. 278: 42545-42550. PMID 12888571 DOI: 10.1074/Jbc.M303718200 |
0.773 |
|
| 2003 |
Norman LP, Matters GL, Crisman JM, Bond JS. Expression of meprins in health and disease. Current Topics in Developmental Biology. 54: 145-66. PMID 12696749 DOI: 10.1016/S0070-2153(03)54008-X |
0.384 |
|
| 2003 |
Norman LP, Jiang W, Han X, Saunders TL, Bond JS. Targeted disruption of the meprin beta gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles. Molecular and Cellular Biology. 23: 1221-30. PMID 12556482 DOI: 10.1128/Mcb.23.4.1221-1230.2003 |
0.36 |
|
| 2003 |
Bertenshaw GP, Norcum MT, Bond JS. Structure of homo- and hetero-oligomeric meprin metalloproteases: Dimers, tetramers, and high molecular mass multimers Journal of Biological Chemistry. 278: 2522-2532. PMID 12399461 DOI: 10.1074/Jbc.M208808200 |
0.782 |
|
| 2002 |
Bertenshaw GP, Villa JP, Hengst JA, Bond JS. Probing the active sites and mechanisms of rat metalloproteases meprin A and B Biological Chemistry. 383: 1175-1183. PMID 12437103 DOI: 10.1515/Bc.2002.129 |
0.744 |
|
| 2002 |
Doll BA, Villa JP, Ishmael FT, Bond JS. Zinc ligands in an astacin family metalloprotease meprin A Biological Chemistry. 383: 1167-1173. PMID 12437102 DOI: 10.1515/Bc.2002.128 |
0.758 |
|
| 2002 |
Tsukuba T, Kadowaki T, Hengst JA, Bond JS. Chaperone interactions of the metalloproteinase meprin A in the secretory or proteasomal-degradative pathway Archives of Biochemistry and Biophysics. 397: 191-198. PMID 11795871 DOI: 10.1006/Abbi.2001.2672 |
0.709 |
|
| 2002 |
Norcum MT, Labat KB, Bertenshaw GP, Bond JS. Three-dimensional architecture of latent and active meprin B Microscopy and Microanalysis. 8: 824-825. |
0.706 |
|
| 2001 |
Ishmael FT, Norcum MT, Benkovic SJ, Bond JS. Multimeric Structure of the Secreted Meprin A Metalloproteinase and Characterization of the Functional Protomer Journal of Biological Chemistry. 276: 23207-23211. PMID 11301339 DOI: 10.1074/Jbc.M102654200 |
0.688 |
|
| 2001 |
Bertenshaw GP, Turk BE, Hubbard SJ, Matters GL, Bylander JE, Crisman JM, Cantley LC, Bond JS. Marked Differences between Metalloproteases Meprin A and B in Substrate and Peptide Bond Specificity Journal of Biological Chemistry. 276: 13248-13255. PMID 11278902 DOI: 10.1074/Jbc.M011414200 |
0.777 |
|
| 2001 |
Kumar JM, Bond JS. Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning Biochimica Et Biophysica Acta - Gene Structure and Expression. 1518: 106-114. PMID 11267665 DOI: 10.1016/S0167-4781(01)00188-9 |
0.384 |
|
| 2000 |
Kadowaki T, Tsukuba T, Bertenshaw GP, Bond JS. N-linked oligosaccharides on the meprin A metalloprotease are important for secretion and enzymatic activity, but not for apical targeting Journal of Biological Chemistry. 275: 25577-25584. PMID 10837482 DOI: 10.1074/Jbc.M003521200 |
0.775 |
|
| 2000 |
Jiang W, Kumar JM, Matters GL, Bond JS. Structure of the mouse metalloprotease meprin β gene (Mep1b): Alternative splicing in cancer cells Gene. 248: 77-87. PMID 10806353 DOI: 10.1016/S0378-1119(00)00143-8 |
0.311 |
|
| 2000 |
Bertenshaw GP, Bond JS. Proteases: From fertilization to cell death Trends in Pharmacological Sciences. 21: 319-320. DOI: 10.1016/S0165-6147(00)01525-X |
0.702 |
|
| 1999 |
Matters GL, Bond JS. Expression and regulation of the meprin β gene in human cancer cells Molecular Carcinogenesis. 25: 169-178. PMID 10411143 DOI: 10.1002/(Sici)1098-2744(199907)25:3<169::Aid-Mc3>3.0.Co;2-Y |
0.337 |
|
| 1999 |
Matters GL, Bond JS. Meprin B: Transcriptional and posttranscriptional regulation of the meprin β metalloproteinase subunit in human and mouse cancer cells Apmis. 107: 19-27. PMID 10190276 DOI: 10.1111/J.1699-0463.1999.Tb01522.X |
0.329 |
|
| 1998 |
Tsukuba T, Bond JS. Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase. The Journal of Biological Chemistry. 273: 35260-7. PMID 9857066 DOI: 10.1074/Jbc.273.52.35260 |
0.452 |
|
| 1998 |
Tang J, Bond JS. Maturation of secreted meprin alpha during biosynthesis: role of the furin site and identification of the COOH-terminal amino acids of the mouse kidney metalloprotease subunit. Archives of Biochemistry and Biophysics. 349: 192-200. PMID 9439598 DOI: 10.1006/Abbi.1997.0453 |
0.463 |
|
| 1998 |
Doll BA, Bond JS. Mutation of proposed zinc ligands in the protease domain of the meprin a subunit Faseb Journal. 12: A1426. |
0.68 |
|
| 1997 |
Johnson GD, Bond JS. Activation mechanism of meprins, members of the astacin metalloendopeptidase family. The Journal of Biological Chemistry. 272: 28126-32. PMID 9346968 DOI: 10.1074/Jbc.272.44.28126 |
0.468 |
|
| 1997 |
Bond JS, Jiang W. Membrane metalloendopeptidases in immune function and disease. Advances in Experimental Medicine and Biology. 421: 1-6. PMID 9330673 DOI: 10.1007/978-1-4757-9613-1_1 |
0.321 |
|
| 1996 |
Ricardo SD, Bond JS, Johnson GD, Kaspar J, Diamond JR. Expression of subunits of the metalloendopeptidase meprin in renal cortex in experimental hydronephrosis. The American Journal of Physiology. 270: F669-76. PMID 8967345 DOI: 10.1152/Ajprenal.1996.270.4.F669 |
0.363 |
|
| 1996 |
Marchand P, Volkmann M, Bond JS. Cysteine mutations in the MAM domain result in monomeric meprin and alter stability and activity of the proteinase. The Journal of Biological Chemistry. 271: 24236-41. PMID 8798668 DOI: 10.1074/Jbc.271.39.24236 |
0.462 |
|
| 1996 |
Bankus JM, Bond JS. Expression and distribution of meprin protease subunits in mouse intestine. Archives of Biochemistry and Biophysics. 331: 87-94. PMID 8660687 DOI: 10.1006/Abbi.1996.0286 |
0.389 |
|
| 1996 |
Dietrich JM, Jiang W, Bond JS. A novel meprin beta' mRNA in mouse embryonal and human colon carcinoma cells. The Journal of Biological Chemistry. 271: 2271-8. PMID 8567689 DOI: 10.1074/Jbc.271.4.2271 |
0.364 |
|
| 1995 |
Marchand P, Tang J, Johnson GD, Bond JS. COOH-terminal proteolytic processing of secreted and membrane forms of the alpha subunit of the metalloprotease meprin A. Requirement of the I domain for processing in the endoplasmic reticulum. The Journal of Biological Chemistry. 270: 5449-56. PMID 7890660 DOI: 10.1074/Jbc.270.10.5449 |
0.443 |
|
| 1995 |
Bond JS, Rojas K, Overhauser J, Zoghbi HY, Jiang W. The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively. Genomics. 25: 300-3. PMID 7774936 DOI: 10.1016/0888-7543(95)80142-9 |
0.301 |
|
| 1995 |
Bond JS, Beynon RJ. The astacin family of metalloendopeptidases. Protein Science : a Publication of the Protein Society. 4: 1247-61. PMID 7670368 DOI: 10.1002/Pro.5560040701 |
0.42 |
|
| 1993 |
Gorbea CM, Marchand P, Jiang W, Copeland NG, Gilbert DJ, Jenkins NA, Bond JS. Cloning, expression, and chromosomal localization of the mouse meprin beta subunit. The Journal of Biological Chemistry. 268: 21035-43. PMID 8407940 |
0.302 |
|
| 1993 |
Hall JL, Sterchi EE, Bond JS. Biosynthesis and degradation of meprins, kidney brush border proteinases. Archives of Biochemistry and Biophysics. 307: 73-7. PMID 8239666 DOI: 10.1006/Abbi.1993.1562 |
0.405 |
|
| 1992 |
Jiang W, Gorbea CM, Flannery AV, Beynon RJ, Grant GA, Bond JS. The alpha subunit of meprin A. Molecular cloning and sequencing, differential expression in inbred mouse strains, and evidence for divergent evolution of the alpha and beta subunits. The Journal of Biological Chemistry. 267: 9185-93. PMID 1374387 |
0.328 |
|
| 1991 |
Gorbea CM, Flannery AV, Bond JS. Homo- and heterotetrameric forms of the membrane-bound metalloendopeptidases meprin A and B. Archives of Biochemistry and Biophysics. 290: 549-53. PMID 1929422 DOI: 10.1016/0003-9861(91)90580-C |
0.409 |
|
| 1991 |
Wolz RL, Harris RB, Bond JS. Mapping the active site of meprin-A with peptide substrates and inhibitors. Biochemistry. 30: 8488-93. PMID 1883833 DOI: 10.1021/Bi00098A029 |
0.332 |
|
| 1991 |
Craig SS, Mader C, Bond JS. Immunohistochemical localization of the metalloproteinase meprin in salivary glands of male and female mice. The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society. 39: 123-9. PMID 1701182 DOI: 10.1177/39.1.1701182 |
0.333 |
|
| 1991 |
Birkett AJ, Soler DF, Wolz RL, Bond JS, Wiseman J, Berman J, Harris RB. Determination of enzyme specificity in a complex mixture of peptide substrates by N-terminal sequence analysis. Analytical Biochemistry. 196: 137-43. PMID 1653548 DOI: 10.1016/0003-2697(91)90129-H |
0.326 |
|
| 1990 |
Macadam GC, Beynon RJ, Bond JS. A cryptic meprin-like proteolytic activity in mouse kidney brush border membranes. The International Journal of Biochemistry. 22: 989-96. PMID 2282966 DOI: 10.1016/0020-711X(90)90205-H |
0.354 |
|
| 1990 |
Wolz RL, Bond JS. Phe5(4-nitro)-bradykinin: a chromogenic substrate for assay and kinetics of the metalloendopeptidase meprin. Analytical Biochemistry. 191: 314-20. PMID 1964766 DOI: 10.1016/0003-2697(90)90225-X |
0.322 |
|
| 1988 |
Spolarics Z, Bond JS. Multiple molecular forms of mouse liver arginase. Archives of Biochemistry and Biophysics. 260: 469-79. PMID 3277533 DOI: 10.1016/0003-9861(88)90471-7 |
0.364 |
|
| 1988 |
Reckelhoff JF, Craig SS, Beynon RJ, Bond JS. Meprin phenotype and cyclosporin A toxicity in mice. Advances in Experimental Medicine and Biology. 240: 293-304. PMID 3245492 DOI: 10.1007/978-1-4613-1057-0_34 |
0.343 |
|
| 1988 |
Hopgood MF, Knowles SE, Bond JS, Ballard FJ. Degradation of native and modified forms of fructose-bisphosphate aldolase microinjected into HeLa cells. The Biochemical Journal. 256: 81-8. PMID 3223914 DOI: 10.1042/Bj2560081 |
0.365 |
|
| 1987 |
Butler PE, McKay MJ, Bond JS. Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney. The Biochemical Journal. 241: 229-35. PMID 3105525 DOI: 10.1042/Bj2410229 |
0.404 |
|
| 1986 |
Bond JS, Beynon RJ. Meprin: a membrane-bound metallo-endopeptidase. Current Topics in Cellular Regulation. 28: 263-90. PMID 3539535 DOI: 10.1016/B978-0-12-152828-7.50009-3 |
0.351 |
|
| 1986 |
Beynon RJ, Bond JS. Catabolism of intracellular protein: molecular aspects. The American Journal of Physiology. 251: C141-52. PMID 3017118 DOI: 10.1152/Ajpcell.1986.251.2.C141 |
0.31 |
|
| 1985 |
McKay MJ, Garganta CL, Beynon RJ, Bond JS. Deficiency of a mouse kidney metalloendopeptidase activity: immunological demonstration of an altered gene product. Biochemical and Biophysical Research Communications. 132: 171-7. PMID 3933495 DOI: 10.1016/0006-291X(85)91003-4 |
0.315 |
|
| 1984 |
McKay MJ, Marsh MW, Kirschke H, Bond JS. Inactivation of fructose-1,6-bisphosphate aldolase by cathepsin L. Stimulation by ATP. Biochimica Et Biophysica Acta. 784: 9-15. PMID 6691988 DOI: 10.1016/0167-4838(84)90166-3 |
0.308 |
|
| 1984 |
Rosin DL, Bond JS, Bradley SG. A cysteine metalloproteinase from mouse liver cytosol. Proceedings of the Society For Experimental Biology and Medicine. Society For Experimental Biology and Medicine (New York, N.Y.). 177: 112-9. PMID 6433352 DOI: 10.3181/00379727-177-41919 |
0.326 |
|
| 1983 |
McKay MJ, Offermann MK, Barrett AJ, Bond JS. Action of human liver cathepsin B on the oxidized insulin B chain. The Biochemical Journal. 213: 467-71. PMID 6351842 DOI: 10.1042/Bj2130467 |
0.371 |
|
| 1983 |
Bond JS, Shannon JD, Beynon RJ. Certain mouse strains are deficient in a kidney brush-border metalloendopeptidase activity Biochemical Journal. 209: 251-255. PMID 6342606 DOI: 10.1042/Bj2090251 |
0.315 |
|
| 1983 |
Beynon RJ, Bond JS. Deficiency of a kidney metalloproteinase activity in inbred mouse strains Science. 219: 1347-1348. DOI: 10.1126/Science.6338590 |
0.301 |
|
| 1982 |
Shannon JD, Bond JS, Bradley SG. Isolation and characterization of an intracellular serine protease from Rhodococcus erythropolis. Archives of Biochemistry and Biophysics. 219: 80-8. PMID 6758705 DOI: 10.1016/0003-9861(82)90136-9 |
0.353 |
|
| 1981 |
Beynon RJ, Shannon JD, Bond JS. Purification and characterization of a metallo-endoproteinase from mouse kidney Biochemical Journal. 199: 591-598. PMID 7041888 DOI: 10.1042/Bj1990591 |
0.357 |
|
| 1980 |
Duncan WE, Offermann MK, Bond JS. Intracellular turnover of stable and labile soluble liver proteins Archives of Biochemistry and Biophysics. 199: 331-341. PMID 7362232 DOI: 10.1016/0003-9861(80)90288-X |
0.305 |
|
| 1977 |
Bond JS. Acid inactivation of short-lived rat liver enzymes. Biochimica Et Biophysica Acta. 451: 238-49. PMID 12803 DOI: 10.1016/0304-4165(76)90274-9 |
0.323 |
|
| 1974 |
Bond JS, Bird JW. Effects of vitamin E-deficiency on guinea pig lysosomes. Proceedings of the Society For Experimental Biology and Medicine. Society For Experimental Biology and Medicine (New York, N.Y.). 146: 608-12. PMID 4834468 DOI: 10.3181/00379727-146-38157 |
0.596 |
|
| 1974 |
Bond JS. Effect of manganese and amino acids on proteolytic inactivation of beef liver arginase. Biochimica Et Biophysica Acta. 327: 157-65. PMID 4770739 DOI: 10.1016/0005-2744(73)90113-7 |
0.306 |
|
| 1971 |
Bond JS. A comparison of the proteolytic susceptibility of several rat liver enzymes. Biochemical and Biophysical Research Communications. 43: 333-9. PMID 4397029 DOI: 10.1016/0006-291X(71)90757-1 |
0.305 |
|
| 1970 |
Bond JS, Francis SH, Park JH. An essential histidine in the catalytic activities of 3-phosphoglyceraldehyde dehydrogenase. The Journal of Biological Chemistry. 245: 1041-53. PMID 4313702 |
0.426 |
|
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