Year |
Citation |
Score |
2020 |
Manka SW, Brew K. Thermodynamic and mechanistic insights into coupled binding and unwinding of collagen by matrix metalloproteinase 1. Journal of Molecular Biology. PMID 33058879 DOI: 10.1016/j.jmb.2020.10.003 |
0.363 |
|
2019 |
Logue T, Lizotte-Waniewski M, Brew K. Thermodynamic profiles of the interactions of suramin, chondroitin sulfate, and pentosan polysulfate with the inhibitory domain of TIMP-3. Febs Letters. PMID 31359422 DOI: 10.1002/1873-3468.13556 |
0.377 |
|
2018 |
Brew K. Reflections on the evolution of the vertebrate tissue inhibitors of metalloproteinases. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. fj201801262R. PMID 30125136 DOI: 10.1096/Fj.201801262R |
0.497 |
|
2016 |
Zou H, Wu Y, Brew K. Thermodynamic basis of selectivity in the interactions of tissue inhibitors of metalloproteinases N-domains with matrix metalloproteinases -1, -3 and -14. The Journal of Biological Chemistry. PMID 27033700 DOI: 10.1074/Jbc.M116.720250 |
0.516 |
|
2015 |
Lizotte-Waniewski M, Brew K, Hennekens CH. Hypothesis: Metalloproteinase Inhibitors Decrease Risks of Cardiovascular Disease. Journal of Cardiovascular Pharmacology and Therapeutics. PMID 26703451 DOI: 10.1177/1074248415615237 |
0.442 |
|
2014 |
Pham TT, Stinson B, Thiyagarajan N, Lizotte-Waniewski M, Brew K, Acharya KR. Structures of complexes of a metal-independent glycosyltransferase GT6 from Bacteroides ovatus with UDP-N-acetylgalactosamine (UDP-GalNAc) and its hydrolysis products. The Journal of Biological Chemistry. 289: 8041-50. PMID 24459149 DOI: 10.1074/Jbc.M113.545384 |
0.528 |
|
2012 |
Thiyagarajan N, Pham TT, Stinson B, Sundriyal A, Tumbale P, Lizotte-Waniewski M, Brew K, Acharya KR. Structure of a metal-independent bacterial glycosyltransferase that catalyzes the synthesis of histo-blood group A antigen. Scientific Reports. 2: 940. PMID 23230506 DOI: 10.1038/Srep00940 |
0.766 |
|
2011 |
Bahudhanapati H, Zhang Y, Sidhu SS, Brew K. Phage display of tissue inhibitor of metalloproteinases-2 (TIMP-2): identification of selective inhibitors of collagenase-1 (metalloproteinase 1 (MMP-1)). The Journal of Biological Chemistry. 286: 31761-70. PMID 21715326 DOI: 10.1074/Jbc.M111.253328 |
0.815 |
|
2011 |
Wu Y, Wei S, Van Doren SR, Brew K. Entropy increases from different sources support the high-affinity binding of the N-terminal inhibitory domains of tissue inhibitors of metalloproteinases to the catalytic domains of matrix metalloproteinases-1 and -3. The Journal of Biological Chemistry. 286: 16891-9. PMID 21454617 DOI: 10.1074/Jbc.M111.222307 |
0.703 |
|
2010 |
Brew K, Tumbale P, Acharya KR. Family 6 glycosyltransferases in vertebrates and bacteria: inactivation and horizontal gene transfer may enhance mutualism between vertebrates and bacteria. The Journal of Biological Chemistry. 285: 37121-7. PMID 20870714 DOI: 10.1074/Jbc.R110.176248 |
0.748 |
|
2010 |
Lim NH, Kashiwagi M, Visse R, Jones J, Enghild JJ, Brew K, Nagase H. Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications. The Biochemical Journal. 431: 113-22. PMID 20645923 DOI: 10.1042/Bj20100725 |
0.592 |
|
2010 |
Brew K, Nagase H. The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochimica Et Biophysica Acta. 1803: 55-71. PMID 20080133 DOI: 10.1016/J.Bbamcr.2010.01.003 |
0.652 |
|
2010 |
FANG J, LI J, CHEN X, ZHANG Y, WANG J, GUO Z, ZHANG W, YU L, BREW K, WANG PG. ChemInform Abstract: Highly Efficient Chemoenzymatic Synthesis of α-Galactosyl Epitopes with a Recombinant α(1→3)-Galactosyltransferase. Cheminform. 29: no-no. DOI: 10.1002/chin.199845215 |
0.479 |
|
2009 |
Ould-yahoui A, Tremblay E, Sbai O, Ferhat L, Bernard A, Charrat E, Gueye Y, Lim NH, Brew K, Risso JJ, Dive V, Khrestchatisky M, Rivera S. A new role for TIMP-1 in modulating neurite outgrowth and morphology of cortical neurons. Plos One. 4: e8289. PMID 20011518 DOI: 10.1371/Journal.Pone.0008289 |
0.441 |
|
2009 |
Tumbale P, Brew K. Characterization of a metal-independent CAZy family 6 glycosyltransferase from Bacteroides ovatus. The Journal of Biological Chemistry. 284: 25126-34. PMID 19622749 DOI: 10.1074/Jbc.M109.033878 |
0.76 |
|
2009 |
Jamaluddin H, Tumbale P, Ferns TA, Thiyagarajan N, Brew K, Acharya KR. Crystal structure of alpha-1,3-galactosyltransferase (alpha3GT) in a complex with p-nitrophenyl-beta-galactoside (pNPbetaGal). Biochemical and Biophysical Research Communications. 385: 601-4. PMID 19486884 DOI: 10.1016/J.Bbrc.2009.05.111 |
0.782 |
|
2008 |
Tumbale P, Jamaluddin H, Thiyagarajan N, Acharya KR, Brew K. Screening a limited structure-based library identifies UDP-GalNAc-specific mutants of alpha-1,3-galactosyltransferase. Glycobiology. 18: 1036-43. PMID 18782853 DOI: 10.1093/Glycob/Cwn083 |
0.796 |
|
2008 |
Tumbale P, Jamaluddin H, Thiyagarajan N, Brew K, Acharya KR. Structural basis of UDP-galactose binding by alpha-1,3-galactosyltransferase (alpha3GT): role of negative charge on aspartic acid 316 in structure and activity. Biochemistry. 47: 8711-8. PMID 18651752 DOI: 10.1021/Bi800852A |
0.801 |
|
2008 |
Van Doren SR, Wei S, Gao G, DaGue BB, Palmier MO, Bahudhanapati H, Brew K. Inactivation of N-TIMP-1 by N-terminal acetylation when expressed in bacteria. Biopolymers. 89: 960-8. PMID 18615493 DOI: 10.1002/Bip.21043 |
0.812 |
|
2008 |
Lauer-Fields JL, Whitehead JK, Li S, Hammer RP, Brew K, Fields GB. Selective modulation of matrix metalloproteinase 9 (MMP-9) functions via exosite inhibition. The Journal of Biological Chemistry. 283: 20087-95. PMID 18499673 DOI: 10.1074/Jbc.M801438200 |
0.768 |
|
2008 |
Zhao Y, Lyons CE, Xiao A, Templeton DJ, Sang QA, Brew K, Hussaini IM. Urokinase directly activates matrix metalloproteinases-9: a potential role in glioblastoma invasion. Biochemical and Biophysical Research Communications. 369: 1215-20. PMID 18355442 DOI: 10.1016/J.Bbrc.2008.03.038 |
0.474 |
|
2008 |
Jacobsen J, Visse R, Sørensen HP, Enghild JJ, Brew K, Wewer UM, Nagase H. Catalytic properties of ADAM12 and its domain deletion mutants. Biochemistry. 47: 537-47. PMID 18081311 DOI: 10.1021/Bi701629C |
0.627 |
|
2008 |
Cudic M, Patel DA, Lauer-Fields JL, Brew K, Fields GB. Development of a convenient peptide-based assay for lysyl hydroxylase. Biopolymers. 90: 330-8. PMID 17610258 DOI: 10.1002/Bip.20799 |
0.659 |
|
2008 |
Jamaluddin H, Tumbale P, Withers SG, Acharya KR, Brew K. Corrigendum to "Conformational Changes Induced by Binding of UDP-2F-galactose to α-1,3 Galactosyltransferase-Implications for Catalysis" [J. Mol. Biol. 369 (2007) 1270-1281] (DOI:10.1016/j.jmb.2007.04.012) Journal of Molecular Biology. 378: 295-296. DOI: 10.1016/J.Jmb.2008.02.030 |
0.77 |
|
2007 |
Lauer-Fields JL, Minond D, Brew K, Fields GB. Application of topologically constrained mini-proteins as ligands, substrates, and inhibitors. Methods in Molecular Biology (Clifton, N.J.). 386: 125-66. PMID 18604945 DOI: 10.1007/978-1-59745-430-8_5 |
0.732 |
|
2007 |
Crabtree B, Thiyagarajan N, Prior SH, Wilson P, Iyer S, Ferns T, Shapiro R, Brew K, Subramanian V, Acharya KR. Characterization of human angiogenin variants implicated in amyotrophic lateral sclerosis. Biochemistry. 46: 11810-8. PMID 17900154 DOI: 10.1021/Bi701333H |
0.442 |
|
2007 |
Kopitz C, Gerg M, Bandapalli OR, Ister D, Pennington CJ, Hauser S, Flechsig C, Krell HW, Antolovic D, Brew K, Nagase H, Stangl M, von Weyhern CW, Brücher BL, Brand K, et al. Tissue inhibitor of metalloproteinases-1 promotes liver metastasis by induction of hepatocyte growth factor signaling. Cancer Research. 67: 8615-23. PMID 17875701 DOI: 10.1158/0008-5472.Can-07-0232 |
0.55 |
|
2007 |
Lauer-Fields J, Brew K, Whitehead JK, Li S, Hammer RP, Fields GB. Triple-helical transition state analogues: a new class of selective matrix metalloproteinase inhibitors. Journal of the American Chemical Society. 129: 10408-17. PMID 17672455 DOI: 10.1021/Ja0715849 |
0.763 |
|
2007 |
Hamze AB, Wei S, Bahudhanapati H, Kota S, Acharya KR, Brew K. Constraining specificity in the N-domain of tissue inhibitor of metalloproteinases-1; gelatinase-selective inhibitors. Protein Science : a Publication of the Protein Society. 16: 1905-13. PMID 17660250 DOI: 10.1110/Ps.072978507 |
0.767 |
|
2007 |
Lauer-Fields JL, Cudic M, Wei S, Mari F, Fields GB, Brew K. Engineered sarafotoxins as tissue inhibitor of metalloproteinases-like matrix metalloproteinase inhibitors. The Journal of Biological Chemistry. 282: 26948-55. PMID 17626018 DOI: 10.1074/Jbc.M611612200 |
0.816 |
|
2007 |
Jamaluddin H, Tumbale P, Withers SG, Acharya KR, Brew K. Conformational Changes Induced by Binding UDP-2F-galactose to α-1,3 Galactosyltransferase- Implications for Catalysis Journal of Molecular Biology. 369: 1270-1281. PMID 17493636 DOI: 10.1016/J.Jmb.2007.04.012 |
0.8 |
|
2007 |
Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Moss ML, Fields GB. Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences. Biochemistry. 46: 3724-33. PMID 17338550 DOI: 10.1021/Bi062199J |
0.768 |
|
2007 |
Iyer S, Wei S, Brew K, Acharya KR. Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1. The Journal of Biological Chemistry. 282: 364-71. PMID 17050530 DOI: 10.1074/Jbc.M607625200 |
0.778 |
|
2006 |
Minond D, Lauer-Fields JL, Cudic M, Overall CM, Pei D, Brew K, Visse R, Nagase H, Fields GB. The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity. The Journal of Biological Chemistry. 281: 38302-13. PMID 17065155 DOI: 10.1074/Jbc.M606004200 |
0.795 |
|
2005 |
Cui T, Wei S, Brew K, Leng F. Energetics of binding the mammalian high mobility group protein HMGA2 to poly(dA-dT)2 and poly(dA)-poly(dT). Journal of Molecular Biology. 352: 629-45. PMID 16109425 DOI: 10.1016/J.Jmb.2005.07.048 |
0.611 |
|
2005 |
Wei S, Kashiwagi M, Kota S, Xie Z, Nagase H, Brew K. Reactive site mutations in tissue inhibitor of metalloproteinase-3 disrupt inhibition of matrix metalloproteinases but not tumor necrosis factor-alpha-converting enzyme. The Journal of Biological Chemistry. 280: 32877-82. PMID 16079149 DOI: 10.1074/Jbc.C500220200 |
0.786 |
|
2005 |
Azzarolo AM, Brew K, Ponomareva O, Zylberberg C, Vellala K. Expression of MMP-2 and MMP-9 in Lacrimal Gland of New Zealand White Rabbits: Up-Regulation by Estrogen The Ocular Surface. 3: S45. DOI: 10.1016/S1542-0124(12)70350-6 |
0.423 |
|
2004 |
Zhang Y, Deshpande A, Xie Z, Natesh R, Acharya KR, Brew K. Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase. Glycobiology. 14: 1295-302. PMID 15229192 DOI: 10.1093/Glycob/Cwh119 |
0.695 |
|
2004 |
Azzarolo AM, Brew K, Kota S, Ponomareva O, Schwartz J, Zylberberg C. Presence of tear lipocalin and other major proteins in lacrimal fluid of rabbits. Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 138: 111-7. PMID 15193265 DOI: 10.1016/J.Cbpc.2004.02.012 |
0.306 |
|
2003 |
Zhang Y, Swaminathan GJ, Deshpande A, Boix E, Natesh R, Xie Z, Acharya KR, Brew K. Roles of individual enzyme-substrate interactions by alpha-1,3-galactosyltransferase in catalysis and specificity. Biochemistry. 42: 13512-21. PMID 14621997 DOI: 10.1021/Bi035430R |
0.684 |
|
2003 |
Nagase H, Brew K. Designing TIMP (tissue inhibitor of metalloproteinases) variants that are selective metalloproteinase inhibitors. Biochemical Society Symposium. 201-12. PMID 14587293 DOI: 10.1042/Bss0700201 |
0.676 |
|
2003 |
Wei S, Xie Z, Filenova E, Brew K. Drosophila TIMP is a potent inhibitor of MMPs and TACE: similarities in structure and function to TIMP-3. Biochemistry. 42: 12200-7. PMID 14567681 DOI: 10.1021/Bi035358X |
0.743 |
|
2003 |
Greene LH, Hamada D, Eyles SJ, Brew K. Conserved signature proposed for folding in the lipocalin superfamily. Febs Letters. 553: 39-44. PMID 14550543 DOI: 10.1016/S0014-5793(03)00925-6 |
0.321 |
|
2003 |
Brew K. Structure of human ACE gives new insights into inhibitor binding and design. Trends in Pharmacological Sciences. 24: 391-4. PMID 12915047 DOI: 10.1016/S0165-6147(03)00196-2 |
0.333 |
|
2003 |
Arumugam S, Gao G, Patton BL, Semenchenko V, Brew K, Van Doren SR. Increased backbone mobility in beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3. Journal of Molecular Biology. 327: 719-34. PMID 12634064 DOI: 10.1016/S0022-2836(03)00180-3 |
0.438 |
|
2003 |
Wei S, Chen Y, Chung L, Nagase H, Brew K. Protein engineering of the tissue inhibitor of metalloproteinase 1 (TIMP-1) inhibitory domain. In search of selective matrix metalloproteinase inhibitors. The Journal of Biological Chemistry. 278: 9831-4. PMID 12515831 DOI: 10.1074/Jbc.M211793200 |
0.767 |
|
2003 |
Murphy F, Zhou X, Issa R, Hussain H, Waung J, Patel N, Collins J, Brew K, Nagase H, Arthur M, Benyon R, Iredale J. The Balance of TIMPs and MMP-2 Determines Hepatic Stellate Cell Fate during Recovery from Liver Fibrosis Clinical Science. 104: 2P-3P. DOI: 10.1042/cs104002Pc |
0.484 |
|
2002 |
Troeberg L, Tanaka M, Wait R, Shi YE, Brew K, Nagase H. E. coli expression of TIMP-4 and comparative kinetic studies with TIMP-1 and TIMP-2: insights into the interactions of TIMPs and matrix metalloproteinase 2 (gelatinase A). Biochemistry. 41: 15025-35. PMID 12475252 DOI: 10.1021/Bi026454L |
0.659 |
|
2002 |
Nagase H, Brew K. Engineering of tissue inhibitor of metalloproteinases mutants as potential therapeutics. Arthritis Research. 4: S51-61. PMID 12110123 DOI: 10.1186/Ar573 |
0.641 |
|
2002 |
Boix E, Zhang Y, Swaminathan GJ, Brew K, Acharya KR. Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase. The Journal of Biological Chemistry. 277: 28310-8. PMID 12011052 DOI: 10.1074/Jbc.M202631200 |
0.684 |
|
2002 |
Nagase H, Chung L, Brew K. Mechanisms of action of collagenases and TIMPs Biochemical Society Transactions. 30: A21-A21. DOI: 10.1042/Bst030A021A |
0.435 |
|
2001 |
Greene LH, Chrysina ED, Irons LI, Papageorgiou AC, Acharya KR, Brew K. Role of conserved residues in structure and stability: Tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily Protein Science. 10: 2301-2316. PMID 11604536 DOI: 10.1110/Ps.22901 |
0.508 |
|
2001 |
Boix E, Swaminathan GJ, Zhang Y, Natesh R, Brew K, Acharya KR. Structure of UDP complex of UDP-galactose:beta-galactoside-alpha -1,3-galactosyltransferase at 1.53-A resolution reveals a conformational change in the catalytically important C terminus. The Journal of Biological Chemistry. 276: 48608-14. PMID 11592969 DOI: 10.1074/Jbc.M108828200 |
0.55 |
|
2001 |
Kashiwagi M, Tortorella M, Nagase H, Brew K. TIMP-3 Is a Potent Inhibitor of Aggrecanase 1 (ADAM-TS4) and Aggrecanase 2 (ADAM-TS5) Journal of Biological Chemistry. 276: 12501-12504. PMID 11278243 DOI: 10.1074/Jbc.C000848200 |
0.645 |
|
2001 |
Zhang Y, Wang PG, Brew K. Specificity and Mechanism of Metal Ion Activation in UDP-galactose:β -Galactoside-α-1,3-galactosyltransferase Journal of Biological Chemistry. 276: 11567-11574. PMID 11133981 DOI: 10.1074/Jbc.M006530200 |
0.605 |
|
2000 |
Yu WH, Yu SSC, Meng Q, Brew K, Woessner JF. TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix Journal of Biological Chemistry. 275: 31226-31232. PMID 10900194 DOI: 10.1074/Jbc.M000907200 |
0.46 |
|
2000 |
Chrysina ED, Brew K, Acharya KR. Crystal structures of Apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions Journal of Biological Chemistry. 275: 37021-37029. PMID 10896943 DOI: 10.1074/jbc.M004752200 |
0.41 |
|
2000 |
Brew K, Dinakarpandian D, Nagase H. Tissue inhibitors of metalloproteinases: Evolution, structure and function Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1477: 267-283. PMID 10708863 DOI: 10.1016/S0167-4838(99)00279-4 |
0.665 |
|
2000 |
Wu B, Arumugam S, Gao G, Lee GI, Semenchenko V, Huang W, Brew K, Van Doren SR. NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases. Journal of Molecular Biology. 295: 257-68. PMID 10623524 DOI: 10.1006/Jmbi.1999.3362 |
0.515 |
|
1999 |
Wu B, Arumugam S, Huang W, Brew K, Van Doren SR. Letter to the editor: 1H, 13C and 15N resonance assignments and secondary structure of the N-terminal domain of human tissue inhibitor of metalloproteinases-1 Journal of Biomolecular Nmr. 14: 289-290. PMID 10481281 DOI: 10.1023/A:1008310807946 |
0.494 |
|
1999 |
Greene LH, Grobler JA, Malinovskii VA, Tian J, Acharya KR, Brew K. Stability, activity and flexibility in α-lactalbumin Protein Engineering. 12: 581-587. PMID 10436084 |
0.414 |
|
1999 |
Nagase H, Meng Q, Malinovskii V, Huang W, Chung L, Bode W, Maskos K, Brew K. Engineering of selective TIMPs Annals of the New York Academy of Sciences. 878: 1-11. PMID 10415716 DOI: 10.1111/J.1749-6632.1999.Tb07670.X |
0.678 |
|
1999 |
Zhang Y, Malinovskii VA, Fiedler TJ, Brew K. Role of a conserved acidic cluster in bovine β1,4 galactosyltransferase-1 probed by mutagenesis of a bacterially expressed recombinant enzyme Glycobiology. 9: 815-822. PMID 10406847 DOI: 10.1093/Glycob/9.8.815 |
0.601 |
|
1999 |
Forge V, Wijesinha RT, Balbach J, Brew K, Robinson CV, Redfield C, Dobson CM. Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin Journal of Molecular Biology. 288: 673-688. PMID 10329172 DOI: 10.1006/Jmbi.1999.2687 |
0.334 |
|
1999 |
Meng Q, Malinovskii V, Huang W, Hu Y, Chung L, Nagase H, Bode W, Maskos K, Brew K. Residue 2 of TIMP-1 is a major determinant of affinity and specificity for matrix metalloproteinases but effects of substitutions do not correlate with those of the corresponding P1' residue of substrate Journal of Biological Chemistry. 274: 10184-10189. PMID 10187802 DOI: 10.1074/Jbc.274.15.10184 |
0.676 |
|
1998 |
Chandra N, Brew K, Acharya KR. Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Biochemistry. 37: 4767-72. PMID 9537992 DOI: 10.1021/Bi973000T |
0.473 |
|
1998 |
Suzuki K, Kan CC, Hung W, Gehring MR, Brew K, Nagase H. Expression of human pro-matrix metalloproteinase 3 that lacks the N-terminal 34 residues in Escherichia coli autoactivation and interaction with tissue inhibitor of metalloproteinase 1 (TIMP-1) Biological Chemistry. 379: 185-191. PMID 9524070 DOI: 10.1515/Bchm.1998.379.2.185 |
0.648 |
|
1998 |
Fang J, Li J, Chen X, Zhang Y, Wang J, Guo Z, Zhang W, Yu L, Brew K, Wang PG. Highly efficient chemoenzymatic synthesis of α-galactosyl epitopes with a recombinant α(1→3)-galactosyltransferase Journal of the American Chemical Society. 120: 6635-6638. DOI: 10.1021/Ja9808898 |
0.555 |
|
1997 |
Gomis-Rüth FX, Maskos K, Betz M, Bergner A, Huber R, Suzuki K, Yoshida N, Nagase H, Brew K, Bourenkov GP, Bartunik H, Bode W. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature. 389: 77-81. PMID 9288970 DOI: 10.1038/37995 |
0.667 |
|
1997 |
Huang W, Meng Q, Suzuki K, Nagase H, Brew K. Mutational study of the amino-terminal domain of human tissue inhibitor of metalloproteinases 1 (TIMP-1) locates an inhibitory region for matrix metalloproteinases Journal of Biological Chemistry. 272: 22086-22091. PMID 9268350 DOI: 10.1074/Jbc.272.35.22086 |
0.669 |
|
1997 |
Nagase H, Suzuki K, Cawston TE, Brew K. Involvement of a region near valine-69 of tissue inhibitor of metalloproteinases (TIMP)-1 in the interaction with matrix metalloproteinase 3 (stromelysin 1) Biochemical Journal. 325: 163-167. PMID 9224642 DOI: 10.1042/Bj3250163 |
0.671 |
|
1997 |
Huang W, Nagase H, Brew K. Mutation studies of n-terminal domain of human TIMP-1 indicate an inhibitory region for MMP Protein Engineering. 10: 48. |
0.312 |
|
1996 |
Balbach J, Forge V, Lau WS, van Nuland NA, Brew K, Dobson CM. Protein folding monitored at individual residues during a two-dimensional NMR experiment. Science (New York, N.Y.). 274: 1161-3. PMID 8895458 DOI: 10.1126/Science.274.5290.1161 |
0.3 |
|
1996 |
Nagase H, Suzuki K, Itoh Y, Kan CC, Gehring MR, Huang W, Brew K. Involvement of tissue inhibitors of metalloproteinases (TIMPs) during matrix metalloproteinase activation Advances in Experimental Medicine and Biology. 389: 23-31. PMID 8860990 DOI: 10.1007/978-1-4613-0335-0_3 |
0.603 |
|
1996 |
Pike ACW, Brew K, Acharya KR. Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase Structure. 4: 691-703. PMID 8805552 DOI: 10.1016/S0969-2126(96)00075-5 |
0.527 |
|
1996 |
Malinovskii VA, Tian J, Grobler JA, Brew K. Functional site in α-lactalbumin encompasses a region corresponding to a subsite in lysozyme and parts of two adjacent flexible substructures Biochemistry. 35: 9710-9715. PMID 8703942 DOI: 10.1021/Bi960437C |
0.355 |
|
1996 |
Zhang J, Zhang Z, Brew K, Lee EYC. Mutational analysis of the catalytic subunit of muscle protein phosphatase-1 Biochemistry. 35: 6276-6282. PMID 8639569 DOI: 10.1021/Bi952954L |
0.302 |
|
1996 |
Huang W, Suzuki K, Nagase H, Arumugam S, Van Doren SR, Brew K. Folding and characterization of the amino-terminal domain of human tissue inhibitor of metalloproteinases-1 (TIMP-1) expressed at high yield in E. coli Febs Letters. 384: 155-161. PMID 8612814 DOI: 10.1016/0014-5793(96)00304-3 |
0.612 |
|
1996 |
Bradshaw RA, Brew K, Fellows RE, Paulson J, Shaper J, Vanaman TC. Symposium on structure, function and evolution of glycoproteins and related molecules Glycobiology. 6: 647-647. DOI: 10.1093/Glycob/6.7.647-D |
0.708 |
|
1994 |
Grobler JA, Rao KR, Pervaiz S, Brew K. Sequences of two highly divergent canine type c lysozymes: Implications for the evolutionary origins of the lysozyme/α-lactalbumin superfamily Archives of Biochemistry and Biophysics. 313: 360-366. PMID 8080284 DOI: 10.1006/Abbi.1994.1399 |
0.318 |
|
1994 |
Yadav SP, Brew K, Puett D. Holoprotein formation of human chorionic gonadotropin: Differential trace labeling with acetic anhydride Molecular Endocrinology. 8: 1547-1558. PMID 7877623 DOI: 10.1210/Mend.8.11.7877623 |
0.309 |
|
1993 |
Zhang J, Xia WL, Brew K, Ahmad F. Adipose pyruvate carboxylase: Amino acid sequence and domain structure deduced from cDNA sequencing Proceedings of the National Academy of Sciences of the United States of America. 90: 1766-1770. PMID 8446588 DOI: 10.1073/Pnas.90.5.1766 |
0.333 |
|
1993 |
Huberman A, Aguilar MB, Brew K, Shabanowitz J, Hunt DF. Primary structure of the major isomorph of the crustacean hyperglycemic hormone (CHH-I) from the sinus gland of the Mexican crayfish Procambarus bouvieri (Ortmann): interspecies comparison. Peptides. 14: 7-16. PMID 8441709 DOI: 10.1016/0196-9781(93)90004-Z |
0.326 |
|
1992 |
Brandt NR, Caswell AH, Brandt T, Brew K, Mellgren RL. Mapping of the calpain proteolysis products of the junctional foot protein of the skeletal muscle triad junction The Journal of Membrane Biology. 127: 35-47. PMID 1328642 DOI: 10.1007/Bf00232756 |
0.349 |
|
1989 |
Enghild JJ, Salvesen G, Brew K, Nagase H. Interaction of human rheumatoid synovial collagenase (Matrix metalloproteinase 1) and stromelysin (Matrix metalloproteinase 3) with human α2-macroglobulin and chicken ovostatin Journal of Biological Chemistry. 264: 8779-8785. PMID 2470748 |
0.375 |
|
1988 |
Clerch LB, Whitney P, Hass M, Brew K, Miller T, Werner R, Massaro D. Sequence of a full-length cDNA for rat lung beta-galactoside-binding protein: primary and secondary structure of the lectin. Biochemistry. 27: 692-9. PMID 3349058 DOI: 10.1021/Bi00402A030 |
0.317 |
|
1987 |
Nagase H, Brew K. Amino acid sequence of a 32-residue region around the thiol ester site in duck ovostatin Febs Letters. 222: 83-88. PMID 3653403 DOI: 10.1016/0014-5793(87)80196-5 |
0.535 |
|
1987 |
Pervaiz S, Brew K. Homology and structure-function correlations between α1-acid glycoprotein and serum retinol-binding protein and its relatives Faseb Journal. 1: 209-214. PMID 3622999 DOI: 10.1096/Fasebj.1.3.3622999 |
0.336 |
|
1987 |
Hunt DF, Yates JR, Shabanowitz J, Zhu NZ, Zirino T, Averill BA, Daurat-Larroque ST, Shewale JG, Roberts RM, Brew K. Sequence homology in the metalloproteins; purple acid phosphatase from beef spleen and uteroferrin from porcine uterus. Biochemical and Biophysical Research Communications. 144: 1154-60. PMID 3579955 DOI: 10.1016/0006-291X(87)91432-X |
0.3 |
|
1987 |
Jackson AE, Carraway KL, Payne ME, Means AR, Puett D, Brew K. Association of calmodulin and smooth muscle myosin light chain kinase: application of a label selection technique with trace acetylated calmodulin. Proteins. 2: 202-9. PMID 3128785 DOI: 10.1002/Prot.340020305 |
0.311 |
|
1986 |
Pervaiz S, Brew K. Purification and characterization of the major whey proteins from the milks of the bottlenose dolphin (Tursiops truncatus), the Florida manatee (Trichechus manatus latirostris), and the beagle (Canis familiaris) Archives of Biochemistry and Biophysics. 246: 846-854. PMID 3707136 DOI: 10.1016/0003-9861(86)90341-3 |
0.331 |
|
1986 |
Narimatsu H, Sinha S, Brew K, Okayama H, Qasba PK. Cloning and sequencing of cDNA of bovine N-acetylglucosamine (β1-4)galactosyltransferase Proceedings of the National Academy of Sciences of the United States of America. 83: 4720-4724. PMID 3014508 DOI: 10.1073/Pnas.83.13.4720 |
0.316 |
|
1982 |
MacGillivray RTA, Mendez E, Sinha SK, Sutton MR, Lineback-Zins J, Brew K. The complete amino acid sequence of human serum transferrin Proceedings of the National Academy of Sciences of the United States of America. 79: 2504-2508. PMID 6953407 DOI: 10.1073/Pnas.79.8.2504 |
0.35 |
|
1979 |
Macgillivray RTA, Brew K, Barnes K. The amino acid sequence of goat α-lactalbumin Archives of Biochemistry and Biophysics. 197: 404-414. PMID 507821 DOI: 10.1016/0003-9861(79)90262-5 |
0.314 |
|
1976 |
Brew K. Affinity labeling of bovine colostrum galactosyltransferase with a uridine 5′-diphosphate derivative Biochemistry. 15: 3499-3505. PMID 952873 DOI: 10.1021/Bi00661A016 |
0.341 |
|
1975 |
PRIEELS J‐, DOLMANS M, LEONIS J, BREW K. Nitration of Tyrosyl Residues in Human α‐Lactalbumin: Effect on Lactose Synthase Specifier Activity European Journal of Biochemistry. 60: 533-539. PMID 812700 DOI: 10.1111/J.1432-1033.1975.Tb21032.X |
0.358 |
|
1975 |
Hill RL, Brew K. Lactose synthetase. Advances in Enzymology and Related Areas of Molecular Biology. 43: 411-90. PMID 812340 DOI: 10.1002/9780470122884.ch5 |
0.402 |
|
1975 |
Brew K, Hill RL. Lactose biosynthesis Reviews of Physiology Biochemistry and Pharmacology. 72: 105-158. PMID 806951 DOI: 10.1007/bfb0031548 |
0.384 |
|
1975 |
Brew K, Shaper JH, Olsen KW, Trayer IP, Hill RL. Cross-linking of the components of lactose synthetase with dimethylpimelimidate. The Journal of Biological Chemistry. 250: 1434-44. PMID 234456 |
0.579 |
|
1974 |
POWELL JT, BREW K. The Preparation and Characterization of Two Forms of Bovine Galactosyl Transferase European Journal of Biochemistry. 48: 217-228. PMID 4217276 DOI: 10.1111/J.1432-1033.1974.Tb03759.X |
0.316 |
|
1974 |
Khatra BS, Herries DG, Brew K. Some kinetic properties human milk galactosyl transferase European Journal of Biochemistry. 44: 537-560. PMID 4209349 DOI: 10.1111/J.1432-1033.1974.Tb03513.X |
0.328 |
|
1973 |
Sommers PB, Kronman MJ, Brew K. Molecular conformation and fluorescence properties of α lactalbumin from four animal species Biochemical and Biophysical Research Communications. 52: 98-105. PMID 4736474 DOI: 10.1016/0006-291X(73)90959-5 |
0.3 |
|
1972 |
Findlay JBC, Brew K. The Complete Amino‐Acid Sequence of Human α‐Lactalbumin European Journal of Biochemistry. 27: 65-86. PMID 5049057 DOI: 10.1111/J.1432-1033.1972.Tb01812.X |
0.3 |
|
1970 |
Vanaman TC, Brew K, Hill RL. The disulfide bonds of bovine alpha-lactalbumin Journal of Biological Chemistry. 245: 4583-4590. PMID 5532232 |
0.556 |
|
1970 |
Brew K, Castellino FJ, Vanaman TC, Hill RL. The complete amino acid sequence of bovine alpha-lactalbumin. The Journal of Biological Chemistry. 245: 4570-82. PMID 5532231 |
0.696 |
|
1969 |
Browne WJ, North AC, Phillips DC, Brew K, Vanaman TC, Hill RL. A possible three-dimensional structure of bovine alpha-lactalbumin based on that of hen's egg-white lysozyme. Journal of Molecular Biology. 42: 65-86. PMID 5817651 DOI: 10.1016/0022-2836(69)90487-2 |
0.625 |
|
1968 |
Hill RL, Brew K, Vanaman TC, Trayer IP, Mattock P. The structure, function, and evolution of alpha-lactalbumin. Brookhaven Symposia in Biology. 21: 139-54. PMID 5719192 |
0.696 |
|
1968 |
Turkington RW, Brew K, Vanaman TC, Hill RL. The hormonal control of lactose synthetase in the developing mouse mammary gland. The Journal of Biological Chemistry. 243: 3382-7. PMID 5656376 |
0.507 |
|
1968 |
Brew K, Vanaman TC, Hill RL. The role of alpha-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction Proceedings of the National Academy of Sciences of the United States of America. 59: 491-497. PMID 5238979 DOI: 10.1073/Pnas.59.2.491 |
0.666 |
|
1967 |
Brew K, Campbell PN. Studies on the biosynthesis of protein by lactating guinea-pig mammary gland. Characteristics of the synthesis of alpha-lactalbumin and total protein by slices and cell-free systems Biochemical Journal. 102: 265-274. PMID 6067664 |
0.339 |
|
1967 |
Brew K, Vanaman TC, Hill RL. Comparison of the amino acid sequence of bovine alpha-lactalbumin and hens egg white lysozyme Journal of Biological Chemistry. 242: 3747-3749. PMID 6038502 |
0.571 |
|
1967 |
Brew K, Campbell PN. The characterization of the whey proteins of guinea-pig milk. The isolation and properties of alpha-lactalbumin Biochemical Journal. 102: 258-264. PMID 6030288 |
0.336 |
|
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