Year |
Citation |
Score |
2021 |
Olivieri C, Walker C, Karamafrooz A, Wang Y, Manu VS, Porcelli F, Blumenthal DK, Thomas DD, Bernlohr DA, Sandford SM, Taylor SS, Veglia G. Defective internal allosteric network imparts dysfunctional ATP/substrate-binding cooperativity in oncogenic chimera of protein kinase A. Communications Biology. 4: 321. PMID 33692454 DOI: 10.1038/s42003-021-01819-6 |
0.302 |
|
2020 |
Olivieri C, Wang Y, Li GC, Subrahmanian MV, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, T Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. Elife. 9. PMID 32338601 DOI: 10.7554/Elife.55607 |
0.416 |
|
2020 |
Olivieri C, Wang Y, Li GC, S MV, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. Author response: Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A Elife. DOI: 10.7554/Elife.55607.Sa2 |
0.341 |
|
2019 |
Gerlits O, Kong X, Cheng X, Wymore T, Blumenthal DK, Taylor P, Radić Z, Kovalevsky A. Productive reorientation of a bound oxime reactivator revealed in room-temperature X-ray structures of native and VX-inhibited human acetylcholinesterase. Journal of Biological Chemistry. 294: 10607-10618. DOI: 10.2210/Pdb6O66/Pdb |
0.315 |
|
2018 |
Kwon SH, Li L, Terry CM, Shiu YT, Moos PJ, Milash BA, Cheung AK, Blumenthal DK. Differential Gene Expression Patterns in Vein Regions Susceptible versus Resistant to Neointimal Hyperplasia. Physiological Genomics. PMID 29750603 DOI: 10.1152/Physiolgenomics.00082.2017 |
0.512 |
|
2018 |
Moon TM, Sheehe JL, Nukareddy P, Nausch LW, Wohlfahrt J, Matthews DE, Blumenthal DK, Dostmann WR. An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric, autoinhibited, and provides a model for activation. The Journal of Biological Chemistry. PMID 29602907 DOI: 10.1074/Jbc.Ra117.000647 |
0.436 |
|
2016 |
Bruystens JG, Wu J, Fortezzo A, Del Rio J, Nielsen C, Blumenthal DK, Rock R, Stefan E, Taylor SS. Structure of a PKA RIα Recurrent Acrodysostosis Mutant Explains Defective cAMP-Dependent Activation. Journal of Molecular Biology. PMID 27825928 DOI: 10.1016/J.Jmb.2016.10.033 |
0.377 |
|
2016 |
Kwon SH, Li L, He Y, Tey JC, Li H, Zhuplatov I, Kim SJ, Terry CM, Blumenthal DK, Shiu YT, Cheung AK. Prevention of Venous Neointimal Hyperplasia by a Multitarget Receptor Tyrosine Kinase Inhibitor. Journal of Vascular Research. 52: 244-256. PMID 26788996 DOI: 10.1159/000442977 |
0.548 |
|
2016 |
González Bardeci N, Caramelo JJ, Blumenthal DK, Rinaldi J, Rossi S, Moreno S. The PKA regulatory subunit from yeast forms a homotetramer: Low-resolution structure of the N-terminal oligomerization domain. Journal of Structural Biology. 193: 141-54. PMID 26687415 DOI: 10.1016/J.Jsb.2015.12.001 |
0.336 |
|
2014 |
Terry CM, Carlson ML, He Y, Ulu A, Morisseau C, Blumenthal DK, Hammock BD, Cheung AK. Aberrant soluble epoxide hydrolase and oxylipin levels in a porcine arteriovenous graft stenosis model. Journal of Vascular Research. 51: 269-82. PMID 25196102 DOI: 10.1159/000365251 |
0.318 |
|
2014 |
Blumenthal DK, Copps J, Smith-Nguyen EV, Zhang P, Heller WT, Taylor SS. The roles of the RIIβ linker and N-terminal cyclic nucleotide-binding domain in determining the unique structures of the type IIβ protein kinase A: a small angle x-ray and neutron scattering study. The Journal of Biological Chemistry. 289: 28505-12. PMID 25112875 DOI: 10.1074/Jbc.M114.584177 |
0.426 |
|
2014 |
Bruystens JG, Wu J, Fortezzo A, Kornev AP, Blumenthal DK, Taylor SS. PKA RIα homodimer structure reveals an intermolecular interface with implications for cooperative cAMP binding and Carney complex disease. Structure (London, England : 1993). 22: 59-69. PMID 24316401 DOI: 10.1016/J.Str.2013.10.012 |
0.381 |
|
2014 |
Zhang P, Copps J, Blumenthal D, Taylor S. Assembly of Protein Kinase a RIIβ Macromolecular Complexes Biophysical Journal. 106: 464a. DOI: 10.1016/J.Bpj.2013.11.2629 |
0.391 |
|
2012 |
Ilouz R, Bubis J, Wu J, Yim YY, Deal MS, Kornev AP, Ma Y, Blumenthal DK, Taylor SS. Localization and quaternary structure of the PKA RIβ holoenzyme. Proceedings of the National Academy of Sciences of the United States of America. 109: 12443-8. PMID 22797896 DOI: 10.1073/Pnas.1209538109 |
0.366 |
|
2012 |
White MA, Cheng X, Tsalkova T, Mei FC, Woods VL, Li S, Liu T, Blumenthal DK. The Many Conformations of Epac2: A Cyclic-AMP Sensing Cellular Regulator Studied Via Solution X-Ray Scattering (SAXS) & Hydrogen Deuterium Exchange Mass Spectrometry Biophysical Journal. 102: 47a. DOI: 10.1016/J.Bpj.2011.11.285 |
0.364 |
|
2011 |
Osborne BW, Menke AT, Blumenthal DK, Dostmann WR. A structural analysis of the regulatory domain from the cGMP-dependent protein kinase Iα Bmc Pharmacology. 11: 53. DOI: 10.1186/1471-2210-11-S1-P53 |
0.416 |
|
2010 |
Jamros MA, Oliveira LC, Whitford PC, Onuchic JN, Adams JA, Blumenthal DK, Jennings PA. Proteins at work: a combined small angle X-RAY scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscape. The Journal of Biological Chemistry. 285: 36121-8. PMID 20801888 DOI: 10.1074/Jbc.M110.116947 |
0.39 |
|
2009 |
Cheng CY, Yang J, Taylor SS, Blumenthal DK. Sensing domain dynamics in protein kinase A-I{alpha} complexes by solution X-ray scattering. The Journal of Biological Chemistry. 284: 35916-25. PMID 19837668 DOI: 10.1074/Jbc.M109.059493 |
0.362 |
|
2009 |
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X. Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. The Journal of Biological Chemistry. 284: 23644-51. PMID 19553663 DOI: 10.1074/Jbc.M109.024950 |
0.347 |
|
2006 |
Zhuplatov SB, Masaki T, Blumenthal DK, Cheung AK. Mechanism of dipyridamole's action in inhibition of venous and arterial smooth muscle cell proliferation. Basic & Clinical Pharmacology & Toxicology. 99: 431-9. PMID 17169124 DOI: 10.1111/J.1742-7843.2006.Pto_516.X |
0.365 |
|
2006 |
Li L, Blumenthal DK, Masaki T, Terry CM, Cheung AK. Differential effects of imatinib on PDGF-induced proliferation and PDGF receptor signaling in human arterial and venous smooth muscle cells. Journal of Cellular Biochemistry. 99: 1553-63. PMID 16817200 DOI: 10.1002/Jcb.20993 |
0.357 |
|
2006 |
Vigil D, Blumenthal DK, Taylor SS, Trewhella J. Solution scattering reveals large differences in the global structures of type II protein kinase A isoforms. Journal of Molecular Biology. 357: 880-9. PMID 16460759 DOI: 10.1016/J.Jmb.2006.01.006 |
0.393 |
|
2006 |
Blumenthal DK. Protein Tyrosine Kinases: From Inhibitors to Useful Drugs European Journal of Haematology. 77: 268-269. DOI: 10.1111/J.1600-0609.2006.00684.X |
0.334 |
|
2005 |
Vigil D, Blumenthal DK, Taylor SS, Trewhella J. The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding. The Journal of Biological Chemistry. 280: 35521-7. PMID 16109722 DOI: 10.1074/Jbc.M506769200 |
0.404 |
|
2004 |
Vigil D, Blumenthal DK, Brown S, Taylor SS, Trewhella J. Differential effects of substrate on type I and type II PKA holoenzyme dissociation. Biochemistry. 43: 5629-36. PMID 15134437 DOI: 10.1021/Bi0499157 |
0.363 |
|
2004 |
Vigil D, Blumenthal DK, Heller WT, Brown S, Canaves JM, Taylor SS, Trewhella J. Conformational differences among solution structures of the type Ialpha, IIalpha and IIbeta protein kinase A regulatory subunit homodimers: role of the linker regions. Journal of Molecular Biology. 337: 1183-94. PMID 15046986 DOI: 10.1016/J.Jmb.2004.02.028 |
0.415 |
|
2004 |
Heller WT, Vigil D, Brown S, Blumenthal DK, Taylor SS, Trewhella J. C subunits binding to the protein kinase A RI alpha dimer induce a large conformational change. The Journal of Biological Chemistry. 279: 19084-90. PMID 14985329 DOI: 10.1074/Jbc.M313405200 |
0.347 |
|
2003 |
Burns LL, Canaves JM, Pennypacker JK, Blumenthal DK, Taylor SS. Isoform specific differences in binding of a dual-specificity A-kinase anchoring protein to type I and type II regulatory subunits of PKA. Biochemistry. 42: 5754-63. PMID 12741833 DOI: 10.1021/Bi0265729 |
0.401 |
|
1999 |
Hernández G, Blumenthal DK, Kennedy MA, Unkefer CJ, Trewhella J. Troponin I inhibitory peptide (96-115) has an extended conformation when bound to skeletal muscle troponin C. Biochemistry. 38: 6911-7. PMID 10346913 DOI: 10.1021/Bi990150Q |
0.317 |
|
1999 |
Vargas G, Yeh TY, Blumenthal DK, Lucero MT. Common components of patch-clamp internal recording solutions can significantly affect protein kinase A activity. Brain Research. 828: 169-73. PMID 10320738 DOI: 10.1016/S0006-8993(99)01306-2 |
0.321 |
|
1998 |
Krueger JK, Bishop NA, Blumenthal DK, Zhi G, Beckingham K, Stull JT, Trewhella J. Calmodulin binding to myosin light chain kinase begins at substoichiometric Ca2+ concentrations: a small-angle scattering study of binding and conformational transitions. Biochemistry. 37: 17810-7. PMID 9922147 DOI: 10.1021/Bi981656W |
0.358 |
|
1997 |
Wangsgard WP, Dasgupta M, Blumenthal DK. Antipeptide Antibodies as Probes of Subunit-Dependent Structural Changes in the Regulatory Domain of the Gamma-Subunit of Phosphorylase Kinase☆ Biochemical and Biophysical Research Communications. 230: 179-183. PMID 9020041 DOI: 10.1006/Bbrc.1996.5927 |
0.388 |
|
1996 |
Wangsgard WP, Meixell GE, Dasgupta M, Blumenthal DK. Activation and inhibition of phosphorylase kinase by monospecific antibodies raised against peptides from the regulatory domain of the gamma-subunit. Journal of Biological Chemistry. 271: 21126-21133. PMID 8702882 DOI: 10.1074/Jbc.271.35.21126 |
0.397 |
|
1995 |
Huang CYF, Yuan CJ, Blumenthal DK, Graves DJ. Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase γ-subunit Journal of Biological Chemistry. 270: 7183-7188. PMID 7706257 DOI: 10.1074/Jbc.270.13.7183 |
0.406 |
|
1995 |
Dasgupta M, Blumenthal DK. Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory. Journal of Biological Chemistry. 270: 22283-22289. PMID 7673209 DOI: 10.1074/Jbc.270.38.22283 |
0.429 |
|
1993 |
Blumenthal DK. Development and characterization of fluorescently-labeled myosin light chain kinase calmodulin-binding domain peptides. Molecular and Cellular Biochemistry. 127: 45-50. PMID 7935361 DOI: 10.1007/Bf01076756 |
0.414 |
|
1991 |
Charbonneau H, Kumar S, Novack JP, Blumenthal DK, Griffin PR, Shabanowitz J, Hunt DF, Beavo JA, Walsh KA. Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain. Biochemistry. 30: 7931-40. PMID 1651111 DOI: 10.1021/Bi00246A009 |
0.395 |
|
1990 |
Trewhella J, Blumenthal DK, Rokop SE, Seeger PA. Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase Biochemistry®. 29: 9316-9324. PMID 2248948 DOI: 10.1021/Bi00492A003 |
0.458 |
|
1989 |
Heidorn DB, Seeger PA, Rokop SE, Blumenthal DK, Means AR, Crespi H, Trewhella J. Changes in the structure of calmodulin induced by a peptide based on the calmodulin-binding domain of myosin light chain kinase. Biochemistry. 28: 6757-64. PMID 2790029 DOI: 10.1021/Bi00442A032 |
0.393 |
|
1989 |
Novack JP, Charbonneau H, Blumenthal DK, Walsh KA, Beavo JA. The domain structure of the calmodulin-dependent phosphodiesterase isozymes Advances in Experimental Medicine and Biology. 255: 387-395. PMID 2618869 DOI: 10.1007/978-1-4684-5679-0_42 |
0.373 |
|
1988 |
Blumenthal DK, Charbonneau H, Edelman AM, Hinds TR, Rosenberg GB, Storm DR, Vincenzi FF, Beavo JA, Krebs EG. Synthetic peptides based on the calmodulin-binding domain of myosin light chain kinase inhibit activation of other calmodulin-dependent enzymes. Biochemical and Biophysical Research Communications. 156: 860-5. PMID 2903735 DOI: 10.1016/S0006-291X(88)80923-9 |
0.435 |
|
1987 |
Blumenthal DK, Krebs EG. Preparation and properties of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. Methods in Enzymology. 139: 115-26. PMID 3587020 DOI: 10.1016/0076-6879(87)39079-2 |
0.369 |
|
1987 |
Edelman AM, Blumenthal DK, Krebs EG. Protein serine/threonine kinases. Annual Review of Biochemistry. 56: 567-613. PMID 2956925 DOI: 10.1146/Annurev.Bi.56.070187.003031 |
0.31 |
|
1987 |
Nunnally MH, Blumenthal DK, Krebs EG, Stull JT. Properties of a monoclonal antibody directed to the calmodulin-binding domain of rabbit skeletal muscle myosin light chain kinase. Biochemistry. 26: 5885-90. PMID 2445376 DOI: 10.1021/Bi00392A046 |
0.403 |
|
1987 |
Kennelly PJ, Takio K, Blumenthal DK, Edelman AM, Glaccum MB, Klevit RE, Roush CL, Scott JD, Titani K, Walsh KA, Krebs EG. Organization Of Myosin Light Chain Kinase From Rabbit Skeletal Muscle Calcium-Binding Proteins in Health and Disease. 494-504. DOI: 10.1016/B978-0-12-521040-9.50091-7 |
0.344 |
|
1987 |
Klevit RE, Blumenthal DK. 1H NMR Studies of Calmodulin-Peptide Interactions Calcium-Binding Proteins in Health and Disease. 333-347. DOI: 10.1016/B978-0-12-521040-9.50059-0 |
0.34 |
|
1986 |
Takio K, Blumenthal DK, Walsh KA, Titani K, Krebs EG. Amino acid sequence of rabbit skeletal muscle myosin light chain kinase. Biochemistry. 25: 8049-57. PMID 3542042 DOI: 10.1021/Bi00372A038 |
0.346 |
|
1985 |
Blumenthal DK, Takio K, Edelman AM, Charbonneau H, Titani K, Walsh KA, Krebs EG. Identification of the calmodulin-binding domain of skeletal muscle myosin light chain kinase. Proceedings of the National Academy of Sciences of the United States of America. 82: 3187-91. PMID 3858814 DOI: 10.1073/Pnas.82.10.3187 |
0.4 |
|
1985 |
Klevit RE, Blumenthal DK, Wemmer DE, Krebs EG. Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formation. Biochemistry. 24: 8152-7. PMID 3841496 DOI: 10.1021/Bi00348A047 |
0.38 |
|
1985 |
Takio K, Blumenthal DK, Edelman AM, Walsh KA, Krebs EG, Titani K. Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase. Biochemistry. 24: 6028-37. PMID 3841288 DOI: 10.1021/Bi00343A002 |
0.394 |
|
1985 |
Stull JT, Nunnally MH, Moore RL, Blumenthal DK. Myosin light chain kinases and myosin phosphorylation in skeletal muscle Advances in Enzyme Regulation. 23: 123-140. PMID 3840948 DOI: 10.1016/0065-2571(85)90043-3 |
0.354 |
|
1982 |
Stull JT, Blumenthal DK, Miller JR, DiSalvo J. Regulation of myosin phosphorylation Journal of Molecular and Cellular Cardiology. 14: 105-110. PMID 6897266 DOI: 10.1016/0022-2828(82)90137-7 |
0.39 |
|
1982 |
Blumenthal DK, Stull JT. Effects of pH, Ionic Strength, and Temperature on Activation by Calmodulin and Catalytic Activity of Myosin Light Chain Kinase Biochemistry. 21: 2386-2391. PMID 6896461 DOI: 10.1021/Bi00539A017 |
0.342 |
|
1980 |
Ritz-Gold CJ, Cooke R, Blumenthal DK, Stull JT. Light chain phosphorylation alters the conformation of skeletal muscle myosin Biochemical and Biophysical Research Communications. 93: 209-214. PMID 6990926 DOI: 10.1016/S0006-291X(80)80267-1 |
0.368 |
|
1980 |
Blumenthal DK, Stull JT. Activation of skeletal muscle myosin light chain kinase by calcium(2+) and calmodulin. Biochemistry. 19: 5608-5614. PMID 6893940 DOI: 10.1021/Bi00565A023 |
0.339 |
|
1980 |
Stull JT, Blumenthal DK, Cooke R. Regulation of contraction by myosin phosphorylation. A comparison between smooth and skeletal muscles. Biochemical Pharmacology. 29: 2537-2543. PMID 6252902 DOI: 10.1016/0006-2952(80)90063-5 |
0.306 |
|
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