| Year |
Citation |
Score |
| 2008 |
Nelsestuen GL, Harvey SB, Zhang Y, Kasthuri RS, Sinaiko AR, Ely EW, Bernard GR, Homoncik M, Jilma B. Top-down proteomic analysis by MALDI-TOF profiling: Concentration-independent biomarkers. Proteomics. Clinical Applications. 2: 158-66. PMID 21136822 DOI: 10.1002/Prca.200780107 |
0.342 |
|
| 2007 |
Kasthuri RS, Wroblewski M, Jilma B, Key NS, Nelsestuen GL. Potential biomarkers of an exaggerated response to endotoxemia. Biomarkers : Biochemical Indicators of Exposure, Response, and Susceptibility to Chemicals. 12: 287-302. PMID 17453742 DOI: 10.1080/13547500601160536 |
0.304 |
|
| 2006 |
Kasthuri RS, Verneris MR, Ibrahim HN, Jilma B, Nelsestuen GL. Studying multiple protein profiles over time to assess biomarker validity. Expert Review of Proteomics. 3: 455-64. PMID 16901203 DOI: 10.1586/14789450.3.4.455 |
0.307 |
|
| 2005 |
Nelsestuen GL, Zhang Y, Martinez MB, Key NS, Jilma B, Verneris M, Sinaiko A, Kasthuri RS. Plasma protein profiling: unique and stable features of individuals. Proteomics. 5: 4012-24. PMID 16130168 DOI: 10.1002/Pmic.200401234 |
0.303 |
|
| 2005 |
Stone MD, Harvey SB, Martinez MB, Bach RR, Nelsestuen GL. Large enhancement of functional activity of active site-inhibited factor VIIa due to protein dimerization: insights into mechanism of assembly/disassembly from tissue factor. Biochemistry. 44: 6321-30. PMID 15835921 DOI: 10.1021/Bi050007Z |
0.41 |
|
| 2005 |
Stone MD, Nelsestuen GL. Efficacy of soluble phospholipids in the prothrombinase reaction. Biochemistry. 44: 4037-41. PMID 15751980 DOI: 10.1021/Bi047655N |
0.387 |
|
| 2005 |
Perez-Pujol S, Anderson LB, Martinez MB, Higgins L, White JG, Nelsestuen GL, Key NS. Proteomic Analysis of Gray Platelet Syndrome by iTRAQ Labelling and Mass Spectroscopy: A Potential New Diagnostic Strategy for Platelet Disorders. Blood. 106: 2161-2161. DOI: 10.1182/Blood.V106.11.2161.2161 |
0.317 |
|
| 2004 |
Kasthuri RS, Hysjulien JL, Norton LE, Rogers T, Jilma B, Key NS, Nelsestuen GL. Plasma Proteome Profiling: Widespread Oxidative Changes in Endotoxemia Correlate with Intravascular Tissue Factor Response. Blood. 104: 2388-2388. DOI: 10.1182/Blood.V104.11.2388.2388 |
0.31 |
|
| 2003 |
Harvey SB, Stone MD, Martinez MB, Nelsestuen GL. Mutagenesis of the gamma-carboxyglutamic acid domain of human factor VII to generate maximum enhancement of the membrane contact site. The Journal of Biological Chemistry. 278: 8363-9. PMID 12506121 DOI: 10.1074/Jbc.M211629200 |
0.385 |
|
| 2002 |
Stone M, Harvey SB, Kisiel W, Foster D, Nelsestuen GL. Unusual benefits of macromolecular shielding by polyethylene glycol for reactions at the diffusional limit: the case of factor VIIai and tissue factor. Biochemistry. 41: 15820-5. PMID 12501211 DOI: 10.1021/Bi0204544 |
0.371 |
|
| 2002 |
Henderson N, Key NS, Christie B, Kisiel W, Foster D, Nelsestuen GL. Response of factor VIII and IX-deficient blood to wild type and high membrane affinity mutant factor VIIa in an in vitro whole blood clotting assay: possible correlation to clinical outcome. Thrombosis and Haemostasis. 88: 98-103. PMID 12152685 DOI: 10.1055/S-0037-1613160 |
0.323 |
|
| 2001 |
Martinez MB, Flickinger M, Higgins LA, Krick T, Nelsestuen GL. Reduced outer membrane permeability of Escherichia coli O157:H7: Suggested role of modified outer membrane porins and theoretical function in resistance to antimicrobial agents Biochemistry. 40: 11965-11974. PMID 11580272 DOI: 10.1021/Bi0109515 |
0.321 |
|
| 2000 |
Nelsestuen GL, Shah AM, Harvey SB. Vitamin K-dependent proteins Vitamins and Hormones Series. 58: 355-389. PMID 10668405 DOI: 10.1016/S0083-6729(00)58031-5 |
0.43 |
|
| 1999 |
Nelsestuen GL. Enhancement of Vitamin-K-Dependent Protein Function by Modification of the γ-Carboxyglutamic Acid Domain: Studies of Protein C and Factor VII Trends in Cardiovascular Medicine. 9: 162-167. PMID 10639722 DOI: 10.1016/S1050-1738(99)00024-9 |
0.424 |
|
| 1999 |
Martinez MB, Flickinger MC, Nelsestuen GL. Steady-state enzyme kinetics in the Escherichia coli periplasm: a model of a whole cell biocatalyst. Journal of Biotechnology. 71: 59-66. PMID 10483101 DOI: 10.1016/S0168-1656(99)00015-2 |
0.326 |
|
| 1999 |
Nelsestuen GL, Ostrowski BG. Membrane association with multiple calcium ions: vitamin-K-dependent proteins, annexins and pentraxins. Current Opinion in Structural Biology. 9: 433-437. PMID 10449363 DOI: 10.1016/S0959-440X(99)80060-8 |
0.409 |
|
| 1998 |
Shen L, Shah AM, Dahlbäck B, Nelsestuen GL. Enhancement of human protein C function by site-directed mutagenesis of the gamma-carboxyglutamic acid domain. The Journal of Biological Chemistry. 273: 31086-91. PMID 9813008 DOI: 10.1074/Jbc.273.47.31086 |
0.458 |
|
| 1998 |
Shah AM, Kisiel W, Foster DC, Nelsestuen GL. Manipulation of the membrane binding site of vitamin K-dependent proteins: Enhanced biological function of human factor VII Proceedings of the National Academy of Sciences of the United States of America. 95: 4229-4234. PMID 9539719 DOI: 10.1073/Pnas.95.8.4229 |
0.389 |
|
| 1998 |
Shen L, Shah AM, Dahlbäck B, Nelsestuen GL. Enhancing the activity of protein C by mutagenesis to improve the membrane-binding site: studies related to proline-10. Biochemistry. 36: 16025-31. PMID 9440875 DOI: 10.1021/Bi971730V |
0.422 |
|
| 1997 |
McDonald JF, Evans TC, Emeagwali DB, Hariharan M, Allewell NM, Pusey ML, Shah AM, Nelsestuen GL. Ionic properties of membrane association by vitamin K-dependent proteins: the case for univalency. Biochemistry. 36: 15589-98. PMID 9398287 DOI: 10.1021/Bi971114Z |
0.376 |
|
| 1997 |
Nelsestuen GL, Martinez MB. Steady State Enzyme Velocities That Are Independent of [Enzyme]: An Important Behavior in Many Membrane and Particle-Bound States† Biochemistry. 36: 9081-9086. PMID 9254133 DOI: 10.1021/Bi970720R |
0.317 |
|
| 1997 |
McDonald JF, Nelsestuen GL. Potent inhibition of terminal complement assembly by clusterin: characterization of its impact on C9 polymerization. Biochemistry. 36: 7464-73. PMID 9200695 DOI: 10.1021/Bi962895R |
0.307 |
|
| 1997 |
McDonald JF, Shah AM, Schwalbe RA, Kisiel W, Dahlbäck B, Nelsestuen GL. Comparison of naturally occurring vitamin K-dependent proteins: correlation of amino acid sequences and membrane binding properties suggests a membrane contact site. Biochemistry. 36: 5120-7. PMID 9136872 DOI: 10.1021/Bi9626160 |
0.432 |
|
| 1996 |
Evans TC, Nelsestuen GL. Importance of cis-proline 22 in the membrane-binding conformation of bovine prothrombin Biochemistry. 35: 8210-8215. PMID 8679575 DOI: 10.1021/Bi9606354 |
0.406 |
|
| 1996 |
Lu Y, Nelsestuen GL. Dynamic features of prothrombin interaction with phospholipid vesicles of different size and composition: implications for protein--membrane contact. Biochemistry. 35: 8193-8200. PMID 8679573 DOI: 10.1021/Bi960280O |
0.385 |
|
| 1996 |
Martinez MB, Flickinger MC, Nelsestuen GL. Accurate kinetic modeling of alkaline phosphatase in the Escherichia coli periplasm: implications for enzyme properties and substrate diffusion. Biochemistry. 35: 1179-86. PMID 8573572 DOI: 10.1021/Bi951955A |
0.302 |
|
| 1995 |
Lu Y, Bazzi MD, Nelsestuen GL. Kinetics of annexin VI, calcium, and phospholipid association and dissociation. Biochemistry. 34: 10777-10785. PMID 7662658 DOI: 10.1021/Bi00034A010 |
0.42 |
|
| 1995 |
Evans TC, Nelsestuen GL. Dissociation of serum amyloid P from C4b-binding protein and other sites by lactic acid: potential role of lactic acid in the regulation of pentraxin function. Biochemistry. 34: 10440-7. PMID 7654697 DOI: 10.1021/Bi00033A016 |
0.383 |
|
| 1995 |
Schwalbe RA, Coe JE, Nelsestuen GL. Association of rat C-reactive protein and other pentraxins with rat lipoproteins containing apolipoproteins E and A1. Biochemistry. 34: 10432-9. PMID 7544614 DOI: 10.1021/Bi00033A015 |
0.301 |
|
| 1994 |
Plager DA, Nelsestuen GL. Direct enthalpy measurements of factor X and prothrombin association with small and large unilamellar vesicles Biochemistry. 33: 7005-7013. PMID 8204634 DOI: 10.1021/Bi00188A033 |
0.41 |
|
| 1994 |
Plager DA, Nelsestuen GL. Direct enthalpy measurements of the calcium-dependent interaction of annexins V and VI with phospholipid vesicles. Biochemistry. 33: 13239-13249. PMID 7947731 DOI: 10.1021/Bi00249A010 |
0.442 |
|
| 1993 |
Bazzi MD, Nelsestuen GL. Protein kinase C and annexins: Unusual calcium response elements in the cell Cellular Signalling. 5: 357-365. PMID 8373720 DOI: 10.1016/0898-6568(93)90075-W |
0.429 |
|
| 1992 |
Bazzi MD, Nelsestuen GL. Interaction of annexin VI with membranes: highly restricted dissipation of clustered phospholipids in membranes containing phosphatidylethanolamine. Biochemistry. 31: 10406-10413. PMID 1420158 DOI: 10.1021/Bi00157A031 |
0.371 |
|
| 1992 |
Schwalbe RA, Dahlbäck B, Coe JE, Nelsestuen GL. Pentraxin family of proteins interact specifically with phosphorylcholine and/or phosphorylethanolamine Biochemistry. 31: 4907-4915. PMID 1375509 DOI: 10.1021/Bi00135A023 |
0.398 |
|
| 1992 |
Xu Cj, Nelsestuen GL. Association of α-phosphatidylinositol-specific phospholipase C with phospholipid vesicles Biochimica Et Biophysica Acta. 1120: 49-58. PMID 1313300 DOI: 10.1016/0167-4838(92)90423-B |
0.44 |
|
| 1992 |
Plager DA, Nelsestuen GL. Dissociation of peripheral protein‐membrane complexes by high pressure Protein Science. 1: 530-539. PMID 1304354 DOI: 10.1002/Pro.5560010408 |
0.424 |
|
| 1991 |
Nelsestuen GL, Bazzi MD. Activation and regulation of protein Kinase C enzymes Journal of Bioenergetics and Biomembranes. 23: 43-61. PMID 2010434 DOI: 10.1007/Bf00768838 |
0.402 |
|
| 1991 |
Bazzi MD, Nelsestuen GL. Proteins that bind calcium in a phospholipid-dependent manner. Biochemistry. 30: 971-979. PMID 1989687 DOI: 10.1021/Bi00218A013 |
0.404 |
|
| 1991 |
Bazzi MD, Nelsestuen GL. Highly sequential binding of protein kinase C and related proteins to membranes. Biochemistry. 30: 7970-7977. PMID 1868071 DOI: 10.1021/Bi00246A014 |
0.446 |
|
| 1991 |
Bazzi MD, Nelsestuen GL. Extensive segregation of acidic phospholipids in membranes induced by protein kinase C and related proteins. Biochemistry. 30: 7961-7969. PMID 1868070 DOI: 10.1021/Bi00246A013 |
0.408 |
|
| 1990 |
Bazzi MD, Nelsestuen GL. Protein kinase C interaction with calcium: a phospholipid-dependent process. Biochemistry. 29: 7624-7630. PMID 2271522 DOI: 10.1021/Bi00485A012 |
0.383 |
|
| 1989 |
Bazzi MD, Nelsestuen GL. Properties of the protein kinase C-phorbol ester interaction. Biochemistry. 28: 3577-3585. PMID 2742855 DOI: 10.1021/Bi00434A064 |
0.415 |
|
| 1989 |
Malinski JA, Nelsestuen GL. Membrane permeability to macromolecules mediated by the membrane attack complex. Biochemistry. 28: 61-70. PMID 2706268 DOI: 10.1021/Bi00427A010 |
0.363 |
|
| 1989 |
Bazzi MD, Nelsestuen GL. Differences in the effects of phorbol esters and diacylglycerols on protein kinase C. Biochemistry. 28: 9317-9323. PMID 2611232 DOI: 10.1021/Bi00450A011 |
0.416 |
|
| 1988 |
Bazzi MD, Nelsestuen GL. Properties of membrane-inserted protein kinase C. Biochemistry. 27: 7589-7593. PMID 3207690 DOI: 10.1021/Bi00420A003 |
0.411 |
|
| 1988 |
Welsch DJ, Nelsestuen GL. Carbohydrate-linked asparagine-101 of prothrombin contains a metal ion protected acetylation site. Acetylation of this site causes loss of metal ion induced protein fluorescence change. Biochemistry. 27: 4946-4952. PMID 3167023 DOI: 10.1021/Bi00413A053 |
0.339 |
|
| 1988 |
Welsch DJ, Nelsestuen GL. Amino-terminal alanine functions in a calcium-specific process essential for membrane binding by prothrombin fragment 1. Biochemistry. 27: 4939-4945. PMID 3167022 DOI: 10.1021/Bi00413A052 |
0.392 |
|
| 1988 |
Welsch DJ, Pletcher CH, Nelsestuen GL. Chemical modification of prothrombin fragment 1: documentation of sequential, two-stage loss of protein function. Biochemistry. 27: 4933-4938. PMID 3167021 DOI: 10.1021/Bi00413A051 |
0.393 |
|
| 1988 |
Bazzi MD, Nelsestuen GL. Association of protein kinase C with phospholipid monolayers: two-stage irreversible binding Biochemistry. 27: 6776-6783. PMID 3143405 DOI: 10.1021/Bi00418A020 |
0.302 |
|
| 1988 |
Bazzi MD, Nelsestuen GL. Constitutive activity of membrane-inserted protein kinase C. Biochemical and Biophysical Research Communications. 152: 336-343. PMID 3128979 DOI: 10.1016/S0006-291X(88)80719-8 |
0.39 |
|
| 1987 |
Cunningham MT, Nelsestuen GL. Comparison of the kinetic behavior of human and bovine proteins in the heparin-catalyzed antithrombin III/thrombin reaction. Biochimica Et Biophysica Acta. 911: 66-70. PMID 3790599 DOI: 10.1016/0167-4838(87)90271-8 |
0.352 |
|
| 1987 |
Bazzi MD, Lampe PD, Strasburg GM, Nelsestuen GL. Phosphorylation of troponin I by protein kinase C: mechanism of inhibition by calmodulin and troponin C. Biochimica Et Biophysica Acta. 931: 339-46. PMID 3676351 DOI: 10.1016/0167-4889(87)90225-4 |
0.323 |
|
| 1987 |
Bazzi MD, Nelsestuen GL. Substrate-specific stimulation of protein kinase C by polyvalent anions Biochemical and Biophysical Research Communications. 147: 248-253. PMID 3632667 DOI: 10.1016/S0006-291X(87)80113-4 |
0.332 |
|
| 1987 |
Bazzi MD, Nelsestuen GL. Mechanism of protein kinase C inhibition by sphingosine Biochemical and Biophysical Research Communications. 146: 203-207. PMID 3606616 DOI: 10.1016/0006-291X(87)90711-X |
0.36 |
|
| 1987 |
Bazzi MD, Nelsestuen GL. Role of substrate in imparting calcium and phospholipid requirements to protein kinase C activation. Biochemistry. 26: 1974-1982. PMID 3593703 DOI: 10.1021/Bi00381A029 |
0.333 |
|
| 1987 |
Bazzi MD, Nelsestuen GL. Role of substrate in determining the phospholipid specificity of protein kinase C activation. Biochemistry. 26: 5002-5008. PMID 3478093 DOI: 10.1021/Bi00390A018 |
0.33 |
|
| 1987 |
Abbott AJ, Nelsestuen GL. Association of a protein with membrane vesicles at the collisional limit: studies with blood coagulation factor Va light chain also suggest major differences between small and large unilamellar vesicles. Biochemistry. 26: 7994-8003. PMID 3427119 DOI: 10.1021/Bi00398A067 |
0.432 |
|
| 1987 |
Bazzi MD, Nelsestuen GL. Association of protein kinase C with phospholipid vesicles. Biochemistry. 26: 115-122. PMID 3103676 DOI: 10.1021/Bi00375A017 |
0.449 |
|
| 1986 |
Silversmith RE, Nelsestuen GL. Assembly of the Membrane Attack Complex of Complement on Small Unilamellar Phospholipid Vesicles Biochemistry. 25: 852-860. PMID 3964649 DOI: 10.1021/Bi00352A017 |
0.36 |
|
| 1986 |
Silversmith RE, Nelsestuen GL. Interaction of complement proteins C5b-6 and C5b-7 with phospholipid vesicles: effects of phospholipid structural features. Biochemistry. 25: 7717-7725. PMID 3801440 DOI: 10.1021/Bi00371A065 |
0.43 |
|
| 1986 |
Griep MA, Fujikawa K, Nelsestuen GL. Possible basis for the apparent surface selectivity of the contact activation of human blood coagulation factor XII. Biochemistry. 25: 6688-94. PMID 3491625 DOI: 10.1021/Bi00369A054 |
0.661 |
|
| 1986 |
Lampe PD, Bazzi MD, Nelsestuen GL, Johnson RG. Phosphorylation of lens intrinsic membrane proteins by protein kinase C. European Journal of Biochemistry / Febs. 156: 351-7. PMID 2422029 DOI: 10.1111/J.1432-1033.1986.Tb09590.X |
0.365 |
|
| 1985 |
Griep MA, Fujikawa K, Nelsestuen GL. Binding and activation properties of human factor XII, prekallikrein, and derived peptides with acidic lipid vesicles. Biochemistry. 24: 4124-30. PMID 3876845 DOI: 10.1021/Bi00336A047 |
0.674 |
|
| 1985 |
Pletcher CH, Cunningham M, Nelsestuen GL. Kinetic analysis of various heparin fractions and heparin substitutes in the thrombin inhibition reaction. Biochimica Et Biophysica Acta. 838: 106-113. PMID 2578296 DOI: 10.1016/0304-4165(85)90256-9 |
0.345 |
|
| 1984 |
Bouhoutsos-Brown E, Pletcher CH, Nelsestuen GL, Bryant RG. Prothrombin fragment 1-membrane interactions: a calcium-43 NMR study. Journal of Inorganic Biochemistry. 21: 337-43. PMID 6548252 DOI: 10.1016/0162-0134(84)85055-2 |
0.36 |
|
| 1984 |
Pusey ML, Nelsestuen GL. Membrane binding properties of blood coagulation Factor V and derived peptides. Biochemistry. 23: 6202-6210. PMID 6441598 DOI: 10.1021/Bi00320A048 |
0.396 |
|
| 1983 |
Pusey ML, Nelsestuen GL. The physical significance of Km in the prothrombinase reaction Biochemical and Biophysical Research Communications. 114: 526-532. PMID 6882441 DOI: 10.1016/0006-291X(83)90812-4 |
0.394 |
|
| 1983 |
Silversmith RE, Wei GJ, Nelsestuen GL. Calcium effects on prothrombin and its reaction with bifunctional alkylating reagents. Biochemical and Biophysical Research Communications. 111: 213-218. PMID 6830590 DOI: 10.1016/S0006-291X(83)80138-7 |
0.364 |
|
| 1983 |
Lampe PD, Wei GJ, Nelsestuen GL. Stopped-flow studies of myelin basic protein association with phospholipid vesicles and subsequent vesicle aggregation. Biochemistry. 22: 1594-9. PMID 6189513 DOI: 10.1021/Bi00276A011 |
0.369 |
|
| 1983 |
Mayer LD, Pusey ML, Griep MA, Nelsestuen GL. Association of blood coagulation factors V and X with phospholipid monolayers Biochemistry. 22: 6226-6232. DOI: 10.1021/Bi00295A029 |
0.628 |
|
| 1983 |
Nelsestuen GL. Calcium involvement in the protein-membrane systems of blood coagulation Inorganica Chimica Acta. 79: 41. DOI: 10.1016/S0020-1693(00)95066-7 |
0.443 |
|
| 1983 |
Mayer LD, Nelsestuen GL. Membrane lateral phase separation induced by proteins of the prothrombinase complex Biochimica Et Biophysica Acta. 734: 48-53. DOI: 10.1016/0005-2736(83)90073-1 |
0.402 |
|
| 1982 |
Pletcher CH, Bouhoutsos-Brown EF, Bryant RG, Nelsestuen GL. Effects of temperature and pH on prothrombin fragment 1 conformation as determined by nuclear magnetic resonance. Biochemistry. 20: 6149-55. PMID 7306502 DOI: 10.1021/Bi00524A037 |
0.313 |
|
| 1982 |
Pusey ML, Mayer LD, Wei GJ, Bloomfield VA, Nelsestuen GL. Kinetic and hydrodynamic analysis of blood clotting factor V-membrane binding. Biochemistry. 21: 5262-9. PMID 7171555 DOI: 10.1021/Bi00264A022 |
0.445 |
|
| 1982 |
Wei GJ, Bloomfield VA, Resnick RM, Nelsestuen GL. Kinetic and mechanistic analysis of prothrombin-membrane binding by stopped-flow light scattering. Biochemistry. 21: 1949-59. PMID 6805510 DOI: 10.1021/Bi00537A039 |
0.311 |
|
| 1982 |
Lampe PD, Nelsestuen GL. Myelin basic protein-enhanced fusion of membranes. Biochimica Et Biophysica Acta. 693: 320-5. PMID 6186278 DOI: 10.1016/0005-2736(82)90438-2 |
0.382 |
|
| 1981 |
Mayer LD, Nelsestuen GL. Calcium and prothrombin-induced lateral phase separation in membranes. Biochemistry. 20: 2457-2463. PMID 6786334 DOI: 10.1021/Bi00512A015 |
0.322 |
|
| 1980 |
Resnick RM, Nelsestuen GL. Prothrombin--membrane interaction. Effects of ionic strength, pH, and temperature Biochemistry. 19: 3028-3033. PMID 7397115 DOI: 10.1021/Bi00554A030 |
0.406 |
|
| 1980 |
Nelsestuen GL. Origin of life: Consideration of alternatives to proteins and nucleic acids Journal of Molecular Evolution. 15: 59-72. PMID 7365808 DOI: 10.1007/Bf01732583 |
0.305 |
|
| 1978 |
Nelsestuen GL, Kisiel W, Scipio RGD. Interaction of vitamin K dependent proteins with membranes. Biochemistry. 17: 2134-2138. PMID 566556 DOI: 10.1021/Bi00604A017 |
0.459 |
|
| 1977 |
Lim TK, Bloomfield VA, Nelsestuen GL. Structure of the prothrombin- and blood clotting factor X-membrane complexes Biochemistry. 16: 4177-4181. PMID 901767 DOI: 10.1021/Bi00638A007 |
0.382 |
|
| 1977 |
Nelsestuen GL, Broderius M. Interaction of prothrombin and blood-clotting factor X with membranes of varying composition. Biochemistry. 16: 4172-4177. PMID 901766 DOI: 10.1021/Bi00638A006 |
0.441 |
|
| 1977 |
Nelsestuen GL, Lim TK. Equilibria involved in prothrombin- and blood-clotting factor X-membrane binding Biochemistry. 16: 4164-4171. PMID 901765 DOI: 10.1021/Bi00638A005 |
0.432 |
|
| 1976 |
Zytkovicz TH, Nelsestuen GL. γ-carboxyglutamic acid distribution Biochimica Et Biophysica Acta. 444: 344-348. PMID 986832 DOI: 10.1016/0304-4165(76)90377-9 |
0.348 |
|
| 1975 |
Nelsestuen GL, Broderius M, Zytkovicz TH, Howard JB. On the role of gamma-carboxyglutamic acid in calcium and phospholipid binding. Biochemical and Biophysical Research Communications. 65: 233-40. PMID 1147986 DOI: 10.1016/S0006-291X(75)80084-2 |
0.38 |
|
| 1975 |
Howard JB, Nelsestuen GL. Isolation and characterization of vitamin K-dependent region of bovine blood clotting factor X. Proceedings of the National Academy of Sciences of the United States of America. 72: 1281-5. PMID 1055402 DOI: 10.1073/Pnas.72.4.1281 |
0.31 |
|
| 1970 |
Nelsestuen GL, Kirkwood S. Uridine diphosphoglucose 4-epimerase: kinetic isotope effect. Biochimica Et Biophysica Acta. 220: 633-5. PMID 5499644 DOI: 10.1016/0005-2744(70)90299-8 |
0.532 |
|
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