Year |
Citation |
Score |
2015 |
Kim H, Kim HJ, Llinas M. Gestation of a Glu Plasminogen Supra Fold via Molecular Dynamics Simulation Biophysical Journal. 108: 210a. DOI: 10.1016/J.Bpj.2014.11.1162 |
0.401 |
|
2010 |
Bermejo GA, Llinás M. Structure-oriented methods for protein NMR data analysis. Progress in Nuclear Magnetic Resonance Spectroscopy. 56: 311-28. PMID 20633357 DOI: 10.1016/J.Pnmrs.2010.02.001 |
0.792 |
|
2010 |
Christen MT, Frank P, Schaller J, Llinás M. Human plasminogen kringle 3: solution structure, functional insights, phylogenetic landscape. Biochemistry. 49: 7131-50. PMID 20617841 DOI: 10.1021/Bi100687F |
0.39 |
|
2010 |
Kim HJ, Choi MY, Kim HJ, Llinás M. Conformational dynamics and ligand binding in the multi-domain protein PDC109. Plos One. 5: e9180. PMID 20174627 DOI: 10.1371/Journal.Pone.0009180 |
0.351 |
|
2010 |
Llinás M, Lecomte JT, De Marco A. Solvent and temperature effects on crambin, a hydrophobic protein. Biophysical Journal. 32: 90-1. PMID 19431418 DOI: 10.1016/S0006-3495(80)84924-1 |
0.408 |
|
2009 |
Battistel MD, Grishaev A, An SS, Castellino FJ, Llinás M. Solution structure and functional characterization of human plasminogen kringle 5. Biochemistry. 48: 10208-19. PMID 19821587 DOI: 10.1021/Bi901433N |
0.792 |
|
2009 |
Llinás M, Klein M, Neilands J. THE SOLUTION CONFORMATION OF THE FERRICHROMES. International Journal of Peptide and Protein Research. 4: 157-166. DOI: 10.1111/J.1399-3011.1972.Tb03415.X |
0.804 |
|
2008 |
Ozhogina OA, Grishaev A, Bominaar EL, Patthy L, Trexler M, Llinás M. NMR solution structure of the neurotrypsin Kringle domain. Biochemistry. 47: 12290-8. PMID 18956887 DOI: 10.1021/Bi800555Z |
0.669 |
|
2008 |
Lemak A, Steren CA, Arrowsmith CH, Llinás M. Sequence specific resonance assignment via Multicanonical Monte Carlo search using an ABACUS approach. Journal of Biomolecular Nmr. 41: 29-41. PMID 18458824 DOI: 10.1007/S10858-008-9238-2 |
0.39 |
|
2008 |
Bermejo GA, Llinás M. Deuterated protein folds obtained directly from unassigned nuclear overhauser effect data. Journal of the American Chemical Society. 130: 3797-805. PMID 18318535 DOI: 10.1021/Ja074836E |
0.785 |
|
2005 |
Grishaev A, Steren CA, Wu B, Pineda-Lucena A, Arrowsmith C, Llinás M. ABACUS, a direct method for protein NMR structure computation via assembly of fragments. Proteins. 61: 36-43. PMID 16080153 DOI: 10.1002/Prot.20457 |
0.685 |
|
2005 |
Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, Llinas M, Ulrich EL, Markley JL, Ionides J, Laue ED. The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins. 59: 687-96. PMID 15815974 DOI: 10.1002/Prot.20449 |
0.533 |
|
2005 |
Grishaev A, Llinás M. Protein structure elucidation from minimal NMR data: the CLOUDS approach. Methods in Enzymology. 394: 261-95. PMID 15808224 DOI: 10.1016/S0076-6879(05)94010-X |
0.672 |
|
2004 |
Gehrmann ML, Douglas JT, Bányai L, Tordai H, Patthy L, Llinás M. Modular autonomy, ligand specificity, and functional cooperativity of the three in-tandem fibronectin type II repeats from human matrix metalloproteinase 2. The Journal of Biological Chemistry. 279: 46921-9. PMID 15317806 DOI: 10.1074/Jbc.M408859200 |
0.747 |
|
2004 |
Grishaev A, Llinás M. BACUS: A Bayesian protocol for the identification of protein NOESY spectra via unassigned spin systems. Journal of Biomolecular Nmr. 28: 1-10. PMID 14739635 DOI: 10.1023/B:Jnmr.0000012846.56763.F7 |
0.686 |
|
2003 |
Frank PS, Douglas JT, Locher M, Llinás M, Schaller J. Structural/functional characterization of the alpha 2-plasmin inhibitor C-terminal peptide. Biochemistry. 42: 1078-85. PMID 12549929 DOI: 10.1021/Bi026917N |
0.589 |
|
2003 |
Trexler M, Briknarová K, Gehrmann M, Llinás M, Patthy L. Peptide ligands for the fibronectin type II modules of matrix metalloproteinase 2 (MMP-2). The Journal of Biological Chemistry. 278: 12241-6. PMID 12486137 DOI: 10.1074/Jbc.M210116200 |
0.797 |
|
2002 |
Grishaev A, Llinás M. Sorting signals from protein NMR spectra: SPI, a Bayesian protocol for uncovering spin systems. Journal of Biomolecular Nmr. 24: 203-13. PMID 12522308 DOI: 10.1023/A:1021660608913 |
0.682 |
|
2002 |
Grishaev A, Llinas M. Protein structure elucidation from NMR proton densities. Proceedings of the National Academy of Sciences of the United States of America. 99: 6713-8. PMID 12011434 DOI: 10.1073/Pnas.042114399 |
0.657 |
|
2002 |
Grishaev A, Llinás M. CLOUDS, a protocol for deriving a molecular proton density via NMR. Proceedings of the National Academy of Sciences of the United States of America. 99: 6707-12. PMID 12011433 DOI: 10.1073/Pnas.082114199 |
0.695 |
|
2002 |
Gehrmann M, Briknarová K, Bányai L, Patthy L, Llinás M. The col-1 module of human matrix metalloproteinase-2 (MMP-2): structural/functional relatedness between gelatin-binding fibronectin type II modules and lysine-binding kringle domains. Biological Chemistry. 383: 137-48. PMID 11928808 DOI: 10.1515/Bc.2002.014 |
0.805 |
|
2002 |
Douglas JT, von Haller PD, Gehrmann M, Llinás M, Schaller J. The two-domain NK1 fragment of plasminogen: folding, ligand binding, and thermal stability profile. Biochemistry. 41: 3302-10. PMID 11876638 DOI: 10.1021/Bi016018J |
0.729 |
|
2002 |
Orning L, Fischer PM, Hu CK, Agner E, Engebretsen M, Husbyn M, Petersen LB, Orvim U, Llinas M, Sakariassen KS. A cyclic pentapeptide derived from the second EGF-like domain of Factor VII is an inhibitor of tissue factor dependent coagulation and thrombus formation. Thrombosis and Haemostasis. 87: 13-21. PMID 11848442 DOI: 10.1055/S-0037-1612937 |
0.354 |
|
2002 |
Gehrmann M, Briknarova K, Banyai L, Patthy L, Llinas M. Backbone 1H and 15N Chemical Shift Assignements for the first fibronectin type II module of MMP-2 (col-1) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5262 |
0.784 |
|
2001 |
Lewis VO, O'Reilly MS, Gehrmann M, Llinás M, Schaller J, Weissbach L. Inhibition of tumor growth by plasminogen-related protein-B. Anticancer Research. 21: 2287-91. PMID 11724284 |
0.568 |
|
2001 |
Ozhogina OA, Trexler M, Bányai L, Llinás M, Patthy L. Origin of fibronectin type II (FN2) modules: structural analyses of distantly-related members of the kringle family idey the kringle domain of neurotrypsin as a potential link between FN2 domains and kringles. Protein Science : a Publication of the Protein Society. 10: 2114-22. PMID 11567102 DOI: 10.1110/Ps.15801 |
0.364 |
|
2001 |
Hu CK, Llinás M, Agner KE, Örning L, Sakariassen KS, Fischer PM. Synthesis, biological activity, and solution structures of a cyclic dodecapeptide from the EGF-2 domain of blood coagulation factor VII Journal of Peptide Research. 57: 462-472. PMID 11437950 DOI: 10.1034/J.1399-3011.2001.00843.X |
0.431 |
|
2001 |
Briknarová K, Gehrmann M, Bányai L, Tordai H, Patthy L, Llinás M. Gelatin-binding region of human matrix metalloproteinase-2: solution structure, dynamics, and function of the COL-23 two-domain construct. The Journal of Biological Chemistry. 276: 27613-21. PMID 11320090 DOI: 10.1074/Jbc.M101105200 |
0.805 |
|
2001 |
Briknarová K, Takayama S, Brive L, Havert ML, Knee DA, Velasco J, Homma S, Cabezas E, Stuart J, Hoyt DW, Satterthwait AC, Llinás M, Reed JC, Ely KR. Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein. Nature Structural Biology. 8: 349-52. PMID 11276257 DOI: 10.1038/86236 |
0.786 |
|
1999 |
Marti DN, Schaller J, Llinás M. Solution structure and dynamics of the plasminogen kringle 2-AMCHA complex: 31-helix in homologous domains Biochemistry. 38: 15741-15755. PMID 10625440 DOI: 10.1021/Bi9917378 |
0.418 |
|
1999 |
Briknarová K, Grishaev A, Bányai L, Tordai H, Patthy L, Llinás M. The second type II module from human matrix metalloproteinase 2: structure, function and dynamics. Structure (London, England : 1993). 7: 1235-45. PMID 10545322 DOI: 10.1016/S0969-2126(00)80057-X |
0.801 |
|
1999 |
Liu H, Farr-Jones S, Ulyanov NB, Llinas M, Marqusee S, Groth D, Cohen FE, Prusiner SB, James TL. Solution structure of Syrian hamster prion protein rPrP(90-231). Biochemistry. 38: 5362-77. PMID 10220323 DOI: 10.1021/Bi982878X |
0.324 |
|
1999 |
Lewis VO, Gehrmann M, Weissbach L, Hyman JE, Rielly A, Jones DG, Llinás M, Schaller J. Homologous plasminogen N-terminal and plasminogen-related gene A and B peptides. Characterization of cDNAs and recombinant fusion proteins. European Journal of Biochemistry / Febs. 259: 618-25. PMID 10092845 DOI: 10.1046/J.1432-1327.1999.00055.X |
0.634 |
|
1999 |
Medved LV, Migliorini M, Mikhailenko I, Barrientos LG, Llinás M, Strickland DK. Domain organization of the 39-kDa receptor-associated protein Journal of Biological Chemistry. 274: 717-727. PMID 9873007 DOI: 10.1074/Jbc.274.2.717 |
0.319 |
|
1999 |
Briknarova K, Grishaev A, Banyai L, Tordai H, Patthy L, Llinas M. The Second Type II Module From Human Matrix Metalloproteinase 2 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr4510 |
0.755 |
|
1998 |
An SS, Carreño C, Marti DN, Schaller J, Albericio F, Llinas M. Lysine-50 is a likely site for anchoring the plasminogen N-terminal peptide to lysine-binding kringles. Protein Science : a Publication of the Protein Society. 7: 1960-9. PMID 9761476 DOI: 10.1002/Pro.5560070911 |
0.379 |
|
1998 |
An SS, Marti DN, Carreño C, Albericio F, Schaller J, Llinas M. Structural/functional properties of the Glu1-HSer57 N-terminal fragment of human plasminogen: conformational characterization and interaction with kringle domains. Protein Science : a Publication of the Protein Society. 7: 1947-59. PMID 9761475 DOI: 10.1002/Pro.5560070910 |
0.406 |
|
1998 |
Marti DN, Schaller J, Llinás M. Human plasminogen kringle 2: Ligand binding properties and NMR solution structure Fibrinolysis and Proteolysis. 12: 3. |
0.372 |
|
1997 |
Marti DN, Hu CK, An SSA, Von Haller P, Schaller J, Llinás M. Ligand preferences of kringle 2 and homologous domains of human plasminogen: Canvassing weak, intermediate, and high-affinity binding sites by 1H-NMR Biochemistry. 36: 11591-11604. PMID 9305949 DOI: 10.1021/Bi971316V |
0.347 |
|
1996 |
Söhndel S, Hu CK, Marti D, Affolter M, Schaller J, Llinás M, Rickli EE. Recombinant gene expression and 1H NMR characteristics of the kringle (2 + 3) supermodule: Spectroscopic/functional individuality of plasminogen kringle domains Biochemistry. 35: 2357-2364. PMID 8652577 DOI: 10.1021/Bi9520949 |
0.387 |
|
1996 |
Hu CK, Kohnert U, Stürzebecher J, Fischer S, Llinás M. Complexation of the tissue plasminogen activator protease with benzamidine-type inhibitors: Interference by the kringle 2 module Biochemistry. 35: 3270-3276. PMID 8605163 DOI: 10.1021/Bi9515026 |
0.403 |
|
1995 |
Byeon IJ, Kelley RF, Mulkerrin MG, An SS, Llinás M. Ligand binding to the tissue-type plasminogen activator kringle 2 domain: structural characterization by 1H-NMR. Biochemistry. 34: 2739-50. PMID 7893685 DOI: 10.1021/Bi00009A002 |
0.426 |
|
1995 |
Ramesh V, Rajan N, Laursen RA, Llinás M. Plasminogen kringle 4 binds the heptapeptide fragment 44-50 of the plasminogen N-terminal peptide. Blood Coagulation & Fibrinolysis : An International Journal in Haemostasis and Thrombosis. 6: 207-18. PMID 7654934 DOI: 10.1097/00001721-199505000-00003 |
0.329 |
|
1994 |
Cox M, Schaller J, Boelens R, Kaptein R, Rickli E, Llinás M. Kringle solution structures via NMR: two-dimensional 1H-NMR analysis of horse plasminogen kringle 4. Chemistry and Physics of Lipids. 67: 43-58. PMID 8187244 DOI: 10.1016/0009-3084(94)90123-6 |
0.449 |
|
1994 |
Rejante MR, Llinás M. Solution structure of the epsilon-aminohexanoic acid complex of human plasminogen kringle 1. European Journal of Biochemistry. 221: 939-49. PMID 8181476 DOI: 10.1111/J.1432-1033.1994.Tb18809.X |
0.459 |
|
1994 |
Rejante MR, Llinás M. 1H-NMR assignments and secondary structure of human plasminogen kringle 1. European Journal of Biochemistry. 221: 927-37. PMID 8181475 DOI: 10.1111/J.1432-1033.1994.Tb18808.X |
0.417 |
|
1994 |
Li X, Bokman AM, Llinás M, Smith RAG, Dobson CM. Solution structure of the kringle domain from urokinase-type plasminogen activator Journal of Molecular Biology. 235: 1548-1559. PMID 8107091 DOI: 10.1006/Jmbi.1994.1106 |
0.426 |
|
1994 |
Hu CK, Kohnert U, Wilhelm O, Fischer S, Llinás M. Tissue-type plasminogen activator domain-deletion mutant BM 06.022: modular stability, inhibitor binding, and activation cleavage. Biochemistry. 33: 11760-6. PMID 7918392 DOI: 10.1021/Bi00205A011 |
0.402 |
|
1993 |
Bokman AM, Jiménez-Barbero J, Llinás M. 1H NMR characterization of the urokinase kringle module: Structural, but not functional, relatedness to homologous domains Journal of Biological Chemistry. 268: 13858-13868. PMID 8314753 |
0.31 |
|
1992 |
Constantine KL, Madrid M, Bányai L, Trexler M, Patthy L, Llinás M. Refined solution structure and ligand-binding properties of PDC-109 domain b. A collagen-binding type II domain Journal of Molecular Biology. 223: 281-298. PMID 1731074 DOI: 10.1016/0022-2836(92)90731-X |
0.416 |
|
1992 |
An SSA, Jiménez-Barbero J, Petersen TE, Llinás M. The two polypeptide chains in fibronectin are joined in antiparallel fashion: NMR structural characterization Biochemistry. 31: 9927-9933. PMID 1390775 DOI: 10.1021/Bi00156A010 |
0.448 |
|
1991 |
Constantine KL, De Marco A, Madrid M, Brooks CL, Llinás M. The solution conformations of ferrichrome and deferriferrichrome determined by 1H-NMR spectroscopy and computational modeling. Biopolymers. 30: 239-56. PMID 2279065 DOI: 10.1002/Bip.360300303 |
0.444 |
|
1991 |
Constantine KL, Ramesh V, Bányai L, Trexler M, Patthy L, Llinás M. Sequence-specific 1H NMR assignments and structural characterization of bovine seminal fluid protein PDC-109 domain b. Biochemistry. 30: 1663-72. PMID 1993183 DOI: 10.1021/Bi00220A032 |
0.45 |
|
1991 |
Byeon IJ, Kelley RF, Llinás M. Kringle-2 domain of the tissue-type plasminogen activator. 1H-NMR assignments and secondary structure. European Journal of Biochemistry / Febs. 197: 155-65. PMID 1901789 DOI: 10.1111/J.1432-1033.1991.Tb15894.X |
0.45 |
|
1991 |
Kleywegt GJ, Boelens R, Cox M, Llinás M, Kaptein R. Computer-assisted assignment of 2D 1H NMR spectra of proteins: basic algorithms and application to phoratoxin B. Journal of Biomolecular Nmr. 1: 23-47. PMID 1841687 DOI: 10.1007/Bf01874567 |
0.345 |
|
1991 |
Byeon IJL, Llinás M. Solution structure of the tissue-type plasminogen activator kringle 2 domain complexed to 6-aminohexanoic acid an antifibrinolytic drug Journal of Molecular Biology. 222: 1035-1051. PMID 1762144 DOI: 10.1016/0022-2836(91)90592-T |
0.439 |
|
1991 |
Rejante MR, Byeon IJ, Llinás M. Ligand specificity of human plasminogen kringle 4. Biochemistry. 30: 11081-92. PMID 1657159 DOI: 10.1021/Bi00110A010 |
0.381 |
|
1991 |
Rejante M, Elliott BW, Llinás M. A 1H-NMR study of plasminogen kringle 4 interactions with intact and partially digested fibrinogen Fibrinolysis and Proteolysis. 5: 87-92. DOI: 10.1016/0268-9499(91)90048-9 |
0.361 |
|
1991 |
Madrid M, Llinás E, Llinás M. Model-independent refinement of interproton distances generated from 1H NMR overhauser intensities Journal of Magnetic Resonance (1969). 93: 329-346. DOI: 10.1016/0022-2364(91)90009-I |
0.32 |
|
1990 |
Thewes T, Constantine K, Byeon IJL, Llinás M. Ligand interactions with the kringle 5 domain of plasminogen: A study by 1NMR spectroscopy Journal of Biological Chemistry. 265: 3906-3915. PMID 2105955 |
0.39 |
|
1989 |
Byeon IJ, Kelley RF, Llinás M. 1H NMR structural characterization of a recombinant kringle 2 domain from human tissue-type plasminogen activator. Biochemistry. 28: 9350-60. PMID 2558718 DOI: 10.1021/Bi00450A016 |
0.434 |
|
1989 |
De Marco A, Petros AM, Llinás M, Kaptein R, Boelens R. Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy. Biochimica Et Biophysica Acta. 994: 121-37. PMID 2535939 DOI: 10.1016/0167-4838(89)90151-9 |
0.45 |
|
1989 |
Petros AM, Ramesh V, Llinás M. 1H NMR studies of aliphatic ligand binding to human plasminogen kringle 4 Biochemistry. 28: 1368-1376. PMID 2496756 DOI: 10.1021/Bi00429A064 |
0.391 |
|
1989 |
Rasmesh V, Laursen RA, Llinas M. Binding of the plasminogen preactivation heptapeptide to the kringle 4 domain Fibrinolysis. 3: 16. DOI: 10.1016/0268-9499(89)90108-2 |
0.305 |
|
1988 |
Lamerichs RM, Berliner LJ, Boelens R, De Marco A, Llinàs M, Kaptein R. Secondary structure and hydrogen bonding of crambin in solution. A two-dimensional NMR study. European Journal of Biochemistry / Febs. 171: 307-12. PMID 3338468 DOI: 10.1111/J.1432-1033.1988.Tb13791.X |
0.412 |
|
1988 |
Petros AM, Gyenes M, Patthy L, Llinás M. Analysis of the aliphatic 1H-NMR spectrum of plasminogen kringle 4. A comparative study of human, porcine, bovine and chicken homologs. European Journal of Biochemistry. 170: 549-63. PMID 3338451 DOI: 10.1111/J.1432-1033.1988.Tb13734.X |
0.396 |
|
1988 |
Thewes T, Ramesh V, Simplaceanu EL, Llinás M. Analysis of the aromatic 1H-NMR spectrum of the kringle 5 domain from human plasminogen. Evidence for a conserved kringle fold. European Journal of Biochemistry. 175: 237-49. PMID 2841130 DOI: 10.1111/J.1432-1033.1988.Tb14189.X |
0.478 |
|
1988 |
Petros AM, Gyenes M, Patthy L, Llinás M. Analysis of the aromatic 1H NMR spectrum of chicken plasminogen kringle 4. Archives of Biochemistry and Biophysics. 264: 192-202. PMID 2840024 DOI: 10.1016/0003-9861(88)90585-1 |
0.392 |
|
1987 |
Lecomte JTJ, Kaplan D, Llinás M, Thunberg E, Samuelsson G. Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin Biochemistry. 26: 1187-1194. PMID 3567163 DOI: 10.1021/Bi00378A029 |
0.47 |
|
1987 |
De Marco A, Petros AM, Laursen RA, Llinás M. Analysis of ligand-binding to the kringle 4 fragment from human plasminogen. European Biophysics Journal : Ebj. 14: 359-68. PMID 3036485 DOI: 10.1007/Bf00262321 |
0.365 |
|
1987 |
Thewes T, Ramesh V, Simplaceanu EL, Llinás M. Isolation, purification and 1H-NMR characterization of a kringle 5 domain fragment from human plasminogen Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 912: 254-269. PMID 3030435 DOI: 10.1016/0167-4838(87)90096-3 |
0.494 |
|
1987 |
Ramesh V, Petros AM, Llinás M, Tulinsky A, Park CH. Proton magnetic resonance study of lysine-binding to the kringle 4 domain of human plasminogen. The structure of the binding site. Journal of Molecular Biology. 198: 481-98. PMID 2828641 DOI: 10.1016/0022-2836(87)90295-6 |
0.449 |
|
1987 |
Motta A, Laursen RA, Llinás M, Tulinsky A, Park CH. Complete assignment of the aromatic proton magnetic resonance spectrum of the kringle 1 domain from human plasminogen: structure of the ligand-binding site. Biochemistry. 26: 3827-36. PMID 2820478 DOI: 10.1021/Bi00387A014 |
0.495 |
|
1987 |
Vermeulen JAWH, Lamerichs RMJN, Berliner LJ, De Marco A, Llinás M, Boelens R, Alleman J, Kaptein R. 1H NMR characterization of two crambin species Febs Letters. 219: 426-430. DOI: 10.1016/0014-5793(87)80265-X |
0.331 |
|
1986 |
Motta A, Laursen RA, Llinás M. Characterization of the low-field proton magnetic resonance spectrum of plasminogen kringle 4 via selective Overhauser experiments in 1H2O. Biochemistry. 25: 7924-31. PMID 3801451 DOI: 10.1021/Bi00372A021 |
0.461 |
|
1986 |
De Marco A, Zetta L, Petros AM, Llinás M, Boelens R, Kaptein R. Kringle 4 from human plasminogen: a proton magnetic resonance study via two-dimensional photochemically induced dynamic nuclear polarization spectroscopy. Biochemistry. 25: 7918-23. PMID 3801450 DOI: 10.1021/Bi00372A020 |
0.431 |
|
1986 |
Ramesh V, Gyenes M, Patthy L, Llinás M. The aromatic 1H-NMR spectrum of plasminogen kringle 4. A comparative study of human, porcine and bovine homologs. European Journal of Biochemistry. 159: 581-95. PMID 3019697 DOI: 10.1111/J.1432-1033.1986.Tb09925.X |
0.483 |
|
1986 |
De Marco A, Laursen RA, Llinas M. 1H-NMR spectroscopic manifestations of ligand binding to the kringle 4 domain of human plasminogen. Archives of Biochemistry and Biophysics. 244: 727-41. PMID 3004350 DOI: 10.1016/0003-9861(86)90642-9 |
0.433 |
|
1985 |
De Marco A, Motta A, Llinás M, Laursen RA. Macro- and micro-stabilities of the kringle 4 domain from plasminogen. The effect of ligand binding. Biophysical Journal. 48: 411-22. PMID 4041537 DOI: 10.1016/S0006-3495(85)83797-8 |
0.369 |
|
1985 |
De Marco A, Pluck ND, Bányai L, Trexler M, Laursen RA, Patthy L, Llinás M, Williams RJ. Analysis and identification of aromatic signals in the proton magnetic resonance spectrum of the kringle 4 fragment from human plasminogen. Biochemistry. 24: 748-53. PMID 3994983 DOI: 10.1021/Bi00324A032 |
0.449 |
|
1985 |
De Marco A, Laursen RA, Llinás M. Proton Overhauser experiments on kringle 4 from human plasminogen. Implications for the structure of the kringles' hydrophobic core. Biochimica Et Biophysica Acta. 827: 369-80. PMID 2982407 DOI: 10.1016/0167-4838(85)90221-3 |
0.309 |
|
1985 |
Llinás M, Motta A, De Marco A, Laursen RA. Kringle 4 from human plasminogen:1H-nuclear magnetic resonance study of the interactions between ω-amino acid ligands and aromatic residues at the lysine-binding site Journal of Biosciences. 8: 121-139. DOI: 10.1007/Bf02703971 |
0.447 |
|
1984 |
Lecomte JTJ, Llinás M. Characterization of the aromatic proton magnetic resonance spectrum of crambin Biochemistry. 23: 4799-4807. PMID 6548643 DOI: 10.1021/Bi00315A041 |
0.432 |
|
1984 |
Lecomte JTJ, Llinas M. Proton NMR spectral patterns of rapidly flipping tyrosyl rings: a study of crambin in organic solvents Journal of the American Chemical Society. 106: 2741-2748. DOI: 10.1021/Ja00322A001 |
0.428 |
|
1984 |
LECOMTE JTJ, LLINAS M. ChemInform Abstract: PROTON NMR SPECTRAL PATTERNS OF RAPIDLY FLIPPING TYROSYL RINGS: A STUDY OF CRAMBIN IN ORGANIC SOLVENTS Chemischer Informationsdienst. 15. DOI: 10.1002/chin.198433052 |
0.335 |
|
1983 |
Llinas M, De Marco A, Hochschwender SM, Laursen RA. A 1H-NMR study of isolated domains from human plasminogen. Structural homology between kringles 1 and 4. European Journal of Biochemistry / Febs. 135: 379-91. PMID 6311534 DOI: 10.1111/J.1432-1033.1983.Tb07665.X |
0.499 |
|
1983 |
Hochschwender SM, Laursen RA, De Marco A, Llinas M. 600 MHz H nuclear magnetic resonance studies of the kringle 4 fragment of human plasminogen. Archives of Biochemistry and Biophysics. 223: 58-67. PMID 6305276 DOI: 10.1016/0003-9861(83)90571-4 |
0.486 |
|
1982 |
Lecomte JTJ, Jones BL, Llinás M. Proton magnetic resonance studies of barley and wheat thionins: Structural homology with crambin Biochemistry. 21: 4843-4849. PMID 6291592 DOI: 10.1021/Bi00263A003 |
0.492 |
|
1982 |
Philson SB, Llinás M. Siderochromes from Pseudomonas fluorescens. II. Structural homology as revealed by NMR spectroscopy Journal of Biological Chemistry. 257: 8086-8090. PMID 6211451 |
0.416 |
|
1982 |
Lecomte JTJ, De Marco A, Llinás M. Analysis of the methyl 1H-NMR spectrum of crambin, a hydrophobic protein Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 703: 223-230. DOI: 10.1016/0167-4838(82)90052-8 |
0.461 |
|
1981 |
De Marco A, Lecompte JT, Llinás M. Solvent and temperature effects on crambin, a hydrophobic protein, as investigated by proton magnetic resonance European Journal of Biochemistry. 119: 483-490. PMID 6273160 DOI: 10.1111/J.1432-1033.1981.Tb05633.X |
0.389 |
|
1980 |
Llinás M, De Marco A, Lecomte JT. Proton magnetic resonance study of crambin, a hyperstable hydrophobic protein, at 250 and 600 MHz Biochemistry. 19: 1140-1145. PMID 6892782 DOI: 10.1021/Bi00547A016 |
0.467 |
|
1980 |
Llinas M, Marco AD. Aluminum-27 NMR, a quadrupolar probe for the entatic state and stability of metallochromophores. A study of ferrichrome peptides at 65.1 MHz Journal of the American Chemical Society. 102: 2226-2230. DOI: 10.1021/Ja00527A013 |
0.349 |
|
1980 |
Marco AD, Llinas M. Solvent effects and approaches for the fine structure analysis of peptidyl amide 1H NMR spectra Journal of Magnetic Resonance (1969). 39: 253-262. DOI: 10.1016/0022-2364(80)90134-1 |
0.362 |
|
1980 |
Llinas M, Marco AD. Aluminum-27 Nmr, A Quadrupolar Probe For The Entatic State And Stability Of Metallochromophores. A Study Of Ferrichrome Peptides At 65.1 Mhz Cheminform. 11. DOI: 10.1002/Chin.198028054 |
0.349 |
|
1980 |
Llinás M, De Marco A. 27Al NMR, a quadrupolar probe for the entatic state and stability of metallochromophores. A study of ferrichrome peptides at 65.1 MHz Journal of the American Chemical Society. 102: 2226-2230. |
0.33 |
|
1979 |
De Marco A, Llinás M. Complete assignment of carbon signals in a stereospecific peptide via selective and single off-resonance proton decoupling experiments. Analysis of the carbon-13 nuclear magnetic resonance spectrum of alumichrome at 67.88 MHz. Biochemistry. 18: 3846-54. PMID 486399 DOI: 10.1021/Bi00585A003 |
0.456 |
|
1979 |
De Marco A, Llinás M. Signs of heteronuclear spin-spin coupling constants in15N-acetamide Organic Magnetic Resonance. 12: 454-460. DOI: 10.1002/Mrc.1270120804 |
0.385 |
|
1979 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. II. The amide resonances: Errata Biopolymers. 18: 2911-2911. DOI: 10.1002/Bip.1979.360181119 |
0.509 |
|
1979 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. I. The non-amide protons Biopolymers. 18: 2911-2911. DOI: 10.1002/Bip.1979.360181118 |
0.598 |
|
1979 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. II. The amide resonances Biopolymers. 18: 2911-2911. DOI: 10.1002/Bip.1978.360170308 |
0.645 |
|
1978 |
Llinás M, Klein MP, Wüthrich K. Amide proton spin-lattice relaxation in polypeptides. A field-dependence study of the proton and nitrogen dipolar interactions in alumichrome. Biophysical Journal. 24: 849-62. PMID 737289 DOI: 10.1016/S0006-3495(78)85424-1 |
0.762 |
|
1978 |
Llinás M, Wüthrich K. A nitrogen-15 spin-lattice relaxation study of alumichrome Bba - Protein Structure. 532: 29-40. PMID 620055 DOI: 10.1016/0005-2795(78)90444-0 |
0.616 |
|
1978 |
LLINAS M, WILSON DM, KLEIN MP. ChemInform Abstract: PEPTIDE HYDROGEN BONDING. CONFORMATION DEPENDENCE OF THE CARBONYL CARBON-13 NUCLEAR MAGNETIC RESONANCE CHEMICAL SHIFTS IN FERRICHROME. A STUDY BY CARBON-13-(NITROGEN-15) FOURIER DOUBLE RESONANCE SPECTROSCOPY Chemischer Informationsdienst. 9. DOI: 10.1002/chin.197802044 |
0.714 |
|
1978 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. II. The amide resonances Biopolymers. 17: 637-650. DOI: 10.1002/bip.1978.360170308 |
0.563 |
|
1978 |
Demarco A, Llinás M, Wüthrich K. Analysis of the1H-NMR spectra of ferrichrome peptides. I. The non-amide protons Biopolymers. 17: 617-636. DOI: 10.1002/Bip.1978.360170307 |
0.631 |
|
1977 |
Llinás M, Wilson DM, Klein MP. Peptide hydrogen bonding. Conformation dependence of the carbonyl carbon-13 nuclear magnetic resonance chemical shifts in ferrichrome. A study by 13C-[15N] Fourier double resonance spectroscopy1a. Journal of the American Chemical Society. 99: 6846-50. PMID 903527 DOI: 10.1021/Ja00463A010 |
0.741 |
|
1977 |
Llinás M, Meier W, Wüthrich K. A carbon-13 spin lattice relaxation study of alumichrome at 25.1 MHz and 90.5 MHz. Biochimica Et Biophysica Acta. 492: 1-11. PMID 861244 DOI: 10.1016/0005-2795(77)90208-2 |
0.57 |
|
1977 |
Llinás M, Wilson DM, Neilands JB. Peptide strain. Conformation dependence of the carbon-13 nuclear magnetic resonance chemical shifts in the ferrichromes. Journal of the American Chemical Society. 99: 3631-7. PMID 858869 DOI: 10.1021/Ja00453A020 |
0.733 |
|
1977 |
Llinas M, Wilson D, Klein M. Additions and Corrections - Peptide Hydrogen Bonding. Conformation Dependence of the Carbonyl Carbon-13 Nuclear Magnetic Resonance Chemical Shifts in Ferrichrome. A Study by13C-{15N} Fourier Double Resonance Spectroscopy Journal of the American Chemical Society. 99: 8374-8374. DOI: 10.1021/Ja00467A608 |
0.727 |
|
1977 |
LLINAS M, WILSON DM, NEILANDS JB. ChemInform Abstract: SOLUTION CONFORMATION OF THE FERRICHROMES. 10. PEPTIDE STRAIN. CONFORMATION DEPENDENCE OF THE CARBON-13 NUCLEAR MAGNETIC RESONANCE CHEMICAL SHIFTS IN THE FERRICHROMES Chemischer Informationsdienst. 8. DOI: 10.1002/chin.197734044 |
0.727 |
|
1977 |
LLINAS M, HORSLEY WJ, KLEIN MP. ChemInform Abstract: NITROGEN-15 NUCLEAR MAGNETIC RESONANCE SPECTRUM OF ALUMICHROME. DETECTION BY A DOUBLE RESONANCE FOURIER TRANSFORM TECHNIQUE Chemischer Informationsdienst. 8: no-no. DOI: 10.1002/chin.197709054 |
0.678 |
|
1976 |
Llinás M, Horsley WJ, Klein MP. Nitrogen-15 nuclear magnetic resonance spectrum of alumichrome. Detection by a double resonance Fourier transform technique. Journal of the American Chemical Society. 98: 7554-8. PMID 993494 DOI: 10.1021/Ja00440A018 |
0.715 |
|
1976 |
Llinás M, Neilands JB. The structure of two alanine containing ferrichromes: sequence determination by proton magnetic resonance. Biophysics of Structure and Mechanism. 2: 105-17. PMID 963232 DOI: 10.1007/BF00863704 |
0.748 |
|
1976 |
Llinás M, Wilson DM, Klein MP, Neilands JB. 13C nuclear magnetic resonance of the errichrome peptides: structural and strain contributions to the conformational state. Journal of Molecular Biology. 104: 853-64. PMID 957441 DOI: 10.1016/0022-2836(76)90186-8 |
0.81 |
|
1975 |
Llinas M, Klein MP. Solution conformation of the ferrichromes. VI. Charge relay at the peptide bond. Proton magnetic resonance study of solvation effects on the amide electron density distribution Journal of the American Chemical Society. 97: 4731-4737. DOI: 10.1021/Ja00849A040 |
0.75 |
|
1975 |
LLINAS M, KLEIN MP. ChemInform Abstract: SOLUTION CONFORMATION OF THE FERRICHROMES PART 6, CHARGE RELAY AT THE PEPTIDE BOND. A (1)H-NMR STUDY OF SOLVATION EFFECTS ON THE AMIDE ELECTRON DENSITY DISTRIBUTION Chemischer Informationsdienst. 6: no-no. DOI: 10.1002/Chin.197542051 |
0.712 |
|
1973 |
Llinás M, Wilson DM, Neilands JB. Effect of metal binding on the conformation of enterobactin. A proton and carbon-13 nuclear magnetic resonance study. Biochemistry. 12: 3836-43. PMID 4745649 DOI: 10.1021/Bi00744A007 |
0.714 |
|
1972 |
Llinás M, Klein MP, Neilands JB. Solution conformation of the ferrichromes. A comparative proton magnetic resonance study of glycine- and serine-containing ferrichromes. Journal of Molecular Biology. 68: 265-84. PMID 5069791 DOI: 10.1016/0022-2836(72)90213-6 |
0.825 |
|
1972 |
Akers HA, Llinás M, Neilands JB. Protonated amino acid precursor studies on rhodotorulic acid biosynthesis in deuterium oxide media. Biochemistry. 11: 2283-91. PMID 5063738 DOI: 10.1021/Bi00762A012 |
0.661 |
|
1970 |
Llinás M, Klein MP, Neilands JB. Solution conformation of ferrichrome, a microbial iron transport cyclohexapeptide, as deduced by high resolution proton magnetic resonance. Journal of Molecular Biology. 52: 399-414. PMID 5492288 DOI: 10.1016/0022-2836(70)90409-2 |
0.779 |
|
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