| Year |
Citation |
Score |
| 2015 |
Byrnes JR, Duval C, Wang Y, Hansen CE, Ahn B, Mooberry MJ, Clark MA, Johnsen JM, Lord ST, Lam W, Meijers JC, Ni H, Ariëns RA, Wolberg AS. Factor XIIIa-dependent retention of red blood cells in clots is mediated by fibrin α-chain crosslinking. Blood. PMID 26324704 DOI: 10.1182/Blood-2015-06-652263 |
0.348 |
|
| 2014 |
Huang L, Hsiao JP, Powierza C, Taylor RM, Lord ST. Does topology drive fiber polymerization? Biochemistry. 53: 7824-34. PMID 25419972 DOI: 10.1021/Bi500986Z |
0.31 |
|
| 2013 |
Raynal B, Cardinali B, Grimbergen J, Profumo A, Lord ST, England P, Rocco M. Hydrodynamic characterization of recombinant human fibrinogen species. Thrombosis Research. 132: e48-53. PMID 23642654 DOI: 10.1016/J.Thromres.2013.04.005 |
0.314 |
|
| 2013 |
Huang L, Lord ST. The isolation of fibrinogen monomer dramatically influences fibrin polymerization. Thrombosis Research. 131: e258-63. PMID 23622556 DOI: 10.1016/J.Thromres.2013.02.003 |
0.354 |
|
| 2013 |
Park R, Ping L, Song J, Seo JY, Choi TY, Choi JR, Gorkun OV, Lord ST. An engineered fibrinogen variant AαQ328,366P does not polymerise normally, but retains the ability to form α cross-links. Thrombosis and Haemostasis. 109: 199-206. PMID 23224113 DOI: 10.1160/Th12-08-0609 |
0.33 |
|
| 2012 |
Yermolenko IS, Gorkun OV, Fuhrmann A, Podolnikova NP, Lishko VK, Oshkadyerov SP, Lord ST, Ros R, Ugarova TP. The assembly of nonadhesive fibrinogen matrices depends on the αC regions of the fibrinogen molecule. The Journal of Biological Chemistry. 287: 41979-90. PMID 23086938 DOI: 10.1074/Jbc.M112.410696 |
0.31 |
|
| 2012 |
Park R, Ping L, Song J, Hong SY, Choi TY, Choi JR, Gorkun OV, Lord ST. Fibrinogen residue γAla341 is necessary for calcium binding and 'A-a' interactions. Thrombosis and Haemostasis. 107: 875-83. PMID 22437918 DOI: 10.1160/Th11-10-0731 |
0.446 |
|
| 2011 |
Ping L, Huang L, Cardinali B, Profumo A, Gorkun OV, Lord ST. Substitution of the human αC region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibers. Biochemistry. 50: 9066-75. PMID 21932842 DOI: 10.1021/Bi201094V |
0.381 |
|
| 2011 |
Lord ST. Coming full circle with factor XIII. Blood. 117: 3255-6. PMID 21436080 DOI: 10.1182/Blood-2011-02-332627 |
0.314 |
|
| 2011 |
Lord ST. Molecular mechanisms affecting fibrin structure and stability. Arteriosclerosis, Thrombosis, and Vascular Biology. 31: 494-9. PMID 21325671 DOI: 10.1161/Atvbaha.110.213389 |
0.306 |
|
| 2011 |
Yermolenko IS, Alexander F, Gorkun OV, Lishko VK, Lord ST, Ros R, Ugarova TP. The Role of the αC Domains in the Formation of Nonadhesive Fibrinogen Matrices Blood. 118: 1194-1194. DOI: 10.1182/Blood.V118.21.1194.1194 |
0.305 |
|
| 2011 |
Hudson N, Ping L, Olusesi O, O'Brien ET, Superfine R, Lord S, Falvo M. Investigating the Role of the Alpha-C domain in Fibrin Fiber Mechanics Biophysical Journal. 100: 481a. DOI: 10.1016/J.Bpj.2010.12.2822 |
0.335 |
|
| 2010 |
Falvo MR, Gorkun OV, Lord ST. The molecular origins of the mechanical properties of fibrin. Biophysical Chemistry. 152: 15-20. PMID 20888119 DOI: 10.1016/J.Bpc.2010.08.009 |
0.312 |
|
| 2010 |
Hantgan RR, Stahle MC, Lord ST. Dynamic regulation of fibrinogen: integrin αIIbβ3 binding. Biochemistry. 49: 9217-25. PMID 20828133 DOI: 10.1021/Bi1009858 |
0.403 |
|
| 2010 |
Nordstrom SM, Holliday BA, Sos BC, Smyth JW, Levy RE, Dukes JW, Lord ST, Weiss EJ. Increased thrombosis susceptibility and altered fibrin formation in STAT5-deficient mice. Blood. 116: 5724-33. PMID 20823455 DOI: 10.1182/Blood-2010-06-292227 |
0.322 |
|
| 2010 |
Huang L, Lord ST. From Fibrinogen to Fibrin: Dynamic Light Scattering to Probe the Mechanism of Protofibril Assembly Into Fibers. Blood. 116: 1156-1156. DOI: 10.1182/Blood.V116.21.1156.1156 |
0.41 |
|
| 2010 |
Park R, Ping L, Song J, Hong S, Choi J, Gorkun OV, Lord ST. Fibrinogen residue γAla341 Is Necessary for Calcium Binding and ‘A-a’ interaction. Blood. 116: 1154-1154. DOI: 10.1182/Blood.V116.21.1154.1154 |
0.386 |
|
| 2009 |
Bowley SR, Okumura N, Lord ST. Impaired protofibril formation in fibrinogen gamma N308K is due to altered D:D and "A:a" interactions. Biochemistry. 48: 8656-63. PMID 19650644 DOI: 10.1021/Bi900239B |
0.71 |
|
| 2009 |
Lord ST, Henschen-Edman A. Birger Blombäck (May 7, 1926 - October 2, 2008). Journal of Thrombosis and Haemostasis : Jth. 7: 908-9. PMID 19220733 DOI: 10.1111/J.1538-7836.2009.03320.X |
0.359 |
|
| 2009 |
Gersh KC, Nagaswami C, Weisel JW, Lord ST. The presence of gamma' chain impairs fibrin polymerization. Thrombosis Research. 124: 356-63. PMID 19138790 DOI: 10.1016/J.Thromres.2008.11.016 |
0.767 |
|
| 2009 |
Bowley SR, Lord ST. Fibrinogen variant BbetaD432A has normal polymerization but does not bind knob "B". Blood. 113: 4425-30. PMID 19075185 DOI: 10.1182/Blood-2008-09-178178 |
0.743 |
|
| 2008 |
Falvo MR, Millard D, O'Brien ET, Superfine R, Lord ST. Length of tandem repeats in fibrin's alphaC region correlates with fiber extensibility. Journal of Thrombosis and Haemostasis : Jth. 6: 1991-3. PMID 18761721 DOI: 10.1111/J.1538-7836.2008.03147.X |
0.338 |
|
| 2008 |
Bowley SR, Merenbloom BK, Okumura N, Betts L, Heroux A, Gorkun OV, Lord ST. Polymerization-defective fibrinogen variant gammaD364A binds knob "A" peptide mimic. Biochemistry. 47: 8607-13. PMID 18642883 DOI: 10.1021/Bi8000769 |
0.749 |
|
| 2008 |
Geer CB, Stasko NA, Rus IA, Lord ST, Schoenfisch MH. Influence of glutathione and its derivatives on fibrin polymerization. Biomacromolecules. 9: 1876-82. PMID 18570468 DOI: 10.1021/Bm800146J |
0.753 |
|
| 2008 |
Flick M, Ullman JM, Palumbo JS, Mullins ES, Kombrink KW, Talmage KE, Shaw MA, Lord ST, Degen J, Gorkun OV. Loss of Clotting Function in Mice Expressing a Mutant Form of Fibrinogen Lacking the α Chain Thrombin Cleavage Site Blood. 112: 394-394. DOI: 10.1182/Blood.V112.11.394.394 |
0.341 |
|
| 2007 |
Okumura N, Terasawa F, Haneishi A, Fujihara N, Hirota-Kawadobora M, Yamauchi K, Ota H, Lord ST. B:b interactions are essential for polymerization of variant fibrinogens with impaired holes 'a'. Journal of Thrombosis and Haemostasis : Jth. 5: 2352-9. PMID 17922804 DOI: 10.1111/J.1538-7836.2007.02793.X |
0.376 |
|
| 2007 |
Geer CB, Tripathy A, Schoenfisch MH, Lord ST, Gorkun OV. Role of 'B-b' knob-hole interactions in fibrin binding to adsorbed fibrinogen. Journal of Thrombosis and Haemostasis : Jth. 5: 2344-51. PMID 17892530 DOI: 10.1111/J.1538-7836.2007.02774.X |
0.77 |
|
| 2007 |
Geer CB, Rus IA, Lord ST, Schoenfisch MH. Surface-dependent fibrinopeptide A accessibility to thrombin. Acta Biomaterialia. 3: 663-8. PMID 17540627 DOI: 10.1016/J.Actbio.2007.03.004 |
0.74 |
|
| 2007 |
Standeven KF, Carter AM, Grant PJ, Weisel JW, Chernysh I, Masova L, Lord ST, Ariëns RA. Functional analysis of fibrin {gamma}-chain cross-linking by activated factor XIII: determination of a cross-linking pattern that maximizes clot stiffness. Blood. 110: 902-7. PMID 17435113 DOI: 10.1182/Blood-2007-01-066837 |
0.315 |
|
| 2007 |
Lord ST. Fibrinogen and fibrin: scaffold proteins in hemostasis. Current Opinion in Hematology. 14: 236-41. PMID 17414213 DOI: 10.1097/Moh.0B013E3280Dce58C |
0.37 |
|
| 2007 |
Kostelansky MS, Lounes KC, Ping LF, Dickerson SK, Gorkun OV, Lord ST. Probing the gamma2 calcium-binding site: studies with gammaD298,301A fibrinogen reveal changes in the gamma294-301 loop that alter the integrity of the "a" polymerization site. Biochemistry. 46: 5114-23. PMID 17411074 DOI: 10.1021/Bi602607A |
0.789 |
|
| 2006 |
Betts L, Merenbloom BK, Lord ST. The structure of fibrinogen fragment D with the 'A' knob peptide GPRVVE. Journal of Thrombosis and Haemostasis : Jth. 4: 1139-41. PMID 16689770 DOI: 10.2210/Pdb2Ffd/Pdb |
0.316 |
|
| 2006 |
Gersh KC, Lord ST. An Investigation of Factor XIII Binding to Recombinant γ′/γ′ and γ/γ′ Fibrinogen. Blood. 108: 1705-1705. DOI: 10.1182/Blood.V108.11.1705.1705 |
0.779 |
|
| 2005 |
Podolnikova NP, Gorkun OV, Loreth RM, Yee VC, Lord ST, Ugarova TP. A cluster of basic amino acid residues in the gamma370-381 sequence of fibrinogen comprises a binding site for platelet integrin alpha(IIb)beta3 (glycoprotein IIb/IIIa). Biochemistry. 44: 16920-30. PMID 16363805 DOI: 10.1021/Bi051581D |
0.369 |
|
| 2005 |
Evans-Nguyen KM, Tolles LR, Gorkun OV, Lord ST, Schoenfisch MH. Interactions of thrombin with fibrinogen adsorbed on methyl-, hydroxyl-, amine-, and carboxyl-terminated self-assembled monolayers. Biochemistry. 44: 15561-8. PMID 16300405 DOI: 10.1021/Bi0514358 |
0.308 |
|
| 2005 |
Kani S, Terasawa F, Lord ST, Tozuka M, Ota H, Okumura N, Katsuyama T. In vitro expression demonstrates impaired secretion of the gammaAsn319, Asp320 deletion variant fibrinogen. Thrombosis and Haemostasis. 94: 53-9. PMID 16113784 DOI: 10.1160/Th05-02-0134 |
0.341 |
|
| 2005 |
Collet JP, Moen JL, Veklich YI, Gorkun OV, Lord ST, Montalescot G, Weisel JW. The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis. Blood. 106: 3824-30. PMID 16091450 DOI: 10.1182/Blood-2005-05-2150 |
0.324 |
|
| 2004 |
Butler SP, O'Sickey TK, Lord ST, Lubon H, Gwazdauskas FC, Velander WH. Secretion of recombinant human fibrinogen by the murine mammary gland. Transgenic Research. 13: 437-50. PMID 15587268 DOI: 10.1007/S11248-004-9589-8 |
0.35 |
|
| 2004 |
Phillips JE, Lord ST, Gilbert GE. Fibrin stimulates platelets to increase factor VIIIa binding site expression. Journal of Thrombosis and Haemostasis : Jth. 2: 1806-15. PMID 15456493 DOI: 10.1111/J.1538-7836.2004.00919.X |
0.411 |
|
| 2004 |
Wilhelm SE, Lounes KC, Lord ST. Investigation of residues in the fibrin(ogen) gamma chain involved in tissue plasminogen activator binding and plasminogen activation. Blood Coagulation & Fibrinolysis : An International Journal in Haemostasis and Thrombosis. 15: 451-61. PMID 15311153 DOI: 10.1097/00001721-200408000-00003 |
0.786 |
|
| 2004 |
Hogan KA, Merenbloom BK, Kim HS, Lord ST. Neonatal bleeding and decreased plasma fibrinogen levels in mice modeled after the dysfibrinogen Vlissingen/Frankfurt IV. Journal of Thrombosis and Haemostasis : Jth. 2: 1484-7. PMID 15304068 DOI: 10.1111/J.1538-7836.2004.00841.X |
0.588 |
|
| 2004 |
Kostelansky MS, Lounes KC, Ping LF, Dickerson SK, Gorkun OV, Lord ST. Calcium-binding site beta 2, adjacent to the "b" polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization. Biochemistry. 43: 2475-83. PMID 14992585 DOI: 10.1021/Bi0359978 |
0.789 |
|
| 2004 |
Kostelansky MS, Bolliger-Stucki B, Betts L, Gorkun OV, Lord ST. B beta Glu397 and B beta Asp398 but not B beta Asp432 are required for "B:b" interactions. Biochemistry. 43: 2465-74. PMID 14992584 DOI: 10.1021/Bi035996F |
0.8 |
|
| 2004 |
Okumura N, Gorkun OV, Terasawa F, Lord ST. Substitution of the gamma-chain Asn308 disturbs the D:D interface affecting fibrin polymerization, fibrinopeptide B release, and FXIIIa-catalyzed cross-linking. Blood. 103: 4157-63. PMID 14764520 DOI: 10.1182/Blood-2003-12-4296 |
0.416 |
|
| 2004 |
Lefebvre P, Velasco PT, Dear A, Lounes KC, Lord ST, Brennan SO, Green D, Lorand L. Severe hypodysfibrinogenemia in compound heterozygotes of the fibrinogen AalphaIVS4 + 1G>T mutation and an AalphaGln328 truncation (fibrinogen Keokuk). Blood. 103: 2571-6. PMID 14615374 DOI: 10.1182/Blood-2003-07-2316 |
0.318 |
|
| 2003 |
Ugarova TP, Lishko VK, Podolnikova NP, Okumura N, Merkulov SM, Yakubenko VP, Yee VC, Lord ST, Haas TA. Sequence gamma 377-395(P2), but not gamma 190-202(P1), is the binding site for the alpha MI-domain of integrin alpha M beta 2 in the gamma C-domain of fibrinogen. Biochemistry. 42: 9365-73. PMID 12899623 DOI: 10.1021/Bi034057K |
0.341 |
|
| 2003 |
Moen JL, Gorkun OV, Weisel JW, Lord ST. Recombinant BbetaArg14His fibrinogen implies participation of N-terminus of Bbeta chain in desA fibrin polymerization. Blood. 102: 2466-71. PMID 12805063 DOI: 10.1182/Blood-2003-01-0204 |
0.39 |
|
| 2002 |
Kostelansky MS, Betts L, Gorkun OV, Lord ST. 2.8 A crystal structures of recombinant fibrinogen fragment D with and without two peptide ligands: GHRP binding to the "b" site disrupts its nearby calcium-binding site. Biochemistry. 41: 12124-32. PMID 12356313 DOI: 10.1021/Bi0261894 |
0.792 |
|
| 2002 |
Remijn JA, IJsseldijk MJ, van Hemel BM, Galanakis DK, Hogan KA, Lounes KC, Lord ST, Sixma JJ, de Groot PG. Reduced platelet adhesion in flowing blood to fibrinogen by alterations in segment gamma316-322, part of the fibrin-specific region. British Journal of Haematology. 117: 650-7. PMID 12028038 DOI: 10.1046/J.1365-2141.2002.03467.X |
0.657 |
|
| 2002 |
Hogan KA, Weiler H, Lord ST. Mouse models in coagulation. Thrombosis and Haemostasis. 87: 563-74. PMID 12008936 DOI: 10.1055/S-0037-1613050 |
0.634 |
|
| 2002 |
Okumura N, Terasawa F, Tanaka H, Hirota M, Ota H, Kitano K, Kiyosawa K, Lord ST. Analysis of fibrinogen gamma-chain truncations shows the C-terminus, particularly gammaIle387, is essential for assembly and secretion of this multichain protein. Blood. 99: 3654-60. PMID 11986220 DOI: 10.1182/Blood.V99.10.3654 |
0.37 |
|
| 2002 |
Lounes KC, Ping L, Gorkun OV, Lord ST. Analysis of engineered fibrinogen variants suggests that an additional site mediates platelet aggregation and that "B-b" interactions have a role in protofibril formation. Biochemistry. 41: 5291-9. PMID 11955079 DOI: 10.1021/Bi011988S |
0.502 |
|
| 2001 |
Lounes KC, Lefkowitz JB, Henschen-Edman AH, Coates AI, Hantgan RR, Lord ST. The impaired polymerization of fibrinogen Longmont (Bbeta166Arg-->Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers. Blood. 98: 661-6. PMID 11468164 DOI: 10.1182/Blood.V98.3.661 |
0.422 |
|
| 2001 |
Remijn JA, Lounes KC, Hogan KA, Lord ST, Galanakis DK, Sixma JJ, De Groot PG. Mutations on fibrinogen (gamma 316-322) are associated with reduction in platelet adhesion under flow conditions. Annals of the New York Academy of Sciences. 936: 444-8. PMID 11460499 DOI: 10.1111/J.1749-6632.2001.Tb03528.X |
0.642 |
|
| 2001 |
Mullin JL, Norfolk SE, Weisel JW, Lord ST. Clot lysis of variant recombinant fibrinogens confirms that fiber diameter is a major determinant of lysis rate. Annals of the New York Academy of Sciences. 936: 331-4. PMID 11460489 DOI: 10.1111/J.1749-6632.2001.Tb03519.X |
0.317 |
|
| 2001 |
Hogan KA, Bolliger B, Okumura N, Lord ST. The formation of beta fibrin requires a functional a site. Annals of the New York Academy of Sciences. 936: 219-22. PMID 11460478 DOI: 10.1111/J.1749-6632.2001.Tb03509.X |
0.656 |
|
| 2001 |
Lounes KC, Okumura N, Hogan KA, Ping L, Lord ST. Polymerization site a function dependence on structural integrity of its nearby calcium binding site. Annals of the New York Academy of Sciences. 936: 205-9. PMID 11460475 DOI: 10.1111/J.1749-6632.2001.Tb03506.X |
0.671 |
|
| 2001 |
Lounes KC, Lefkowitz JB, Coates AI, Hantgan RR, Henschen-Edman A, Lord ST. Fibrinogen Longmont. A heterozygous abnormal fibrinogen with B beta Arg-166 to Cys substitution associated with defective fibrin polymerization. Annals of the New York Academy of Sciences. 936: 129-32. PMID 11460470 DOI: 10.1111/J.1749-6632.2001.Tb03501.X |
0.448 |
|
| 2001 |
Hogan KA, Maeda N, Kluckman KD, Lord ST. Synthesis of a mouse model of the dysfibrinogen Vlissingen/Frankfurt IV. Annals of the New York Academy of Sciences. 936: 117-21. PMID 11460467 DOI: 10.1111/J.1749-6632.2001.Tb03498.X |
0.635 |
|
| 2001 |
Lord ST, Gorkun OV. Insight from studies with recombinant fibrinogens. Annals of the New York Academy of Sciences. 936: 101-16. PMID 11460465 DOI: 10.1111/J.1749-6632.2001.Tb03497.X |
0.462 |
|
| 2001 |
Bolliger-Stucki B, Lord ST, Furlan M. Fibrinogen Milano XII: a dysfunctional variant containing 2 amino acid substitutions, Aalpha R16C and gamma G165R. Blood. 98: 351-7. PMID 11435303 DOI: 10.1182/Blood.V98.2.351 |
0.413 |
|
| 2001 |
Soslau G, Class R, Morgan DA, Foster C, Lord ST, Marchese P, Ruggeri ZM. Unique pathway of thrombin-induced platelet aggregation mediated by glycoprotein Ib. The Journal of Biological Chemistry. 276: 21173-83. PMID 11283012 DOI: 10.1074/Jbc.M008249200 |
0.359 |
|
| 2000 |
Michelsen AE, Santi C, Holme R, Lord ST, Simpson-Haidaris PJ, Solum NO, Pedersen TM, Brosstad F. The charge-heterogeneity of human fibrinogen as investigated by 2D electrophoresis. Thrombosis Research. 100: 529-35. PMID 11152933 DOI: 10.1016/S0049-3848(00)00359-5 |
0.344 |
|
| 2000 |
Smith RA, Rooney MM, Lord ST, Mosesson MW, Gartner TK. Evidence for new endothelial cell binding sites on fibrinogen. Thrombosis and Haemostasis. 84: 819-25. PMID 11127863 DOI: 10.1055/S-0037-1614123 |
0.369 |
|
| 2000 |
Mullin JL, Gorkun OV, Lord ST. Decreased lateral aggregation of a variant recombinant fibrinogen provides insight into the polymerization mechanism. Biochemistry. 39: 9843-9. PMID 10933802 DOI: 10.1021/Bi000045C |
0.378 |
|
| 2000 |
Mullin JL, Gorkun OV, Binnie CG, Lord ST. Recombinant fibrinogen studies reveal that thrombin specificity dictates order of fibrinopeptide release. The Journal of Biological Chemistry. 275: 25239-46. PMID 10837485 DOI: 10.1074/Jbc.M004142200 |
0.328 |
|
| 2000 |
Hogan KA, Lord ST, Okumura N, Terasawa F, Galanakis DK, Scharrer I, Gorkun OV. A functional assay suggests that heterodimers exist in two C-terminal gamma-chain dysfibrinogens: Matsumoto I and Vlissingen/Frankfurt IV. Thrombosis and Haemostasis. 83: 592-7. PMID 10780323 |
0.625 |
|
| 2000 |
Hogan KA, Gorkun OV, Lounes KC, Coates AI, Weisel JW, Hantgan RR, Lord ST. Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the gamma chain of firbinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation. The Journal of Biological Chemistry. 275: 17778-85. PMID 10748039 DOI: 10.1074/jbc.M001618200 |
0.685 |
|
| 2000 |
Hogan KA, Lord ST, Okumura N, Terasawa F, Galanakis DK, Scharrer I, Gorkun OV. A Functional Assay Suggests that Heterodimers Exist in Two C-Terminal γ-Chain Dysfibrinogens: Matsumoto I and Vlissingen/Frankfurt IV Thrombosis and Haemostasis. 83: 592-597. DOI: 10.1055/S-0037-1613869 |
0.649 |
|
| 1999 |
Terasawa F, Okumura N, Kitano K, Hayashida N, Shimosaka M, Okazaki M, Lord ST. Hypofibrinogenemia associated with a heterozygous missense mutation gamma153Cys to arg (Matsumoto IV): in vitro expression demonstrates defective secretion of the variant fibrinogen. Blood. 94: 4122-31. PMID 10590057 DOI: 10.1182/Blood.V94.12.4122.424K35_4122_4131 |
0.355 |
|
| 1998 |
Gorkun OV, Henschen-Edman AH, Ping LF, Lord ST. Analysis of A alpha 251 fibrinogen: the alpha C domain has a role in polymerization, albeit more subtle than anticipated from the analogous proteolytic fragment X. Biochemistry. 37: 15434-41. PMID 9799505 DOI: 10.1021/Bi981551T |
0.359 |
|
| 1998 |
Rooney MM, Mullin JL, Lord ST. Substitution of tyrosine for phenylalanine in fibrinopeptide A results in preferential thrombin cleavage of fibrinopeptide B from fibrinogen. Biochemistry. 37: 13704-9. PMID 9753458 DOI: 10.1021/Bi981190H |
0.448 |
|
| 1998 |
Rooney MM, Farrell DH, van Hemel BM, de Groot PG, Lord ST. The contribution of the three hypothesized integrin-binding sites in fibrinogen to platelet-mediated clot retraction. Blood. 92: 2374-81. PMID 9746777 DOI: 10.1182/Blood.V92.7.2374 |
0.436 |
|
| 1998 |
Yee KO, Rooney MM, Giachelli CM, Lord ST, Schwartz SM. Role of beta1 and beta3 integrins in human smooth muscle cell adhesion to and contraction of fibrin clots in vitro. Circulation Research. 83: 241-51. PMID 9710116 DOI: 10.1161/01.Res.83.3.241 |
0.303 |
|
| 1998 |
Liu Q, Rooney MM, Kasirer-Friede A, Brown E, Lord ST, Frojmovic MM. Role of the gamma chain Ala-Gly-Asp-Val and Aalpha chain Arg-Gly-Asp-Ser sites of fibrinogen in coaggregation of platelets and fibrinogen-coated beads. Biochimica Et Biophysica Acta. 1385: 33-42. PMID 9630497 DOI: 10.1016/S0167-4838(98)00039-9 |
0.404 |
|
| 1998 |
Rooney MM, Farrell DH, van Hemel BM, de Groot PG, Lord ST. The Contribution of the Three Hypothesized Integrin-Binding Sites in Fibrinogen to Platelet-Mediated Clot Retraction Blood. 92: 2374-2381. DOI: 10.1182/blood.v92.7.2374.2374_2374_2381 |
0.315 |
|
| 1998 |
Côté HC, Lord ST, Pratt KP. γ-Chain Dysfibrinogenemias: Molecular Structure-Function Relationships of Naturally Occurring Mutations in the γ Chain of Human Fibrinogen Blood. 92: 2195-2212. DOI: 10.1182/Blood.V92.7.2195.2195_2195_2212 |
0.315 |
|
| 1997 |
Okumura N, Gorkun OV, Lord ST. Severely impaired polymerization of recombinant fibrinogen gamma-364 Asp --> His, the substitution discovered in a heterozygous individual. The Journal of Biological Chemistry. 272: 29596-601. PMID 9368024 DOI: 10.1074/Jbc.272.47.29596 |
0.431 |
|
| 1997 |
Malkowski MG, Martin PD, Lord ST, Edwards BF. Crystal structure of fibrinogen-Aalpha peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16. The Biochemical Journal. 326: 815-22. PMID 9307032 DOI: 10.1042/Bj3260815 |
0.348 |
|
| 1997 |
Smith RA, Mosesson MW, Rooney MM, Lord ST, Daniels AU, Gartner TK. The role of putative fibrinogen Aalpha-, Bbeta-, and GammaA-chain integrin binding sites in endothelial cell-mediated clot retraction. The Journal of Biological Chemistry. 272: 22080-5. PMID 9268349 DOI: 10.1074/Jbc.272.35.22080 |
0.402 |
|
| 1997 |
Gorkun OV, Veklich YI, Weisel JW, Lord ST. The conversion of fibrinogen to fibrin: recombinant fibrinogen typifies plasma fibrinogen. Blood. 89: 4407-14. PMID 9192765 DOI: 10.1182/Blood.V89.12.4407 |
0.342 |
|
| 1997 |
Chen Q, Lord ST, Lentz BR. Partially purified Echis carinatus venom cleaves active-site-mutated bovine prothrombin at two sites. Thrombosis Research. 85: 369-75. PMID 9076894 DOI: 10.1016/S0049-3848(97)00025-X |
0.311 |
|
| 1996 |
Chen Q, Lord ST, Lentz BR. Construction, properties and specific fluorescent labeling of a bovine prothrombin mutant engineered with a free C-terminal cysteine. Protein Engineering. 9: 545-53. PMID 8862556 DOI: 10.1093/Protein/9.6.545 |
0.316 |
|
| 1996 |
Lord ST, Strickland E, Jayjock E. Strategy for recombinant multichain protein synthesis: fibrinogen B beta-chain variants as thrombin substrates. Biochemistry. 35: 2342-8. PMID 8652575 DOI: 10.1021/Bi952353U |
0.364 |
|
| 1996 |
Rooney MM, Parise LV, Lord ST. Dissecting clot retraction and platelet aggregation. Clot retraction does not require an intact fibrinogen gamma chain C terminus. The Journal of Biological Chemistry. 271: 8553-5. PMID 8621481 DOI: 10.1074/Jbc.271.15.8553 |
0.392 |
|
| 1996 |
Lord ST, Strickland E, Jayjock E, Rooney MM. Fibrinogen residues that are critical for thrombin binding: Assessment with engineered variants Fibrinolysis. 10: 10. DOI: 10.1016/S0268-9499(96)80787-9 |
0.334 |
|
| 1995 |
Lord ST, Rooney MM, Hopfner KP, Di Cera E. Binding of fibrinogen A alpha 1-50-beta-galactosidase fusion protein to thrombin stabilizes the slow form. The Journal of Biological Chemistry. 270: 24790-3. PMID 7559597 DOI: 10.1074/Jbc.270.42.24790 |
0.409 |
|
| 1994 |
Wada Y, Lord ST. A correlation between thrombotic disease and a specific fibrinogen abnormality (A alpha 554 Arg-->Cys) in two unrelated kindred, Dusart and Chapel Hill III. Blood. 84: 3709-14. PMID 7949126 DOI: 10.1182/Blood.V84.11.3709.Bloodjournal84113709 |
0.309 |
|
| 1993 |
Koopman J, Haverkate F, Grimbergen J, Lord ST, Mosesson MW, DiOrio JP, Siebenlist KS, Legrand C, Soria J, Soria C. Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia. The Journal of Clinical Investigation. 91: 1637-43. PMID 8473507 DOI: 10.1172/Jci116371 |
0.362 |
|
| 1993 |
Lord ST, Binnie CG, Hettasch JM, Strickland E. Purification and characterization of recombinant human fibrinogen. Blood Coagulation & Fibrinolysis : An International Journal in Haemostasis and Thrombosis. 4: 55-9. PMID 8457652 DOI: 10.1097/00001721-199302000-00009 |
0.334 |
|
| 1993 |
Binnie CG, Hettasch JM, Strickland E, Lord ST. Characterization of purified recombinant fibrinogen: partial phosphorylation of fibrinopeptide A. Biochemistry. 32: 107-13. PMID 8418831 DOI: 10.1021/Bi00052A015 |
0.336 |
|
| 1992 |
Koopman J, Haverkate F, Lord ST, Grimbergen J, Mannucci PM. Molecular basis of fibrinogen Naples associated with defective thrombin binding and thrombophilia. Homozygous substitution of B beta 68 Ala----Thr. The Journal of Clinical Investigation. 90: 238-44. PMID 1634610 DOI: 10.1172/Jci115841 |
0.42 |
|
| 1992 |
Koopman J, Haverkate F, Grimbergen J, Engesser L, Nováková I, Kerst AF, Lord ST. Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes. Proceedings of the National Academy of Sciences of the United States of America. 89: 3478-82. PMID 1565641 DOI: 10.1073/Pnas.89.8.3478 |
0.357 |
|
| 1992 |
Koopman J, Haverkate F, Grimbergen J, Egbring R, Lord ST. Fibrinogen Marburg: a homozygous case of dysfibrinogenemia, lacking amino acids A alpha 461-610 (Lys 461 AAA-->stop TAA). Blood. 80: 1972-9. PMID 1391954 DOI: 10.1182/Blood.V80.8.1972.Bloodjournal8081972 |
0.336 |
|
| 1992 |
Hettasch JM, Bolyard MG, Lord ST. The residues AGDV of recombinant gamma chains of human fibrinogen must be carboxy-terminal to support human platelet aggregation. Thrombosis and Haemostasis. 68: 701-6. PMID 1287885 DOI: 10.1055/S-0038-1646347 |
0.376 |
|
| 1991 |
Bolyard MG, Lord ST. Mutagenesis of human fibrinogen gamma chain 259-411 synthesized in E. coli: further characterization of the role of the disulfide bond CYS326-CYS339 in calcium binding. Biochemical and Biophysical Research Communications. 174: 853-60. PMID 1993077 DOI: 10.1016/0006-291X(91)91496-Y |
0.395 |
|
| 1991 |
Binnie CG, Lord ST. A Synthetic Analog of Fibrinogen α27–50 Is an Inhibitor of Thrombin Thrombosis and Haemostasis. 65: 165-168. DOI: 10.1055/S-0038-1647477 |
0.37 |
|
| 1989 |
Ni F, Konishi Y, Frazier RB, Scheraga HA, Lord ST. High-resolution NMR studies of fibrinogen-like peptides in solution: interaction of thrombin with residues 1-23 of the A alpha chain of human fibrinogen. Biochemistry. 28: 3082-94. PMID 2742826 DOI: 10.1021/Bi00433A052 |
0.312 |
|
| 1989 |
Bolyard MG, Lord ST. Expression in Escherichia coli of the human fibrinogen B beta chain and its cleavage by thrombin. Blood. 73: 1202-6. PMID 2649171 DOI: 10.1182/Blood.V73.5.1202.1202 |
0.334 |
|
| 1989 |
Lord ST, Fowlkes DM. Expression of a fibrinogen fusion peptide in Escherichia coli: a model thrombin substrate for structure/function analysis. Blood. 73: 166-71. PMID 2642712 DOI: 10.1182/Blood.V73.1.166.166 |
0.36 |
|
| 1988 |
Denton PH, Fowlkes DM, Lord ST, Reisner HM. Hemophilia B Durham: a mutation in the first EGF-like domain of factor IX that is characterized by polymerase chain reaction. Blood. 72: 1407-11. PMID 3262389 DOI: 10.1182/Blood.V72.4.1407.Bloodjournal7241407 |
0.312 |
|
| 1988 |
Ni F, Scheraga HA, Lord ST. High-resolution NMR studies of fibrinogen-like peptides in solution: resonance assignments and conformational analysis of residues 1-23 of the A alpha chain of human fibrinogen. Biochemistry. 27: 4481-91. PMID 3166991 DOI: 10.1021/Bi00412A040 |
0.338 |
|
| 1988 |
Bolyard MG, Lord ST. High-level expression of a functional human fibrinogen gamma chain in Escherichia coli. Gene. 66: 183-92. PMID 3049244 DOI: 10.1016/0378-1119(88)90355-1 |
0.332 |
|
| 1981 |
Lord ST, Richards FM. The labeling with 8-azido-cyclic adenosine monophosphate of proteins in vesicles of sarcoplasmic reticulum from rabbit skeletal muscle. Biochimica Et Biophysica Acta. 649: 13-23. PMID 6272856 DOI: 10.1016/0005-2736(81)90003-1 |
0.447 |
|
| 1980 |
Lord ST, Breslow E. Synthesis of peptide spin-labels that bind to neurophysin and their application to distance measurements within neurophysin complexes Biochemistry. 19: 5593-5602. PMID 7459333 DOI: 10.1021/Bi00565A021 |
0.656 |
|
| 1979 |
Lord ST, Breslow E. Identification and observation of alkyl proton resonances of the amino-terminal residues of bovine neurophysins. Evidence for conformational differences between neurophysin-I and neurophysin-II International Journal of Peptide and Protein Research. 13: 71-77. PMID 33930 DOI: 10.1111/J.1399-3011.1979.Tb01851.X |
0.58 |
|
| 1978 |
Lord ST, Breslow E. Nuclear magnetic resonance spin label studies of neurophysin: Evidence for secondary peptide-binding sites Biochemical and Biophysical Research Communications. 80: 63-70. PMID 564188 DOI: 10.1016/0006-291X(78)91104-X |
0.633 |
|
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