| Year |
Citation |
Score |
| 2016 |
Kalli AC, Rog T, Vattulainen I, Campbell ID, Sansom MS. The Integrin Receptor in Biologically Relevant Bilayers: Insights from Molecular Dynamics Simulations. The Journal of Membrane Biology. PMID 27465729 DOI: 10.1007/S00232-016-9908-Z |
0.305 |
|
| 2014 |
Kalli AC, Campbell ID, Sansom MS. Interactions of the Kindlin Family Pleckstrin Homology Domains with Model Membranes Containing Zwitterionic Lipids and Phosphatidyl Inositol Phosphates Biophysical Journal. 106: 517a. DOI: 10.1016/J.Bpj.2013.11.2889 |
0.307 |
|
| 2013 |
Kalli AC, Campbell ID, Sansom MSP. Conformational Changes in Talin on Binding to Anionic Phospholipid Membranes Facilitate Signaling by Integrin Transmembrane Helices Plos Computational Biology. 9. PMID 24204243 DOI: 10.1371/Journal.Pcbi.1003316 |
0.333 |
|
| 2013 |
Calderwood DA, Campbell ID, Critchley DR. Talins and kindlins: Partners in integrin-mediated adhesion Nature Reviews Molecular Cell Biology. 14: 503-517. PMID 23860236 DOI: 10.1038/Nrm3624 |
0.327 |
|
| 2013 |
Bonet R, Vakonakis I, Campbell ID. Characterization of 14-3-3-ζ Interactions with integrin tails. Journal of Molecular Biology. 425: 3060-72. PMID 23763993 DOI: 10.1016/J.Jmb.2013.05.024 |
0.303 |
|
| 2013 |
Erat MC, Sladek B, Campbell ID, Vakonakis I. Structural analysis of collagen type I interactions with human fibronectin reveals a cooperative binding mode Journal of Biological Chemistry. 288: 17441-17450. PMID 23653354 DOI: 10.1074/Jbc.M113.469841 |
0.358 |
|
| 2013 |
Campbell ID. The evolution of protein NMR Biomedical Spectroscopy and Imaging. 2: 245-264. DOI: 10.3233/Bsi-130055 |
0.351 |
|
| 2013 |
Kalli AC, Campbell ID, Sansom MS. Computational Studies of Talin-Mediated Integrin Activation Biophysical Journal. 104: 430a-431a. DOI: 10.1016/J.Bpj.2012.11.2396 |
0.317 |
|
| 2012 |
Yates LA, Füzéry AK, Bonet R, Campbell ID, Gilbert RJC. Biophysical analysis of kindlin-3 reveals an elongated conformation and maps integrin binding to the membrane-distal β-subunit NPXY motif Journal of Biological Chemistry. 287: 37715-37731. PMID 22989875 DOI: 10.1074/Jbc.M112.415208 |
0.331 |
|
| 2012 |
Ruskamo S, Gilbert R, Hofmann G, Jiang P, Campbell ID, Ylänne J, Pentikäinen U. The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended. The Biochemical Journal. 446: 261-269. PMID 22676060 DOI: 10.1042/Bj20120361 |
0.351 |
|
| 2012 |
Tossavainen H, Koskela O, Jiang P, Ylänne J, Campbell ID, Kilpeläinen I, Permi P. Model of a six immunoglobulin-like domain fragment of filamin a (16-21) built using residual dipolar couplings Journal of the American Chemical Society. 134: 6660-6672. PMID 22452512 DOI: 10.1021/Ja2114882 |
0.372 |
|
| 2012 |
Phan IQ, Boyd J, Campbell ID. Dynamic studies of a fibronectin type I module pair at three frequencies: Anisotropic modelling and direct determination of conformational exchange. Journal of Biomolecular Nmr. 8: 369-78. PMID 20859776 DOI: 10.1007/Bf00228140 |
0.32 |
|
| 2011 |
Kalli AC, Hall BA, Campbell ID, Sansom MSP. A helix heterodimer in a lipid bilayer: Prediction of the structure of an integrin transmembrane domain via multiscale simulations Structure. 19: 1477-1484. PMID 22000516 DOI: 10.1016/J.Str.2011.07.014 |
0.321 |
|
| 2011 |
Pentikäinen U, Jiang P, Takala H, Ruskamo S, Campbell ID, Ylänne J. Assembly of a filamin four-domain fragment and the influence of splicing variant-1 on the structure Journal of Biological Chemistry. 286: 26921-26930. PMID 21636571 DOI: 10.1074/Jbc.M110.195958 |
0.367 |
|
| 2011 |
Campbell ID, Humphries MJ. Integrin structure, activation, and interactions. Cold Spring Harbor Perspectives in Biology. 3. PMID 21421922 DOI: 10.1101/Cshperspect.A004994 |
0.35 |
|
| 2010 |
Anthis NJ, Wegener KL, Critchley DR, Campbell ID. Structural diversity in integrin/talin interactions Structure. 18: 1654-1666. PMID 21134644 DOI: 10.1016/J.Str.2010.09.018 |
0.32 |
|
| 2010 |
Kalli AC, Wegener KL, Goult BT, Anthis NJ, Campbell ID, Sansom MSP. The Structure of the Talin/Integrin Complex at a Lipid Bilayer: An NMR and MD Simulation Study Structure. 18: 1280-1288. PMID 20947017 DOI: 10.1016/J.Str.2010.07.012 |
0.311 |
|
| 2010 |
Campbell ID. The talin FERM domain is not so FERM. Structure (London, England : 1993). 18: 1222-3. PMID 20947007 DOI: 10.1016/J.Str.2010.09.002 |
0.301 |
|
| 2010 |
Atkin KE, Brentnall AS, Harris G, Bingham RJ, Erat MC, Millard CJ, Schwarz-Linek U, Staunton D, Vakonakis I, Campbell ID, Potts JR. The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules Journal of Biological Chemistry. 285: 36977-36983. PMID 20843804 DOI: 10.1074/Jbc.M110.156935 |
0.34 |
|
| 2010 |
Erat MC, Schwarz-Linek U, Pickford AR, Farndale RW, Campbell ID, Vakonakis I. Implications for collagen binding from the crystallographic structure of fibronectin 6FnI1-2FnII7FnI Journal of Biological Chemistry. 285: 33764-33770. PMID 20739283 DOI: 10.1074/Jbc.M110.139394 |
0.357 |
|
| 2009 |
Anthis NJ, Haling JR, Oxley CL, Memo M, Wegener KL, Lim CJ, Ginsberg MH, Campbell ID. β integrin tyrosine phosphorylation is a conserved mechanism for regulating talin-induced integrin activation Journal of Biological Chemistry. 284: 36700-36710. PMID 19843520 DOI: 10.1074/Jbc.M109.061275 |
0.352 |
|
| 2009 |
Goult BT, Bouaouina M, Harburger DS, Bate N, Patel B, Anthis NJ, Campbell ID, Calderwood DA, Barsukov IL, Roberts GC, Critchley DR. The structure of the N-terminus of kindlin-1: a domain important for alphaiibbeta3 integrin activation. Journal of Molecular Biology. 394: 944-56. PMID 19804783 DOI: 10.1016/J.Jmb.2009.09.061 |
0.313 |
|
| 2009 |
Anthis NJ, Wegener KL, Ye F, Kim C, Goult BT, Lowe ED, Vakonakis I, Bate N, Critchley DR, Ginsberg MH, Campbell ID. The structure of an integrin/talin complex reveals the basis of inside-out signal transduction Embo Journal. 28: 3623-3632. PMID 19798053 DOI: 10.1038/Emboj.2009.287 |
0.338 |
|
| 2009 |
Hardy AP, Prokes I, Kelly L, Campbell ID, Schofield CJ. Asparaginyl beta-hydroxylation of proteins containing ankyrin repeat domains influences their stability and function. Journal of Molecular Biology. 392: 994-1006. PMID 19646994 DOI: 10.1016/J.Jmb.2009.07.070 |
0.362 |
|
| 2009 |
Vakonakis I, Staunton D, Ellis IR, Sarkies P, Flanagan A, Schor AM, Schor SL, Campbell ID. Motogenic sites in human fibronectin are masked by long range interactions. The Journal of Biological Chemistry. 284: 15668-75. PMID 19366708 DOI: 10.1074/Jbc.M109.003673 |
0.342 |
|
| 2009 |
Goult BT, Bate N, Anthis NJ, Wegener KL, Gingras AR, Patel B, Barsukov IL, Campbell ID, Roberts GC, Critchley DR. The structure of an interdomain complex that regulates talin activity. The Journal of Biological Chemistry. 284: 15097-106. PMID 19297334 DOI: 10.1074/Jbc.M900078200 |
0.385 |
|
| 2009 |
Erat MC, Slatter DA, Lowe ED, Millard CJ, Farndale RW, Campbell ID, Vakonakis I. Identification and structural analysis of type i collagen sites in complex with fibronectin fragments Proceedings of the National Academy of Sciences of the United States of America. 106: 4195-4200. PMID 19251642 DOI: 10.1073/Pnas.0812516106 |
0.363 |
|
| 2009 |
Staunton D, Millard CJ, Aricescu AR, Campbell ID. Preparation of recombinant fibronectin fragments for functional and structural studies. Methods in Molecular Biology (Clifton, N.J.). 522: 73-99. PMID 19247602 DOI: 10.1007/978-1-59745-413-1_5 |
0.325 |
|
| 2009 |
Verdone G, Corazza A, Colebrooke SA, Cicero D, Eliseo T, Boyd J, Doliana R, Fogolari F, Viglino P, Colombatti A, Campbell ID, Esposito G. NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1 Journal of Biomolecular Nmr. 43: 79-96. PMID 19023665 DOI: 10.1007/S10858-008-9290-Y |
0.413 |
|
| 2008 |
Lorenz S, Vakonakis I, Lowe ED, Campbell ID, Noble ME, Hoellerer MK. Structural analysis of the interactions between paxillin LD motifs and alpha-parvin. Structure (London, England : 1993). 16: 1521-31. PMID 18940607 DOI: 10.1016/J.Str.2008.08.007 |
0.664 |
|
| 2008 |
Lad Y, Jiang P, Ruskamo S, Harburger DS, Ylänne J, Campbell ID, Calderwood DA. Structural basis of the migfilin-filamin interaction and competition with integrin β tails Journal of Biological Chemistry. 283: 35154-35163. PMID 18829455 DOI: 10.1074/Jbc.M802592200 |
0.372 |
|
| 2008 |
Jiang P, Campbell ID. Integrin binding immunoglobulin type filamin domains have variable stability Biochemistry. 47: 11055-11061. PMID 18817417 DOI: 10.1021/Bi8011466 |
0.348 |
|
| 2008 |
Wegener KL, Campbell ID. Transmembrane and cytoplasmic domains in integrin activation and protein-protein interactions (review). Molecular Membrane Biology. 25: 376-87. PMID 18654929 DOI: 10.1080/09687680802269886 |
0.344 |
|
| 2008 |
Wegener KL, Basran J, Bagshaw CR, Campbell ID, Roberts GC, Critchley DR, Barsukov IL. Structural basis for the interaction between the cytoplasmic domain of the hyaluronate receptor layilin and the talin F3 subdomain. Journal of Molecular Biology. 382: 112-26. PMID 18638481 DOI: 10.1016/J.Jmb.2008.06.087 |
0.353 |
|
| 2008 |
Vakonakis I, Langenhan T, Prömel S, Russ A, Campbell ID. Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain. Structure (London, England : 1993). 16: 944-53. PMID 18547526 DOI: 10.1016/J.Str.2008.02.020 |
0.371 |
|
| 2008 |
Verdone G, Doliana R, Corazza A, Colebrooke SA, Spessotto P, Bot S, Bucciotti F, Capuano A, Silvestri A, Viglino P, Campbell ID, Colombatti A, Esposito G. The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin. The Journal of Biological Chemistry. 283: 18947-56. PMID 18463100 DOI: 10.1074/Jbc.M801085200 |
0.373 |
|
| 2008 |
Campbell ID. Studies of focal adhesion assembly. Biochemical Society Transactions. 36: 263-6. PMID 18363570 DOI: 10.1042/Bst0360263 |
0.306 |
|
| 2008 |
Oxley CL, Anthis NJ, Lowe ED, Vakonakis I, Campbell ID, Wegener KL. An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding. The Journal of Biological Chemistry. 283: 5420-6. PMID 18156175 DOI: 10.1074/Jbc.M709435200 |
0.347 |
|
| 2007 |
Millard CJ, Ellis IR, Pickford AR, Schor AM, Schor SL, Campbell ID. The role of the fibronectin IGD motif in stimulating fibroblast migration. The Journal of Biological Chemistry. 282: 35530-5. PMID 17921136 DOI: 10.1074/Jbc.M707532200 |
0.329 |
|
| 2007 |
Lad Y, Kiema T, Jiang P, Pentikäinen OT, Coles CH, Campbell ID, Calderwood DA, Ylänne J. Structure of three tandem filamin domains reveals auto-inhibition of ligand binding. The Embo Journal. 26: 3993-4004. PMID 17690686 DOI: 10.1038/Sj.Emboj.7601827 |
0.379 |
|
| 2007 |
Vakonakis I, Staunton D, Rooney LM, Campbell ID. Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis. The Embo Journal. 26: 2575-83. PMID 17464288 DOI: 10.1038/Sj.Emboj.7601694 |
0.357 |
|
| 2007 |
Blundell CD, Mahoney DJ, Cordell MR, Almond A, Kahmann JD, Perczel A, Taylor JD, Campbell ID, Day AJ. Determining the molecular basis for the pH-dependent interaction between the link module of human TSG-6 and hyaluronan. The Journal of Biological Chemistry. 282: 12976-88. PMID 17307731 DOI: 10.1074/Jbc.M611713200 |
0.32 |
|
| 2007 |
Banerji S, Wright AJ, Noble M, Mahoney DJ, Campbell ID, Day AJ, Jackson DG. Structures of the Cd44-hyaluronan complex provide insight into a fundamental carbohydrate-protein interaction. Nature Structural & Molecular Biology. 14: 234-9. PMID 17293874 DOI: 10.1038/Nsmb1201 |
0.545 |
|
| 2007 |
Wegener KL, Partridge AW, Han J, Pickford AR, Liddington RC, Ginsberg MH, Campbell ID. Structural basis of integrin activation by talin. Cell. 128: 171-82. PMID 17218263 DOI: 10.1016/J.Cell.2006.10.048 |
0.357 |
|
| 2006 |
Staunton D, Schlinkert R, Zanetti G, Colebrook SA, Campbell ID. Cell-free expression and selective isotope labelling in protein NMR. Magnetic Resonance in Chemistry : Mrc. 44: S2-9. PMID 16826537 DOI: 10.1002/Mrc.1835 |
0.323 |
|
| 2006 |
Kiema T, Lad Y, Jiang P, Oxley CL, Baldassarre M, Wegener KL, Campbell ID, Ylänne J, Calderwood DA. The molecular basis of filamin binding to integrins and competition with talin. Molecular Cell. 21: 337-47. PMID 16455489 DOI: 10.1016/J.Molcel.2006.01.011 |
0.365 |
|
| 2006 |
Pilka ES, Werner JM, Schwarz-Linek U, Pickford AR, Meenan NA, Campbell ID, Potts JR. Structural insight into binding of Staphylococcus aureus to human fibronectin. Febs Letters. 580: 273-7. PMID 16376343 DOI: 10.1016/J.Febslet.2005.12.008 |
0.351 |
|
| 2006 |
Deschamps M, Campbell ID. Cooling overall spin temperature: protein NMR experiments optimized for longitudinal relaxation effects. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 178: 206-11. PMID 16249110 DOI: 10.1016/J.Jmr.2005.09.011 |
0.647 |
|
| 2005 |
Hofmann G, Schweimer K, Kiessling A, Hofinger E, Bauer F, Hoffmann S, Rösch P, Campbell ID, Werner JM, Sticht H. Binding, domain orientation, and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases. Biochemistry. 44: 13043-50. PMID 16185072 DOI: 10.1021/Bi050814Y |
0.323 |
|
| 2005 |
Trempe JF, Brown NR, Lowe ED, Gordon C, Campbell ID, Noble ME, Endicott JA. Mechanism of Lys48-linked polyubiquitin chain recognition by the Mud1 UBA domain. The Embo Journal. 24: 3178-89. PMID 16138082 DOI: 10.1038/Sj.Emboj.7600797 |
0.561 |
|
| 2005 |
Millard CJ, Campbell ID, Pickford AR. Gelatin binding to the 8F19F1 module pair of human fibronectin requires site-specific N-glycosylation. Febs Letters. 579: 4529-34. PMID 16083879 DOI: 10.1016/J.Febslet.2005.05.082 |
0.38 |
|
| 2005 |
Colebrooke SA, Blundell CD, DeAngelis PL, Campbell ID, Almond A. Exploiting the carboxylate chemical shift to resolve degenerate resonances in spectra of 13C-labelled glycosaminoglycans. Magnetic Resonance in Chemistry : Mrc. 43: 805-15. PMID 15996005 DOI: 10.1002/Mrc.1620 |
0.342 |
|
| 2005 |
Deschamps ML, Pilka ES, Potts JR, Campbell ID, Boyd J. Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE). Journal of Biomolecular Nmr. 31: 155-60. PMID 15772755 DOI: 10.1007/S10858-004-7912-6 |
0.634 |
|
| 2005 |
Blundell CD, Almond A, Mahoney DJ, DeAngelis PL, Campbell ID, Day AJ. Towards a structure for a TSG-6.hyaluronan complex by modeling and NMR spectroscopy: insights into other members of the link module superfamily. The Journal of Biological Chemistry. 280: 18189-201. PMID 15718240 DOI: 10.1074/Jbc.M414343200 |
0.39 |
|
| 2005 |
Neerathilingam M, Greene LH, Colebrooke SA, Campbell ID, Staunton D. Quantitation of protein expression in a cell-free system: Efficient detection of yields and 19F NMR to identify folded protein. Journal of Biomolecular Nmr. 31: 11-9. PMID 15692735 DOI: 10.1007/S10858-004-5357-6 |
0.339 |
|
| 2005 |
de Pereda JM, Wegener KL, Santelli E, Bate N, Ginsberg MH, Critchley DR, Campbell ID, Liddington RC. Structural basis for phosphatidylinositol phosphate kinase type Igamma binding to talin at focal adhesions. The Journal of Biological Chemistry. 280: 8381-6. PMID 15623515 DOI: 10.1074/Jbc.M413180200 |
0.337 |
|
| 2005 |
Deschamps M, Campbell ID, Boyd J. Residual dipolar couplings and some specific models for motional averaging. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 172: 118-32. PMID 15589415 DOI: 10.1016/J.Jmr.2004.09.023 |
0.596 |
|
| 2004 |
Altroff H, Schlinkert R, van der Walle CF, Bernini A, Campbell ID, Werner JM, Mardon HJ. Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin. The Journal of Biological Chemistry. 279: 55995-6003. PMID 15485890 DOI: 10.1074/Jbc.M406976200 |
0.327 |
|
| 2004 |
Campbell ID, Ginsberg MH. The talin-tail interaction places integrin activation on FERM ground. Trends in Biochemical Sciences. 29: 429-35. PMID 15362227 DOI: 10.1016/J.Tibs.2004.06.005 |
0.306 |
|
| 2004 |
Pickford AR, Campbell ID. NMR studies of modular protein structures and their interactions. Chemical Reviews. 104: 3557-66. PMID 15303827 DOI: 10.1021/Cr0304018 |
0.36 |
|
| 2004 |
Schwarz-Linek U, Pilka ES, Pickford AR, Kim JH, Höök M, Campbell ID, Potts JR. High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules. The Journal of Biological Chemistry. 279: 39017-25. PMID 15247227 DOI: 10.1074/Jbc.M405083200 |
0.386 |
|
| 2004 |
Verdone G, Colebrooke SA, Boyd J, Viglino P, Corazza A, Doliana R, Mungiguerra G, Colombatti A, Esposito G, Campbell ID. Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1. Journal of Biomolecular Nmr. 29: 91-2. PMID 15017143 DOI: 10.1023/B:Jnmr.0000019460.94913.6A |
0.327 |
|
| 2004 |
Teriete P, Banerji S, Noble M, Blundell CD, Wright AJ, Pickford AR, Lowe E, Mahoney DJ, Tammi MI, Kahmann JD, Campbell ID, Day AJ, Jackson DG. Structure of the regulatory hyaluronan binding domain in the inflammatory leukocyte homing receptor CD44. Molecular Cell. 13: 483-96. PMID 14992719 DOI: 10.1016/S1097-2765(04)00080-2 |
0.532 |
|
| 2004 |
Ulmer TS, Campbell ID, Boyd J. Amide proton relaxation measurements employing a highly deuterated protein. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 166: 190-201. PMID 14729031 DOI: 10.1016/J.Jmr.2003.10.012 |
0.337 |
|
| 2004 |
Teriete P, Banerji S, Blundell C, Kahmann J, Pickford A, Wright A, Campbell I, Jackson D, Day A. Solution Structure Of The Hyaluronan Binding Domain Of Human Cd44 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1Poz/Pdb |
0.31 |
|
| 2004 |
Verdone G, Colebrooke S, Boyd J, Viglino P, Corazza A, Esposito G, Campbell I. Backbone chemical shift assignments for the C-terminal globular domain of EMILIN-1 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5882 |
0.312 |
|
| 2004 |
Wright A, Banerji S, Noble M, Jackson D, Campbell I, Day A. Analysis of CD44 hyaluronan-binding domain mutants by NMR International Journal of Experimental Pathology. 85: A77-A77. DOI: 10.1111/J.0959-9673.2004.390As.X |
0.537 |
|
| 2003 |
Brown PJ, Mulvey D, Potts JR, Tomley FM, Campbell ID. Solution structure of a PAN module from the apicomplexan parasite Eimeria tenella. Journal of Structural and Functional Genomics. 4: 227-34. PMID 15185963 DOI: 10.1023/B:Jsfg.0000016118.87333.03 |
0.329 |
|
| 2003 |
Gao M, Craig D, Lequin O, Campbell ID, Vogel V, Schulten K. Structure and functional significance of mechanically unfolded fibronectin type III1 intermediates. Proceedings of the National Academy of Sciences of the United States of America. 100: 14784-9. PMID 14657397 DOI: 10.1073/Pnas.2334390100 |
0.323 |
|
| 2003 |
Campbell ID. Modular proteins at the cell surface. Biochemical Society Transactions. 31: 1107-14. PMID 14641006 DOI: 10.1042/Bst0311107 |
0.342 |
|
| 2003 |
Hoellerer MK, Noble ME, Labesse G, Campbell ID, Werner JM, Arold ST. Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain. Structure (London, England : 1993). 11: 1207-17. PMID 14527389 DOI: 10.1016/J.Str.2003.08.010 |
0.564 |
|
| 2003 |
Clarkson J, Campbell ID. Studies of protein-ligand interactions by NMR. Biochemical Society Transactions. 31: 1006-9. PMID 14505469 DOI: 10.1042/Bst0311006 |
0.351 |
|
| 2003 |
Blundell CD, Mahoney DJ, Almond A, DeAngelis PL, Kahmann JD, Teriete P, Pickford AR, Campbell ID, Day AJ. The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding. The Journal of Biological Chemistry. 278: 49261-70. PMID 12972412 DOI: 10.1074/Jbc.M309623200 |
0.389 |
|
| 2003 |
Schwarz-Linek U, Werner JM, Pickford AR, Gurusiddappa S, Kim JH, Pilka ES, Briggs JA, Gough TS, Höök M, Campbell ID, Potts JR. Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper. Nature. 423: 177-81. PMID 12736686 DOI: 10.1038/Nature01589 |
0.327 |
|
| 2003 |
Clarkson J, Campbell ID, Yudkin MD. Phosphorylation induces subtle structural changes in SpoIIAA, a key regulator of sporulation. The Biochemical Journal. 372: 113-9. PMID 12585962 DOI: 10.1042/Bj20021748 |
0.321 |
|
| 2003 |
García-Alvarez B, de Pereda JM, Calderwood DA, Ulmer TS, Critchley D, Campbell ID, Ginsberg MH, Liddington RC. Structural determinants of integrin recognition by talin. Molecular Cell. 11: 49-58. PMID 12535520 DOI: 10.1016/S1097-2765(02)00823-7 |
0.37 |
|
| 2003 |
Smallridge RS, Whiteman P, Werner JM, Campbell ID, Handford PA, Downing AK. Solution structure and dynamics of a calcium binding epidermal growth factor-like domain pair from the neonatal region of human fibrillin-1. The Journal of Biological Chemistry. 278: 12199-206. PMID 12511552 DOI: 10.1074/Jbc.M208266200 |
0.344 |
|
| 2002 |
Ulmer TS, Campbell ID, Boyd J. The effects of dissolved oxygen upon amide proton relaxation and chemical shift in a perdeuterated protein. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 157: 181-9. PMID 12323136 DOI: 10.1006/Jmre.2002.2585 |
0.308 |
|
| 2002 |
Ulmer TS, Werner JM, Campbell ID. SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn. Structure (London, England : 1993). 10: 901-11. PMID 12121645 DOI: 10.1016/S0969-2126(02)00781-5 |
0.323 |
|
| 2002 |
Boyd J, Campbell ID, Downing AK. The use of dipolar couplings for the structure refinement of a pair of calcium-binding EGF domains. Methods in Molecular Biology (Clifton, N.J.). 173: 301-16. PMID 11859771 DOI: 10.1385/1-59259-184-1:301 |
0.313 |
|
| 2002 |
Werner JM, Campbell ID, Downing AK. Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relaxation. Methods in Molecular Biology (Clifton, N.J.). 173: 285-300. PMID 11859769 DOI: 10.1385/1-59259-184-1:285 |
0.317 |
|
| 2002 |
Yuan X, Werner JM, Lack J, Knott V, Handford PA, Campbell ID, Downing AK. Effects of the N2144S mutation on backbone dynamics of a TB-cbEGF domain pair from human fibrillin-1. Journal of Molecular Biology. 316: 113-25. PMID 11829507 DOI: 10.1006/Jmbi.2001.5329 |
0.342 |
|
| 2001 |
Clarkson J, Campbell ID, Yudkin MD. NMR studies of the interactions of SpoIIAA with its partner proteins that regulate sporulation in Bacillus subtilis. Journal of Molecular Biology. 314: 359-64. PMID 11846550 DOI: 10.1006/Jmbi.2001.5142 |
0.34 |
|
| 2001 |
Altroff H, van der Walle CF, Asselin J, Fairless R, Campbell ID, Mardon HJ. The eighth FIII domain of human fibronectin promotes integrin alpha5beta1 binding via stabilization of the ninth FIII domain. The Journal of Biological Chemistry. 276: 38885-92. PMID 11500513 DOI: 10.1074/Jbc.M105868200 |
0.359 |
|
| 2001 |
Saha S, Boyd J, Werner JM, Knott V, Handford PA, Campbell ID, Downing AK. Solution structure of the LDL receptor EGF-AB pair: a paradigm for the assembly of tandem calcium binding EGF domains. Structure (London, England : 1993). 9: 451-6. PMID 11435110 DOI: 10.1016/S0969-2126(01)00606-2 |
0.335 |
|
| 2001 |
Ulmer TS, Yaspan B, Ginsberg MH, Campbell ID. NMR analysis of structure and dynamics of the cytosolic tails of integrin αIIβ3 in aqueous solution Biochemistry. 40: 7498-7508. PMID 11412103 DOI: 10.1021/Bi010338L |
0.377 |
|
| 2001 |
Schwarz-Linek U, Plevin MJ, Pickford AR, Höök M, Campbell ID, Potts JR. Binding of a peptide from a Streptococcus dysgalactiae MSCRAMM to the N-terminal F1 module pair of human fibronectin involves both modules Febs Letters. 497: 137-140. PMID 11377428 DOI: 10.1016/S0014-5793(01)02418-8 |
0.338 |
|
| 2001 |
Kovacs H, Comfort D, Lord M, Yudkin M, Campbell ID, Nilges M. NMR studies of the sporulation protein SpoIIAA: Implications for the regulation of the transcription factor σF in Bacillus subtilis Journal of Biomolecular Nmr. 19: 293-304. PMID 11370776 DOI: 10.1023/A:1011247523112 |
0.328 |
|
| 2001 |
Arold ST, Ulmer TS, Mulhern TD, Werner JM, Ladbury JE, Campbell ID, Noble ME. The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases. The Journal of Biological Chemistry. 276: 17199-205. PMID 11278857 DOI: 10.1074/Jbc.M011185200 |
0.536 |
|
| 2000 |
Hashimoto Y, Smith SP, Pickford AR, Bocquier AA, Campbell ID, Werner JM. The relative orientation of the fibronectin 6F1(1)F2 module pair: a 15N NMR relaxation study. Journal of Biomolecular Nmr. 17: 203-14. PMID 10959628 DOI: 10.1023/A:1008341609461 |
0.31 |
|
| 2000 |
Kahmann JD, O'Brien R, Werner JM, Heinegârd D, Ladbury JE, Campbell ID, Day AJ. Localization and characterization of the hyaluronan-binding site on the link module from human TSG-6. Structure (London, England : 1993). 8: 763-74. PMID 10903951 DOI: 10.1016/S0969-2126(00)00163-5 |
0.353 |
|
| 2000 |
Corbett EF, Michalak KM, Oikawa K, Johnson S, Campbell ID, Eggleton P, Kay C, Michalak M. The conformation of calreticulin is influenced by the endoplasmic reticulum luminal environment. The Journal of Biological Chemistry. 275: 27177-85. PMID 10842171 DOI: 10.1074/Jbc.M002049200 |
0.33 |
|
| 2000 |
Bright JR, Pickford AR, Potts JR, Campbell ID. Preparation of isotopically labeled recombinant fragments of fibronectin for functional and structural study by heteronuclear nuclear magnetic resonance spectroscopy Methods in Molecular Biology (Clifton, N.J.). 139: 59-69. PMID 10840778 DOI: 10.1385/1-59259-063-2:59 |
0.315 |
|
| 2000 |
Penkett CJ, Dobson CM, Smith LJ, Bright JR, Pickford AR, Campbell ID, Potts JR. Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the 4F15F1 module pair of human fibronectin using heteronuclear NMR spectroscopy Biochemistry. 39: 2887-2893. PMID 10715108 DOI: 10.1021/Bi992267K |
0.486 |
|
| 2000 |
Werner JM, Knott V, Handford PA, Campbell ID, Downing AK. Backbone dynamics of a cbEGF domain pair in the presence of calcium. Journal of Molecular Biology. 296: 1065-78. PMID 10686104 DOI: 10.1006/Jmbi.1999.3513 |
0.335 |
|
| 2000 |
Bocquier AA, Potts JR, Pickford AR, Campbell ID. Solution structure of a pair of modules from the gelatin-binding domain of fibronectin. Structure (London, England : 1993). 7: 1451-60. PMID 10647176 DOI: 10.1016/S0969-2126(00)88336-7 |
0.348 |
|
| 2000 |
Noble M, Arold S, Brown N, Campbell I, Endicott JA, Gruber J, Johnson L, Ladbury J, Tucker J, Ulmer T. Molecular recognition in the action of protein kinases: the basis for affinity and specificity Acta Crystallographica Section a Foundations of Crystallography. 56: s102-s102. DOI: 10.1107/S010876730002273X |
0.452 |
|
| 1999 |
Potts JR, Bright JR, Bolton D, Pickford AR, Campbell ID. Solution structure of the N-terminal F1 module pair from human fibronectin Biochemistry. 38: 8304-8312. PMID 10387076 DOI: 10.1021/Bi990202B |
0.349 |
|
| 1998 |
Kovacs H, Campbell ID, Strong P, Johnson S, Ward FJ, Reid KB, Eggleton P. Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation. Biochemistry. 37: 17865-74. PMID 9922153 DOI: 10.1021/Bi973197P |
0.323 |
|
| 1998 |
Yuan X, Werner JM, Knott V, Handford PA, Campbell ID, Downing K. Effects of proline cis-trans isomerization on TB domain secondary structure. Protein Science : a Publication of the Protein Society. 7: 2127-35. PMID 9792099 DOI: 10.1002/Pro.5560071009 |
0.374 |
|
| 1998 |
Mal TK, Matthews SJ, Kovacs H, Campbell ID, Boyd J. Some NMR experiments and a structure determination employing a [15N,2H] enriched protein. Journal of Biomolecular Nmr. 12: 259-76. PMID 9751998 DOI: 10.1023/A:1008238009056 |
0.391 |
|
| 1998 |
Campbell ID, Downing AK. NMR of modular proteins. Nature Structural Biology. 496-9. PMID 9665177 DOI: 10.1038/733 |
0.36 |
|
| 1998 |
Kovacs H, Comfort D, Lord M, Campbell ID, Yudkin MD. Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigmaF of Bacillus subtilis. Proceedings of the National Academy of Sciences of the United States of America. 95: 5067-71. PMID 9560229 DOI: 10.1073/Pnas.95.9.5067 |
0.336 |
|
| 1998 |
Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM. Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. Journal of Molecular Biology. 276: 657-67. PMID 9551103 DOI: 10.1006/Jmbi.1997.1553 |
0.648 |
|
| 1998 |
Guijarro JI, Sunde M, Jones JA, Campbell ID, Dobson CM. Amyloid fibril formation by an SH3 domain. Proceedings of the National Academy of Sciences of the United States of America. 95: 4224-8. PMID 9539718 DOI: 10.1073/pnas.95.8.4224 |
0.399 |
|
| 1998 |
Sticht H, Pickford AR, Potts JR, Campbell ID. Solution structure of the glycosylated second type 2 module of fibronectin. Journal of Molecular Biology. 276: 177-87. PMID 9514732 DOI: 10.1006/Jmbi.1997.1528 |
0.381 |
|
| 1998 |
Plaxco KW, Guijarro JI, Morton CJ, Pitkeathly M, Campbell ID, Dobson CM. The folding kinetics and thermodynamics of the Fyn-SH3 domain. Biochemistry. 37: 2529-37. PMID 9485402 DOI: 10.1021/Bi972075U |
0.591 |
|
| 1998 |
Boyd J, Mal TK, Soffe N, Campbell ID. The influence of a scalar-coupled deuterium upon the relaxaton of a 15N Nucleus and its possible exploitation as a probe for side-chain interactions in proteins. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 124: 61-71. PMID 9424319 DOI: 10.1006/Jmre.1996.7482 |
0.323 |
|
| 1997 |
Plaxco KW, Morton CJ, Grimshaw SB, Jones JA, Pitkeathly M, Campbell ID, Dobson CM. The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG. Journal of Biomolecular Nmr. 10: 221-30. PMID 20700831 DOI: 10.1023/A:1018340217891 |
0.607 |
|
| 1997 |
Mulhern TD, Shaw GL, Morton CJ, Day AJ, Campbell ID. The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity. Structure (London, England : 1993). 5: 1313-23. PMID 9351806 DOI: 10.1016/S0969-2126(97)00283-9 |
0.379 |
|
| 1997 |
Wiles AP, Shaw G, Bright J, Perczel A, Campbell ID, Barlow PN. NMR studies of a viral protein that mimics the regulators of complement activation. Journal of Molecular Biology. 272: 253-65. PMID 9299352 DOI: 10.1006/Jmbi.1997.1241 |
0.375 |
|
| 1997 |
Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM. A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules. Journal of Molecular Biology. 270: 763-70. PMID 9245603 DOI: 10.1006/Jmbi.1997.1148 |
0.608 |
|
| 1997 |
Pickford AR, Potts JR, Bright JR, Phan I, Campbell ID. Solution structure of a type 2 module from fibronectin: Implications for the structure and function of the gelatin-binding domain Structure. 5: 359-370. PMID 9083105 DOI: 10.1016/S0969-2126(97)00193-7 |
0.366 |
|
| 1997 |
Spitzfaden C, Grant RP, Mardon HJ, Campbell ID. Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity. Journal of Molecular Biology. 265: 565-79. PMID 9048949 DOI: 10.1006/Jmbi.1996.0736 |
0.365 |
|
| 1997 |
Grant RP, Spitzfaden C, Altroff H, Campbell ID, Mardon HJ. Structural requirements for biological activity of the ninth and tenth FIII domains of human fibronectin. The Journal of Biological Chemistry. 272: 6159-66. PMID 9045628 DOI: 10.1074/Jbc.272.10.6159 |
0.365 |
|
| 1997 |
Shaw GL, Müller T, Mott HR, Oschkinat H, Campbell ID, Mitschang L. Constant-Time HQQC Experiment for Protein NMR Spectroscopy Journal of Magnetic Resonance. 124: 479-483. DOI: 10.1006/Jmre.1996.1062 |
0.331 |
|
| 1996 |
Renzoni DA, Pugh DJR, Siligardi G, Das P, Morton CJ, Rossi C, Waterfield MD, Campbell ID, Ladbury JE. Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase Biochemistry. 35: 15646-15653. PMID 8961927 DOI: 10.1021/Bi9620969 |
0.351 |
|
| 1996 |
Plaxco KW, Spitzfaden C, Campbell ID, Dobson CM. Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module. Proceedings of the National Academy of Sciences of the United States of America. 93: 10703-6. PMID 8855243 DOI: 10.1073/Pnas.93.20.10703 |
0.617 |
|
| 1996 |
Morton CJ, Pugh DJ, Brown EL, Kahmann JD, Renzoni DA, Campbell ID. Solution structure and peptide binding of the SH3 domain from human Fyn. Structure (London, England : 1993). 4: 705-14. PMID 8805554 DOI: 10.1016/S0969-2126(96)00076-7 |
0.333 |
|
| 1996 |
Kohda D, Morton CJ, Parkar AA, Hatanaka H, Inagaki FM, Campbell ID, Day AJ. Solution structure of the link module: A hyaluronan-binding domain involved in extracellular matrix stability and cell migration Cell. 86: 767-775. PMID 8797823 DOI: 10.1016/S0092-8674(00)80151-8 |
0.382 |
|
| 1996 |
Ladbury JE, Hensmann M, Panayotou G, Campbell ID. Alternative modes of tyrosyl phosphopeptide binding to a Src family SH2 domain: implications for regulation of tyrosine kinase activity. Biochemistry. 35: 11062-9. PMID 8780508 DOI: 10.1021/Bi960543E |
0.365 |
|
| 1996 |
Pintar A, Hensmann M, Jumel K, Pitkeathly M, Harding SE, Campbell ID. Solution studies of the SH2 domain from the fyn tyrosine kinase: secondary structure, backbone dynamics and protein association. European Biophysics Journal : Ebj. 24: 371-80. PMID 8765711 DOI: 10.1007/Bf00576709 |
0.406 |
|
| 1996 |
Downing AK, Knott V, Werner JM, Cardy CM, Campbell ID, Handford PA. Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders. Cell. 85: 597-605. PMID 8653794 DOI: 10.1016/S0092-8674(00)81259-3 |
0.372 |
|
| 1995 |
Potts JR, Campbell ID. Fibronectin structure and assembly. Current Opinion in Cell Biology. 6: 648-55. PMID 7833045 DOI: 10.1016/0955-0674(94)90090-6 |
0.32 |
|
| 1995 |
Barlow PN, Campbell ID. Strategy for studying modular proteins: application to complement modules. Methods in Enzymology. 239: 464-85. PMID 7830595 DOI: 10.1016/S0076-6879(94)39018-5 |
0.329 |
|
| 1995 |
Mott HR, Baines BS, Hall RM, Cooke RM, Driscoll PC, Weir MP, Campbell ID. The solution structure of the F42A mutant of human interleukin 2. Journal of Molecular Biology. 247: 979-94. PMID 7723044 DOI: 10.1006/Jmbi.1994.0194 |
0.311 |
|
| 1995 |
Rudd PM, Woods RJ, Wormald MR, Opdenakker G, Downing AK, Campbell ID, Dwek RA. The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator. Biochimica Et Biophysica Acta. 1248: 1-10. PMID 7711052 DOI: 10.1016/0167-4838(94)00230-E |
0.486 |
|
| 1995 |
Saether O, Craik DJ, Campbell ID, Sletten K, Juul J, Norman DG. Elucidation of the primary and three-dimensional structure of the uterotonic polypeptide kalata B1. Biochemistry. 34: 4147-58. PMID 7703226 DOI: 10.1021/Bi00013A002 |
0.341 |
|
| 1995 |
Potts JR, Phan I, Williams MJ, Campbell ID. High-resolution structural studies of the factor XIIIa crosslinking site and the first type 1 module of fibronectin. Nature Structural Biology. 2: 946-50. PMID 7583666 DOI: 10.1038/Nsb1195-946 |
0.345 |
|
| 1995 |
Smith BO, Downing AK, Driscoll PC, Dudgeon TJ, Campbell ID. The solution structure and backbone dynamics of the fibronectin type I and epidermal growth factor-like pair of modules of tissue-type plasminogen activator. Structure (London, England : 1993). 3: 823-33. PMID 7582899 DOI: 10.1016/S0969-2126(01)00217-9 |
0.308 |
|
| 1995 |
Williams MJ, Campbell ID. Solution structures of molecular proteins by nuclear magnetic resonance Methods in Enzymology. 245: 451-469. DOI: 10.1016/0076-6879(94)45023-4 |
0.325 |
|
| 1994 |
Williams MJ, Phan I, Harvey TS, Rostagno A, Gold LI, Campbell ID. Solution structure of a pair of fibronectin type 1 modules with fibrin binding activity Journal of Molecular Biology. 235: 1302-1311. PMID 8308892 DOI: 10.1006/Jmbi.1994.1083 |
0.394 |
|
| 1994 |
Boyd J, Soffe N, Campbell I. NMR at very high fields. Structure (London, England : 1993). 2: 253-5. PMID 8087552 DOI: 10.1016/S0969-2126(00)00027-7 |
0.307 |
|
| 1994 |
Morton CJ, Campbell ID. SH3 Domains: Molecular 'Velcro'1 Current Biology. 4: 615-617. PMID 7953536 DOI: 10.1016/S0960-9822(00)00134-2 |
0.334 |
|
| 1994 |
Campbell ID, Downing AK. Building protein structure and function from modular units Trends in Biotechnology. 12: 168-172. PMID 7764899 DOI: 10.1016/0167-7799(94)90078-7 |
0.367 |
|
| 1994 |
Hensmann M, Booker GW, Panayotou G, Boyd J, Linacre J, Waterfield M, Campbell ID. Phosphopeptide binding to the N-terminal SH2 domain of the p85 alpha subunit of PI 3'-kinase: a heteronuclear NMR study. Protein Science : a Publication of the Protein Society. 3: 1020-30. PMID 7522724 DOI: 10.1002/Pro.5560030704 |
0.372 |
|
| 1994 |
Werner JM, Breeze AL, Kara B, Rosenbrock G, Boyd J, Soffe N, Campbell ID. Secondary structure and backbone dynamics of human granulocyte colony-stimulating factor in solution. Biochemistry. 33: 7184-92. PMID 7516182 DOI: 10.1021/Bi00189A022 |
0.356 |
|
| 1994 |
Kieffer B, Driscoll PC, Campbell ID, Willis AC, van der Merwe PA, Davis SJ. Three-Dimensional Solution Structure of the Extracellular Region of the Complement Regulatory Protein CD59, a New Cell-Surface Protein Domain Related to Snake Venom Neurotoxins Biochemistry. 33: 4471-4482. DOI: 10.2210/Pdb1Erg/Pdb |
0.36 |
|
| 1993 |
Barlow PN, Steinkasserer A, Norman DG, Kieffer B, Wiles AP, Sim RB, Campbell ID. Solution structure of a pair of complement modules by nuclear magnetic resonance. Journal of Molecular Biology. 232: 268-84. PMID 8331663 DOI: 10.1006/Jmbi.1993.1381 |
0.332 |
|
| 1993 |
Booker GW, Gout I, Downing AK, Driscoll PC, Boyd J, Waterfield MD, Campbell ID. Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase. Cell. 73: 813-22. PMID 7684655 DOI: 10.1016/0092-8674(93)90259-S |
0.369 |
|
| 1993 |
Gout I, Dhand R, Hiles ID, Fry MJ, Panayotou G, Das P, Truong O, Totty NF, Hsuan J, Booker GW, Campbell ID, Waterfield MD. The GTPase dynamin binds to and is activated by a subset of SH3 domains. Cell. 75: 25-36. DOI: 10.1016/S0092-8674(05)80081-9 |
0.362 |
|
| 1993 |
Williams MJ, Phan I, Baron M, Campbell ID, Applin RT. Toward the Structure of Mosaic Proteins: Expression, Purification and Structural Analysis of a Pair of Fibronectin Type1 Modules Techniques in Protein Chemistry. 623-631. DOI: 10.1016/B978-0-12-058757-5.50073-1 |
0.39 |
|
| 1992 |
Downing AK, Driscoll PC, Harvey TS, Dudgeon TJ, Smith BO, Baron M, Campbell ID. Solution structure of the fibrin binding finger domain of tissue-type plasminogen activator determined by 1H nuclear magnetic resonance Journal of Molecular Biology. 225: 821-833. PMID 1602484 DOI: 10.1016/0022-2836(92)90403-7 |
0.378 |
|
| 1992 |
Barlow PN, Norman DG, Steinkasserer A, Horne TJ, Pearce J, Driscoll PC, Sim RB, Campbell ID. Solution structure of the fifth repeat of factor H: a second example of the complement control protein module. Biochemistry. 31: 3626-34. PMID 1533152 DOI: 10.1021/Bi00129A011 |
0.328 |
|
| 1992 |
Hommel U, Harvey TS, Driscoll PC, Campbell ID. Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor α Journal of Molecular Biology. 227: 271-282. PMID 1522591 DOI: 10.1016/0022-2836(92)90697-I |
0.365 |
|
| 1992 |
Mott HR, Driscoll PC, Boyd J, Cooke RM, Weir MP, Campbell ID. Secondary structure of human interleukin 2 from 3D heteronuclear NMR experiments. Biochemistry. 31: 7741-4. PMID 1510960 DOI: 10.1021/Bi00148A040 |
0.329 |
|
| 1992 |
Mayhew M, Handford P, Baron M, Tse AG, Campbell ID, Brownlee GG. Ligand requirements for Ca2+ binding to EGF-like domains. Protein Engineering. 5: 489-94. PMID 1438159 DOI: 10.1093/Protein/5.6.489 |
0.319 |
|
| 1992 |
Steinkasserer A, Barlow PN, Willis AC, Kertesz Z, Campbell ID, Sim RB, Norman DG. Activity, disulphide mapping and structural modelling of the fifth domain of human beta 2-glycoprotein I. Febs Letters. 313: 193-7. PMID 1426288 DOI: 10.1016/0014-5793(92)81442-O |
0.326 |
|
| 1992 |
Main AL, Harvey TS, Baron M, Boyd J, Campbell ID. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell. 71: 671-8. PMID 1423622 DOI: 10.1016/0092-8674(92)90600-H |
0.375 |
|
| 1992 |
Booker GW, Breeze AL, Downing AK, Panayotou G, Gout I, Waterfield MD, Campbell ID. Structure of an SH2 domain of the p85 alpha subunit of phosphatidylinositol-3-OH kinase. Nature. 358: 684-7. PMID 1323062 DOI: 10.1038/358684A0 |
0.362 |
|
| 1992 |
Baron M, Main AL, Driscoll PC, Mardon HJ, Boyd J, Campbell ID. 1H NMR assignment and secondary structure of the cell adhesion type III module of fibronectin. Biochemistry. 31: 2068-73. PMID 1311202 DOI: 10.1021/Bi00122A025 |
0.388 |
|
| 1992 |
Baron M, Norman DG, Harvey TS, Handford PA, Mayhew M, Tse AG, Brownlee GG, Campbell ID. The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha. Protein Science : a Publication of the Protein Society. 1: 81-90. PMID 1304885 DOI: 10.1002/Pro.5560010109 |
0.343 |
|
| 1991 |
Cooke RM, Tappin MJ, Campbell ID, Kohda D, Miyake T, Fuwa T, Miyazawa T, Inagaki F. Nuclear-magnetic-resonance studies of human epidermal growth factor. European Journal of Biochemistry. 193: 807-15. PMID 2249695 DOI: 10.1111/J.1432-1033.1990.Tb19404.X |
0.36 |
|
| 1991 |
Harvey TS, Wilkinson AJ, Tappin MJ, Cooke RM, Campbell ID. The solution structure of human transforming growth factor α European Journal of Biochemistry. 198: 555-562. PMID 2050136 DOI: 10.1111/J.1432-1033.1991.Tb16050.X |
0.35 |
|
| 1991 |
Cooke RM, Harvey TS, Campbell ID. Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study. Biochemistry. 30: 5484-91. PMID 2036417 DOI: 10.1021/Bi00236A022 |
0.309 |
|
| 1991 |
Handford PA, Mayhew M, Baron M, Winship PR, Campbell ID, Brownlee GG. Key residues involved in calcium-binding motifs in EGF-like domains. Nature. 351: 164-7. PMID 2030732 DOI: 10.1038/351164A0 |
0.358 |
|
| 1991 |
Dempsey CE, Bazzo R, Harvey TS, Syperek I, Boheim G, Campbell ID. Contribution of proline-14 to the structure and actions of melittin. Febs Letters. 281: 240-4. PMID 2015901 DOI: 10.1016/0014-5793(91)80402-O |
0.365 |
|
| 1991 |
Breeze AL, Harvey TS, Bazzo R, Campbell ID. Solution structure of human calcitonin gene-related peptide by 1H NMR and distance geometry with restrained molecular dynamics. Biochemistry. 30: 575-82. PMID 1988044 DOI: 10.1021/Bi00216A036 |
0.381 |
|
| 1991 |
Campbell ID, Cooke RM. Structure function relationships in EGF, TGF-alpha and IGFI. Journal of Cell Science. Supplement. 13: 5-10. PMID 1964687 DOI: 10.1242/Jcs.1990.Supplement_13.2 |
0.342 |
|
| 1991 |
Hommel U, Dudgeon TJ, Fallon A, Edwards RM, Campbell ID. Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR. Biochemistry. 30: 8891-8. PMID 1909576 DOI: 10.1021/Bi00100A024 |
0.387 |
|
| 1991 |
Norman DG, Barlow PN, Baron M, Day AJ, Sim RB, Campbell ID. Three-dimensional structure of a complement control protein module in solution. Journal of Molecular Biology. 219: 717-25. PMID 1829116 DOI: 10.1016/0022-2836(91)90666-T |
0.371 |
|
| 1991 |
Barlow PN, Baron M, Norman DG, Day AJ, Willis AC, Sim RB, Campbell ID. Secondary structure of a complement control protein module by two-dimensional 1H NMR. Biochemistry. 30: 997-1004. PMID 1824927 DOI: 10.1021/Bi00218A016 |
0.385 |
|
| 1991 |
Campbell ID, Baron M. The structure and function of protein modules. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 332: 165-70. PMID 1678535 DOI: 10.1098/Rstb.1991.0045 |
0.353 |
|
| 1990 |
Handford PA, Baron M, Mayhew M, Willis A, Beesley T, Brownlee GG, Campbell ID. The first EGF-like domain from human factor IX contains a high-affinity calcium binding site. The Embo Journal. 9: 475-80. PMID 2406129 DOI: 10.1002/J.1460-2075.1990.Tb08133.X |
0.351 |
|
| 1990 |
Dudgeon TJ, Cooke RM, Baron M, Campbell ID, Edwards RM, Fallon A. Structure-function analysis of epidermal growth factor: site directed mutagenesis and nuclear magnetic resonance. Febs Letters. 261: 392-6. PMID 2178977 DOI: 10.1016/0014-5793(90)80600-N |
0.385 |
|
| 1990 |
Kim HW, Perez JA, Ferguson SJ, Campbell ID. The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate. Application to fluorotryptophan labelling to the H(+)-ATPase of Escherichia coli and NMR studies. Febs Letters. 272: 34-6. PMID 2146161 DOI: 10.1016/0014-5793(90)80442-L |
0.333 |
|
| 1990 |
Baron M, Norman D, Willis A, Campbell ID. Structure of the fibronectin type 1 module. Nature. 345: 642-6. PMID 2112232 DOI: 10.1038/345642A0 |
0.347 |
|
| 1990 |
Wennerberg AB, Cooke RM, Carlquist M, Rigler R, Campbell ID. A 1H NMR study of the solution conformation of the neuropeptide galanin. Biochemical and Biophysical Research Communications. 166: 1102-9. PMID 1689570 DOI: 10.1016/0006-291X(90)90980-2 |
0.329 |
|
| 1990 |
Norwood TJ, Boyd J, Soffe N, Campbell ID. New NMR technique for determining long-range heteronuclear proton-nitrogen-15 correlations in proteins Journal of the American Chemical Society. 112: 9638-9640. DOI: 10.1021/Ja00182A033 |
0.31 |
|
| 1990 |
Norwood TJ, Boyd J, Heritage JE, Soffe N, Campbell ID. Comparison of techniques for 1H-detected heteronuclear 1H15N Spectroscopy Journal of Magnetic Resonance (1969). 87: 488-501. DOI: 10.1016/0022-2364(90)90306-T |
0.306 |
|
| 1990 |
Boyd J, Hommel U, Campbell ID. Influence of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms upon longitudinal relaxation rates of 15N in macromolecules Chemical Physics Letters. 175: 477-482. DOI: 10.1016/0009-2614(90)85567-V |
0.307 |
|
| 1990 |
Carr MD, Mulvey D, Willis A, Ferguson SJ, Campbell ID. Nucleotide binding to active and 4-chloro-7-nitrobenzofurazan-inhibited forms of chloroplast F1-ATPase — an NMR study Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1015: 79-86. DOI: 10.1016/0005-2728(90)90218-S |
0.341 |
|
| 1990 |
Quirk PG, Campbell ID. 31P and 39K nuclear magnetic resonance spectroscopy studies of halobacterial bioenergetics Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1019: 81-90. DOI: 10.1016/0005-2728(90)90127-P |
0.307 |
|
| 1989 |
Pastore A, Harvey TS, Dempsey CE, Campbell ID. The dynamic properties of melittin in solution. Investigations by NMR and molecular dynamics. European Biophysics Journal : Ebj. 16: 363-7. PMID 2924737 DOI: 10.1007/Bf00257885 |
0.35 |
|
| 1989 |
Tappin MJ, Cooke RM, Fitton JE, Campbell ID. A high-resolution 1H-NMR study of human transforming growth factor alpha. Structure and pH-dependent conformational interconversion. European Journal of Biochemistry. 179: 629-37. PMID 2646119 DOI: 10.1111/J.1432-1033.1989.Tb14594.X |
0.315 |
|
| 1989 |
Norwood TJ, Boyd J, Campbell ID. Improved resolution in 1H-detected 1H-15N correlation experiments. Febs Letters. 255: 369-71. PMID 2529140 DOI: 10.1016/0014-5793(89)81124-X |
0.306 |
|
| 1989 |
Campbell ID, Cooke RM, Baron M, Harvey TS, Tappin MJ. The solution structures of epidermal growth factor and transforming growth factor alpha Progress in Growth Factor Research. 1: 13-22. PMID 2491252 DOI: 10.1016/0955-2235(89)90038-0 |
0.319 |
|
| 1988 |
Tappin MJ, Pastore A, Norton RS, Freer JH, Campbell ID. High-resolution 1H NMR study of the solution structure of delta-hemolysin. Biochemistry. 27: 1643-7. PMID 3365416 DOI: 10.1021/Bi00405A038 |
0.383 |
|
| 1988 |
Bazzo R, Tappin MJ, Pastore A, Harvey TS, Carver JA, Campbell ID. The structure of melittin. A 1H-NMR study in methanol European Journal of Biochemistry. 173: 139-146. PMID 3356186 DOI: 10.1111/J.1432-1033.1988.Tb13977.X |
0.375 |
|
| 1988 |
Cooke RM, Campbell ID. Protein structure determination by nuclear magnetic resonance. Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology. 8: 52-6. PMID 3282504 DOI: 10.1002/Bies.950080203 |
0.338 |
|
| 1988 |
Mitsumori F, Rees D, Brindle KM, Radda GK, Campbell ID. 31P-NMR saturation transfer studies of aerobic Escherichia coli cells. Biochimica Et Biophysica Acta. 969: 185-93. PMID 2895671 DOI: 10.1016/0167-4889(88)90074-2 |
0.514 |
|
| 1987 |
Cooke RM, Wilkinson AJ, Baron M, Pastore A, Tappin MJ, Campbell ID, Gregory H, Sheard B. The solution structure of human epidermal growth factor. Nature. 327: 339-41. PMID 3495735 DOI: 10.1038/327339A0 |
0.354 |
|
| 1987 |
Brindle KM, Campbell ID. NMR studies of kinetics in cells and tissues. Quarterly Reviews of Biophysics. 19: 159-82. PMID 3310078 DOI: 10.1017/S003358350000411X |
0.509 |
|
| 1987 |
Moody MF, Jones PT, Carver JA, Boyd J, Campbell ID. 1H nuclear magnetic resonance studies of an integral membrane protein: subunit c of the F1F0 ATP synthase. Journal of Molecular Biology. 193: 759-74. PMID 2886671 DOI: 10.1016/0022-2836(87)90357-3 |
0.384 |
|
| 1987 |
Esposito G, Carver JA, Boyd J, Campbell ID. High-resolution 1H NMR study of the solution structure of alamethicin. Biochemistry. 26: 1043-50. PMID 2436657 DOI: 10.1021/Bi00378A010 |
0.348 |
|
| 1987 |
Esposito G, Zanobi A, Giglio E, Pavel NV, Campbell ID. Intermolecular interactions in sodium deoxycholate micelles: an NMR study involving a spin-labeled cholestane The Journal of Physical Chemistry. 91: 83-89. DOI: 10.1021/J100285A021 |
0.317 |
|
| 1987 |
Campbell ID, Sheard B. Protein structure determination by NMR Trends in Biotechnology. 5: 302-306. DOI: 10.1016/0167-7799(87)90081-3 |
0.359 |
|
| 1986 |
Brindle KM, Campbell ID, Simpson RJ. A 1H-NMR study of the activity expressed by lactate dehydrogenase in the human erythrocyte. European Journal of Biochemistry. 158: 299-305. PMID 3732272 DOI: 10.1111/J.1432-1033.1986.Tb09751.X |
0.533 |
|
| 1986 |
Carver JA, Cooke RM, Esposito G, Campbell ID, Gregory H, Sheard B. A high resolution 1H NMR study of the solution structure of human epidermal growth factor. Febs Letters. 205: 77-81. PMID 3017760 DOI: 10.1016/0014-5793(86)80869-9 |
0.374 |
|
| 1986 |
Campbell ID. NMR studies of enzymes Fresenius' Zeitschrift FüR Analytische Chemie. 324: 437-441. DOI: 10.1007/Bf00474114 |
0.322 |
|
| 1985 |
Campbell ID, Dobson CM, Williams RJ. The study of conformational states of proteins by nuclear magnetic resonance. The Biochemical Journal. 231: 1-10. PMID 2998335 DOI: 10.1042/Bj2310001 |
0.491 |
|
| 1984 |
Oxley ST, Porteous R, Brindle KM, Boyd J, Campbell ID. A multinuclear NMR study of 2,3-bisphosphoglycerate metabolism in the human erythrocyte. Biochimica Et Biophysica Acta. 805: 19-24. PMID 6477971 DOI: 10.1016/0167-4889(84)90031-4 |
0.522 |
|
| 1984 |
Foxall DL, Brindle KM, Campbell ID, Simpson RJ. The inhibition of erythrocyte glyceraldehyde-3-phosphate dehydrogenase. In situ PMR studies. Biochimica Et Biophysica Acta. 804: 209-15. PMID 6372868 DOI: 10.1016/0167-4889(84)90151-4 |
0.53 |
|
| 1984 |
Paul HH, Brindle KM, Campbell ID, Smith DJ. Proton NMR measurements of hydrogen exchange at the C-3 position of 3-hydroxybutyrate in suspensions of rat liver mitochondria. Febs Letters. 163: 185-8. PMID 6315486 DOI: 10.1016/0014-5793(83)80815-1 |
0.526 |
|
| 1984 |
Brindle KM, Porteous R, Campbell ID. 1H NMR measurements of enzyme-catalyzed 15N-label exchange Journal of Magnetic Resonance (1969). 56: 543-547. DOI: 10.1016/0022-2364(84)90320-2 |
0.525 |
|
| 1984 |
Boyd J, Brindle K, Campbell I, Radda G. A comparison of one-dimensional and two-dimensional NMR methods for measuring enzyme-catalyzed exchange Journal of Magnetic Resonance (1969). 60: 149-155. DOI: 10.1016/0022-2364(84)90041-6 |
0.507 |
|
| 1983 |
Brindle KM, Campbell ID, Simpson RJ. A 1H n.m.r. study of the kinetic properties expressed by glyceraldehyde phosphate dehydrogenase in the intact human erythrocyte. The Biochemical Journal. 208: 583-92. PMID 7165719 DOI: 10.1042/Bj2080583 |
0.53 |
|
| 1983 |
Simpson RJ, Brindle KM, Campbell ID. Spin ECHO proton NMR studies of the metabolism of malate and fumarate in human erythrocytes. Dependence on free NAD levels. Biochimica Et Biophysica Acta. 721: 191-200. PMID 7138916 DOI: 10.1016/0167-4889(82)90068-4 |
0.532 |
|
| 1983 |
Simpson RJ, Brindle KM, Campbell ID. Centrifugal analysis of undiluted packed human erythrocyte lysates. Studies of the association of glyceraldehyde-phosphate dehydrogenase with the membrane fraction. Biochimica Et Biophysica Acta. 758: 187-90. PMID 6871248 DOI: 10.1016/0304-4165(83)90301-X |
0.483 |
|
| 1983 |
Brindle KM, Boyd J, Campbell ID, Porteous R, Soffe N. Observation of carbon labelling in cell metabolites using proton spin echo NMR. Biochemical and Biophysical Research Communications. 109: 864-71. PMID 6297492 DOI: 10.1016/0006-291X(82)92020-4 |
0.519 |
|
| 1983 |
SIMPSON RJ, BRINDLE KM, CAMPBELL ID. Association of aldolase with the membranes in concentrated human erythrocyte lysates Biochemical Society Transactions. 11: 281-282. DOI: 10.1042/Bst0110281 |
0.46 |
|
| 1983 |
BRINDLE KM, CAMPBELL ID, SIMPSON RJ. 1H n.m.r. studies of the kinetic properties expressed by erythrocyte enzymes in situ and in vitro Biochemical Society Transactions. 11: 280-281. DOI: 10.1042/Bst0110280 |
0.488 |
|
| 1983 |
Foxall DL, Brindle KM, Campbell I, Simpson RJ. An NMR investigation of isotope exchange involving multiply labelled intermediates Tetrahedron. 39: 3443-3448. DOI: 10.1016/S0040-4020(01)88654-3 |
0.531 |
|
| 1982 |
Simpson RJ, Brindle KM, Brown FF, Campbell ID, Foxall DL. Studies of pyruvate-water isotope exchange catalysed by erythrocytes and proteins. The Biochemical Journal. 193: 401-6. PMID 7305939 DOI: 10.1042/Bj1930401 |
0.541 |
|
| 1982 |
Brindle KM, Brown FF, Campbell ID, Foxall DL, Simpson RJ. A 1H n.m.r. study of isotope exchange catalysed by glycolytic enzymes in the human erythrocyte. The Biochemical Journal. 202: 589-602. PMID 7092833 DOI: 10.1042/Bj2020589 |
0.533 |
|
| 1982 |
Simpson RJ, Brindle KM, Brown FF, Campbell ID, Foxall DL. Studies of lactate dehydrogenase in the purified state and in intact erythrocytes. The Biochemical Journal. 202: 581-7. PMID 7092832 DOI: 10.1042/Bj2020581 |
0.5 |
|
| 1982 |
Simpson RJ, Brindle KM, Brown FF, Campbell ID, Foxall DL. A p.m.r. isotope-exchange method for studying the kinetic properties of dehydrogenases in intact cells. The Biochemical Journal. 202: 573-9. PMID 7092831 DOI: 10.1042/Bj2020573 |
0.492 |
|
| 1981 |
Brindle KM, Brown FF, Campbell ID, Foxall DL, Simpson RJ. 1H/2H isotope exchange studies in intact erythrocytes. Biochemical Society Transactions. 8: 646-7. PMID 7450272 DOI: 10.1042/Bst0080646 |
0.535 |
|
| 1981 |
Kuchel PW, Campbell ID. Nuclear Magnetic Resonance of Biological Samples C R C Critical Reviews in Analytical Chemistry. 12: 155-231. DOI: 10.1080/10408348108542746 |
0.324 |
|
| 1981 |
Brand S, Brindle K, Brown F, Campbell I, Eliot C, Foxall D, Jaroszkiewicz E, Simpson R, Styles P. STUDIES OF TRANSPORT IN SUSPENSIONS OF WHOLE CELLS USING NMR Biochemical Society Transactions. 9: 176P-176P. DOI: 10.1042/Bst009176Pa |
0.491 |
|
| 1980 |
Brown FF, Campbell ID. N.m.r. studies of red cells. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 289: 395-406. PMID 6106214 DOI: 10.1098/Rstb.1980.0056 |
0.319 |
|
| 1980 |
BRAND SC, BRINDLE KM, BROWN FF, CAMPBELL ID, ELIOT CG, FOXALL DL, JAROSZKIEWICZ E, SIMPSON RJ, STYLES P. Studies of transport in suspensions of whole cells by using nuclear magnetic resonance Biochemical Society Transactions. 8: 647-647. DOI: 10.1042/Bst0080647 |
0.492 |
|
| 1979 |
Brindle KM, Brown FF, Campbell ID, Grathwohl C, Kuchel PW. Application of spin-echo nuclear magnetic resonance to whole-cell systems. Membrane transport. The Biochemical Journal. 180: 37-44. PMID 486105 DOI: 10.1042/Bj1800037 |
0.524 |
|
| 1979 |
Campbell ID, Jones RB, Kiener PA, Waley SG. Enzyme-substrate and enzyme-inhibitor complexes of triose phosphate isomerase studied by 31P nuclear magnetic resonance. The Biochemical Journal. 179: 607-21. PMID 38777 DOI: 10.1042/Bj1790607 |
0.335 |
|
| 1979 |
Campbell ID, Dobson CM. The application of high resolution nuclear magnetic resonance to biological systems. Methods of Biochemical Analysis. 25: 1-133. PMID 34772 DOI: 10.1002/9780470110454.Ch1 |
0.413 |
|
| 1978 |
Campbell ID, Jones RB, Kiener PA, Richards E, Waley SC, Wolfenden R. The form of 2-phosphoglycollic acid bound by triosephosphate isomerase. Biochemical and Biophysical Research Communications. 83: 347-52. PMID 29623 DOI: 10.1016/0006-291X(78)90438-2 |
0.303 |
|
| 1978 |
Campbell ID, Dobson CM, Ratcliffe RG, Williams RJP. A method for the accurate measurement of 1H spin-spin coupling constants in large molecules Journal of Magnetic Resonance (1969). 31: 341-345. DOI: 10.1016/0022-2364(78)90198-1 |
0.429 |
|
| 1978 |
Campbell ID, Dobson CM, Ratcliffe RG, Williams RJP. Fourier transform NMR pulse methods for the measurement of slow-exchange rates Journal of Magnetic Resonance (1969). 29: 397-417. DOI: 10.1016/0022-2364(78)90001-X |
0.45 |
|
| 1977 |
Campbell I, Dobson C, Ratcliffe R. Fourier transform proton NMR in H2O. A method for measuring exchange and relaxation rates Journal of Magnetic Resonance (1969). 27: 455-463. DOI: 10.1016/0022-2364(77)90010-5 |
0.471 |
|
| 1976 |
Campbell ID, Dobson CM, Moore GR, Perkins SJ, Williams RJ. Temperature dependent molecular motion of a tyrosine residue of ferrocytochrome C. Febs Letters. 70: 96-100. PMID 186328 DOI: 10.1016/0014-5793(76)80734-X |
0.501 |
|
| 1976 |
Browne CA, Campbell ID, Kiener PA, Phillips DC, Waley SG, Wilson IA. Studies of the histidine residues of triose phosphate isomerase by proton magnetic resonance and x-ray crystallography. Journal of Molecular Biology. 100: 319-43. PMID 3655 DOI: 10.1016/S0022-2836(76)80066-6 |
0.359 |
|
| 1976 |
Campbell ID, Lindskog S, White AI. A study of the histidine residues of human carbonic anhydrase C using 270 MHz proton magnetic resonance. Journal of Molecular Biology. 98: 597-614. PMID 511 DOI: 10.1016/S0022-2836(75)80089-1 |
0.364 |
|
| 1975 |
Campbell ID, Dobson CM, Williams RJ, Wright PE. Pulse methods for the simplification of protein NMR spectra. Febs Letters. 57: 96-9. PMID 1175783 DOI: 10.1016/0014-5793(75)80160-8 |
0.449 |
|
| 1975 |
Campbell ID, Dobson CM, Williams RJ. Proton magnetic resonance studies of the tyrosine residues of hen lysozyme-assignment and detection of conformational mobility. Proceedings of the Royal Society of London. Series B, Biological Sciences. 189: 503-9. PMID 237281 DOI: 10.1098/Rspb.1975.0070 |
0.47 |
|
| 1975 |
Campbell ID, Dobson CM, Williams JP. Studies of exchangeable hydrogens in lysozyme by means of Fourier transform proton magnetic resonance. Proceedings of the Royal Society of London. Series B, Biological Sciences. 189: 485-502. PMID 237280 DOI: 10.1098/Rspb.1975.0069 |
0.474 |
|
| 1975 |
Campbell ID, Dobson CM, Williams RJP. Nuclear Magnetic Resonance Studies on the Structure of Lysozyme in Solution Proceedings of the Royal Society a: Mathematical, Physical and Engineering Sciences. 345: 41-59. DOI: 10.1098/Rspa.1975.0124 |
0.493 |
|
| 1975 |
Campbell ID, Dobson CM, Williams RJP, Feeney J. Assignment of the FormulaH n.m.r. Spectra of Proteins [and Discussion] Proceedings of the Royal Society a: Mathematical, Physical and Engineering Sciences. 345: 23-40. DOI: 10.1098/Rspa.1975.0123 |
0.51 |
|
| 1975 |
Campbell ID, Dobson CM. Spin echo double resonance: a novel method for detecting decoupling in Fourier transform nuclear magnetic resonance Journal of the Chemical Society, Chemical Communications. 750-751. DOI: 10.1039/C39750000750 |
0.444 |
|
| 1975 |
Campbell ID, Freeman R, Turner DL. NMR study of transient complexes in solution by means of a motional anisotropy probe Journal of Magnetic Resonance (1969). 20: 172-176. DOI: 10.1016/0022-2364(75)90164-X |
0.471 |
|
| 1974 |
Campbell ID, Dobson CM, Jeminet G, Williams RJ. Pulsed NMR methods for the observation and assignment of exchangeable hydrogens: application to bacitracin. Febs Letters. 49: 115-9. PMID 4442586 DOI: 10.1016/0014-5793(74)80645-9 |
0.429 |
|
| 1974 |
Campbell ID, Dobson CM, Williams RJP. Intramolecular nuclear Overhauser effects in proton magnetic resonance spectra of proteins Journal of the Chemical Society, Chemical Communications. 888-889. DOI: 10.1039/C39740000888 |
0.483 |
|
| 1973 |
Brown FF, Campbell ID, Henson R, Hirst CW, Richards RE. A study of the interaction of manganese ions with ATP by 31P Fourier-transform nuclear-magnetic resonance. European Journal of Biochemistry / Febs. 38: 54-8. PMID 4774125 DOI: 10.1111/J.1432-1033.1973.Tb03032.X |
0.579 |
|
| 1973 |
Campbell ID, Dobson CM, Williams RJ, Xavier AV. The determination of the structure of proteins in solution: lysozyme. Annals of the New York Academy of Sciences. 222: 163-74. PMID 4522426 DOI: 10.1111/J.1749-6632.1973.Tb15259.X |
0.446 |
|
| 1973 |
Campbell ID, Dwek RA, Price NC, Radda GK. Studies on the interaction of ligands with phosphorylase b using a spin-label probe. European Journal of Biochemistry. 30: 339-47. PMID 4351439 DOI: 10.1111/J.1432-1033.1972.Tb02103.X |
0.483 |
|
| 1973 |
Campbell ID, Freeman R. Determination of nuclear Overhauser enhancement factors from NMR spin‐lattice relaxation rates The Journal of Chemical Physics. 58: 2666-2667. DOI: 10.1063/1.1679558 |
0.511 |
|
| 1973 |
Campbell ID, Dobson CM, Williams RJP, Xavier AV. Resolution enhancement of protein PMR spectra using the difference between a broadened and a normal spectrum Journal of Magnetic Resonance (1969). 11: 172-181. DOI: 10.1016/0022-2364(73)90004-8 |
0.45 |
|
| 1973 |
Campbell I, Freeman R. Influence of cross-relaxation on NMR spin-lattice relaxation times Journal of Magnetic Resonance (1969). 11: 143-162. DOI: 10.1016/0022-2364(73)90002-4 |
0.5 |
|
| 1972 |
Bennick A, Campbell ID, Dwek RA, Price NC, Radda GK, Salmon AG. Relationship between conformationally sensitive probe binding sites on phosphorylase b. Nature: New Biology. 234: 140-3. PMID 4332179 DOI: 10.1038/Newbio234140A0 |
0.455 |
|
| 1971 |
Campbell ID, Dwek RA, Richards RE, Wiseman MN. Research notes: Nitrogen relaxation of methyl cyanide in the presence of ni(ii) ions Molecular Physics. 20: 933-935. DOI: 10.1080/00268977100100901 |
0.564 |
|
| 1971 |
Campbell ID, Nixon PE, Richards RE. The proton relaxation of ch3od in the presence of co(Ii) ions, as studied by spin-echo techniques Molecular Physics. 20: 923-931. DOI: 10.1080/00268977100100891 |
0.519 |
|
| 1971 |
Campbell ID, Carver JP, Dwek RA, Nummelin AJ, Richards RE. The proton relaxation of methyl cyanide in the presence of ni(Ii) ions, as studied by spin-echo techniques Molecular Physics. 20: 913-922. DOI: 10.1080/00268977100100881 |
0.704 |
|
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