articles in refereed journals

  1. Legan, E.R., Liu, Y., Arce, N.A., Parker, E.T., Lollar, P., Zhang, X.F.*, and Li, R.* (2023): Type 2B von Willebrand disease mutations differentially perturb autoinhibition of the A1 domain. Blood 141(10): 1221-1232. (Featured paper, commentary by McKinnon, T.A.J. “2B or not 2B: art thou autoinhibitory?”, Blood, 141(10):1102-1103.)
  2. Cui, X., Zhang, X.F., and Jagota, A. (2023): Penetration of Cell Surface Glycocalyx by Enveloped Viruses is Aided by Weak Multivalent Adhesive Interaction. The Journal of Physical Chemistry B, 127, 2, 486–494.
  3. Kim, S., Liu, Y., Ziarnik, M., Cao, Y., Zhang, X.F.*, and Im, W.* (2023): Binding of Human ACE2 and RBD of Omicron Enhanced by Unique Interaction Patterns Among SARS-CoV-2 Variants of Concern. Journal of Computational Chemistry, 44: 594-601.
  4. Arce, N.A., Liu, Y., Chen W., Zhang, X.F.*, and Li, R.* (2022): Conservation and species-specific adaptation of force-dependent activation of von Willebrand factor. Journal of Thrombosis & Haemostasis, 20: 2686 – 2696.
  5. Seth, R., McKinnon, T.A.*, and Zhang, X.F.* (2022): Contribution of the von Willebrand Factor/ADAMTS13 Imbalance to COVID-19 Coagulopathy. AJP-Heart and Circulatory Physiology, 322: H87-H93. (Cover article of the January 2022 issue)
  6. Voos, K.M., Cao, W., Arce, N.A., Legan, E.R., Wang, Y., Lollar, P., Zhang, X.F.*, and Li R.* (2022):  Desialylation of O-glycans activates von Willebrand factor by destabilizing its autoinhibitory module. Journal of Thrombosis & Haemostasis, 20: 196-207. (Cover article of the January 2022 issue)
  7. Arce, N.A., Cao, W., Brown, A.K., Legan, E.R., Wilson, M.S., Berndt, M.C., Emsley, J., Zhang, X.F.*, and Li, R.* (2021): Activation of von Willebrand factor via mechanical unfolding of its discontinuous autoinhibitory module. Nature Communications, 12:2360.
  8. Kim, S., Liu, Y., Lei, Z., Dicker, J., Cao, Y., Zhang, X.F. *, and Im, W.* (2021): Differential Interactions Between Human ACE2 and Spike RBD of SARS-CoV-2 Variants of Concern. Journal of Chemical Theory and Computation,17:7972-7979.
  9. Cao, W., Kim, S., Dong, C., Hou, D., Im, W.*, and Zhang, X.F.* (2021): Biomechanical Characterization of SARS-CoV-2 Spike RBD and Human ACE2 Protein-Protein Interaction. Biophysical Journal, 120:1211-1219.
  10. Kania, S., Oztekin, A., Cheng, X., Zhang, X.F., and Webb, E. (2021): Flow regulated nucleation protrusion theory for collapsed polymers. Physical Review E, 104:054504.
  11. Nguyen, A., Kania, S., Cheng, X., Oztekin, A., Zhang, X.F., and Webb, E. (2021): Unraveling Kinetics of Collapsed Polymers in Extensional Flow. Macromolecules, 54:8259-8269.
  12. Wang, Y., Pisapati, A., Zhang, X.F., and Cheng, X. (2021): Recent Developments in Nanomaterial‐Based Shear‐Sensitive Drug Delivery Systems. Advanced Healthcare Materials, 2002196.
  13. Zhou, Y., Cao, W., Xu, Z., Zhang, X.F., and Liu, Y. (2021): Binding Kinetics of Liposome Conjugated E-selectin and P-selectin Glycoprotein Ligand-1 Measured with Atomic Force Microscopy. Colloids and Surfaces B: Biointerfaces, 207:112002.
  14. Kania, S., Oztekin, A., Cheng, X., Zhang, X.F., and Webb, E. (2021): Predicting pathological von Willebrand factor unraveling in elongational flow. Biophysical Journal, 120(10):1903-1915.
  15. Pisapati, A., Cao, W., Anderson, K.R., Holick, K.H., Whiteaker, P., Im, W., Miwa J.M.*, and Zhang, X.F.* (2021): Biophysical characterization of lynx-nicotinic receptor interactions using atomic force microscopy. FASEB Bioadvances, 3(12):1034-1042.
  16. Cui, X., Lapinski, N., Zhang, X.F., and Jagota, A. (2021): Length of Mucin-Like Domains Enhance Cell-Ebola Virus Adhesion by Increasing Binding Probability. Biophysical Journal, 120:781-790.
  17. Wang, Y., Chen, W., Zhang, W., Lee-Sundlov, M.M., Casari, C., Berndt, M.C., Lanza, F., Bergmeier, W., Hoffmeister, K.M., Zhang, X.F., and Li, R. (2021): Desialylation of O-glycans on glycoprotein Iba drives receptor signaling and platelet clearance. Haematologica, 106(1):220-229.
  18. O’Brien, H.E., Zhang, X.F., Sanz-Hernandez, M., Chion, A., Shapiro, S., Mobayen, G., Xu, Y., De Simone, A.  Laffan, M.A., and McKinnon, T.A.J. (2021): Blocking von Willebrand factor free thiols inhibits binding to collagen under high and pathological shear stress. Journal of Thrombosis & Haemostasis, 19(2):358-369.
  19. Dong, C., Choi, Y.K., Lee, J., Zhang, X.F., Honerkamp-Smith, A., Göran, W., Lowe-Krentz, L.J., and Im, W. (2021): Structure, Dynamics, and Interactions of GPI-Anchored Human Glypican-1 with Heparan Sulfates in a Membrane. Glycobiology, 31(5):593-602. (Cover article of the May 2021 issue.)
  20. Cao, W., Cao, W., Zhang, W., Zheng, X.L.*, and Zhang, X.F.* (2020): Factor VIII binding affects the mechanical unraveling of the A2 domain of von Willebrand factor. Journal of Thrombosis & Haemostasis, 18(9):2169-2176.
  21. Wang, J., Lapinski, N., Zhang, X.F., and Jagota, A. (2020): Adhesive Contact Between Cylindrical (Ebola) and Spherical (SARS-CoV-2) Viral Particles and a Cell Membrane. Mechanics of Soft Materials, 2(1):1-9.
  22. Wang, H., Wang, L. Shang, Y., Tafti, S.Y., Cao, W., Ning, Z., Zhang, X.F., and Xu, X. (2020): Peak Force Visible Microscopy. Soft Matter, 16(36):8372-8379.
  23. Dong, C., Kem, N.R., Anderson, K.R., Zhang, X.F., Miwa, J.M., and Im, W. (2020): Dynamics and Interactions of GPI-Linked Lynx1 Protein with/without Nicotinic Acetylcholine Receptor in Membrane Bilayers. The Journal of Physical Chemistry B, 124(20):4017-4025. (Cover article of the March 2020 issue.)
  24. Pisapati, A.V., Wang, Y., Blauch, M.E., Wittenberg, N.J., Cheng, X., and Zhang, X.F.* (2020): Characterizing Single-Molecule Conformational Changes Under Shear Flow with Fluorescence. The Journal of Visualized Experiments, (155):e60784.
  25. Zhang, X.F.* and Cheng, X. (2019): Platelet mechanosensing axis. Nature Materials, 18:661-662.
  26. Sarkhosh, T., Zhang, X.F., Jellison, K.L., and Jedlicka, S.S. (2019): Biophysical binding of Cryptosporidium parvum oocysts to engineered substrates as a function of surface chemistry and oocyst age. Applied and environmental microbiology, 00816-19.
  27. Dong, C., Kania, S., Morabito, M., Zhang, X.F., Im, W., Oztekin, A., Cheng, X., and Webb, E.B. (2019): A mechano-reactive coarse-grained model of the blood-clotting agent von Willebrand factor. The Journal of Chemical Physics, 151:124905.
  28. Wang, Y., Morabito, M., Zhang, X.F.*, Oztekin, A., Webb, E.B., and Cheng, X.*, (2019): Shear-Induced Extensional Response Behaviors of Tethered von Willebrand Factor. Biophysical Journal, 116(11):2092-2102.
  29. Zhang. X.F.*, Zhang, W., Quach, M.E., Deng, W., and Li, R. (2019): Force-regulated refolding of the mechanosensory domain in platelet glycoprotein Ib-IX complex. Biophysical Journal, 116(10):1960-1969.
  30. Morabito, M., Usta, M., Zhang, X.F., Cheng, X., Oztekin, A., and Webb, E.B. (2019): Prediction of Sub-Monomer A2 Domain Dynamics of the von Willebrand Factor by Machine Learning Algorithm and Coarse-Grained Molecular Dynamics Simulation. Scientific Reports, 9:9037.
  31. Dragovich, M.A., Fortoul, N., Jagota, A., Schutt, K., Xu, Y., Sanabria, M., Moller-Tank, S., Maury, W., and Zhang. X.F.* (2019): Biomechanical characterization of TIM protein-mediated Ebola virus-host cell adhesion. Scientific Reports, 9:267.
  32. Morabito, M., Dong, C., Wei, W., Cheng, X., Zhang, X.F., Oztekin, A., and Webb, E.B. (2018): Internal Tensile Force and A2 Domain Unfolding of von Willebrand Factor Multimers in Shear Flow. Biophysical Journal, 115(10):1860-1871.
  33. Zheng, Y., Zhang, X.F., Fu, B., and Tarbell, J.M.: (2018):  The role of endothelial glycocalyx in mechanosensing and transduction. Advances in Experimental Medicine and Biology, 1097:1-27.
  34. Zhang, X.F., Sun, D., Song, J.W., Lipphardt, M., and Goligorsky, M.S. (2018): Endothelial cell dysfunction and glycocalyx – the vicious circle. Matrix Biology, 71-72:421-431.
  35. Dong, C., Lee, J., Kim, S., Lai, W., Webb, E.B., Oztekin, A., Zhang, X.F., and Im, W. (2018): Long-ranged protein-glycan interactions stabilize von Willebrand Factor A2 domain from mechanical unfolding. Scientific Reports, 8(1):16017.
  36. Wang, S., Wu, C., Zhang, Y., Zhong, Q., Sun, H., Cao, W., Ge, G.X., Li, G.H., Zhang, X.F.*, and Chen, J.F.* (2018): The Structural basis of chemokine-mediated switch in integrin α4β7 ligand specificity. The Journal of Cell Biology, 217(8): 2799-2812.
  37. Wei, W., Dong, C., Morabito, M., Cheng, X., Zhang, X.F., Oztekin, A., and Webb, E.B. (2018): Characteristics of von Willebrand Factor adhesion on collagen surface under flow. Biophysical Journal, 114(8):1816-1829.
  38. Quach, M.E., Dragovich, M.A., Chen, W., Syed, A.K., Cao, W., Liang, X., Deng, W., De Meyer, S., Zhu, G., Ni, He., Ware, J., Deckmyn, H., Zhang, X.F., and Li, R. (2018): Fc-independent immune thrombocytopenia via mechanomolecular signaling in platelets. Blood, 131(7):787-796.
  39. Song, J.W., Zullo, J.A., Lipphardt, M., Dragovich, M., Zhang X.F., Fu, B., and Goligorsky, M. (2018): Endothelial Glycocalyx – the battleground for complications of sepsis and kidney injury. Nephrology Dialysis Transplantation, 33(2):203-211.
  40. Bondu, V., Wu, C., Cao, W., Simons, P., Gillette, J., Zhu, J., Erb, L., Zhang, X.F.*, and Buranda, T.* (2017): Low affinity binding in cis to P2Y2R mediates force-dependent integrin activation during hantavirus infection. Molecular Biology of the Cell, 28(21):2887-2903.
  41. Guo, X.D., Yan, C., Shi, X., Huang, M., Huang, W., Wang, Y., Pan, W., Cai, M., Li, L., Wu, W., Bai, Y., Zhang, C., Liu, Z., Wang, X., Zhang, X.F., Tang, C., Wang, H., Liu, W., Ouyang, B., Wong, C.C., Chou, J.J., Cao, Y., and Xu, C. (2017): Lipid-dependent conformational dynamics underlie the functional versatility of T-cell receptor. Cell Research, 27(4):505-525.
  42. Song, J.W., Zullo, J.A., Liveris, D., Dragovich, M., Zhang X.F., and Goligorsky, M.S. (2017): Therapeutic Restoration of Endothelial Glycocalyx in Sepsis. The Journal of pharmacology and experimental therapeutics, 361(1):115-121.
  43. Dragovich, M.A., Genemaras, K., Dailey H.L., Jedlicka S., and Zhang, X.F.* (2017): Dual regulation of L-selectin-mediated leukocyte-endothelial adhesion by endothelial surface glycocalyx. Cellular and Molecular Bioengineering, 10(1):102-113.
  44. Deng, W., Xu, Y., Chen, W., Paul, D.S., Syed, A.K., Dragovich, M.A., Liang, X., Zakas, P., Berndt, M.C., DiPaola, J., Ware, J., Lanza, F., Doering, C.B., Bergmeier, W., Zhang, X., and Li, R. (2016): Platelet clearance via shear-induced unfolding of the mechanosensory domain in glycoprotein Ib-IX complex. Nature Communications, 7:12863.
  45. Dragovich, M.A., Chester, D., Fu, B., Goligorsky, M.S., and Zhang. X.F.* (2016): Mechanotransduction of endothelial glycocalyx mediates nitric oxide production by activation of TRP channels. AJP – Cell Physiology, 311(6):C846-853.
  46. LeBlon, C.E, Fodor, C. R., Zhang, T., Zhang, X., and Jedlicka, S.S. (2015): Correlation between in vitro expansion-related cell stiffening and differentiation potential of human mesenchymal stem cells. Differentiation, 90(1):1-15.
  47. Zhang, W., Deng, W., Zhou, L., Xu, Y., Yang, W., Liang, X., Wang, Y., Kulman, J.D., Zhang, X.F.*, and Li, R.* (2015): Identification of a juxtamembrane mechano-sensitive domain in the platelet mechanosensor glycoprotein Ib-IX complex. Blood, 125:562-569. (Featured paper, comments see Ruggeri, E.M. “Platelet GPIb: sensing force and responding”, Blood, 125:423-424.)
  48. Fu, X., Xu, Y., Wu, C., Moy, V.T., and Zhang, X.F.* (2015): Anchorage-dependent binding of integrin I-domain to adhesion ligands. Journal of Molecular Recognition, 28:385-92. 
  49. Ouyang, Y., Wei, W., Cheng X., Zhang, X.F., Webb, E.B. III, and Oztekin, A. (2015): Flow-induced conformational change of von Willebrand Factor multimer. Journal of Non-Newtonian Fluid Mechanics, 217:58-67.
  50. Zhang, W., Deng, W., Wang, Y., Zhou, L., Yang, W., Linag, X., Cho, S., Kulman, J.D., Zhang, X.F., and Li, R. (2014): Identification of the mechanosensory domain in the platelet mechanosensor GPIb-IX complex. Journal of Thrombosis and Haemostasis, 12:74-75.
  51. Wang, Y.Z., Chen, L., Wang, H.Y., Zhang, X., Fu, J., Xiong, X.M., and Zhang, J.X. (2014): Development of “fragility” in relaxor ferroelectrics. Journal of Applied Physics, 115:054106.
  52. Cao, Y., Hoeppner, L.H., Bach, S., Guangqi, E., Guo, Y., Wang, E., Wu, J., Cowley, M.J., Chang, D.K., Waddell, N., Grimmond, S.M., Biankin, A.V., Daly, R.J., Zhang, X.F., and Mukhopadhyay, D. (2013): Neuropilin-2 promotes extravasation and metastasis by interacting with endothelial a5 integrin. Cancer Research, 73(14):4579-4590.
  53. Wang, Y.Z., Zhang, X.F.*, and Zhang, J.X. (2013): A “configurational entropy-loss” law for non-Arrhenius relaxation in disordered systems. Journal of Applied Physics, 113:194105.
  54. Wang, Y.Z., Zhang, X.F., and Zhang, J.X. (2013): New insight into the kinetic behavior of the structural formation process in agar gelation. Rheologica Acta, 52:39-48.
  55. Przybylowski, C., Quinn, T., Callahan, A., Kaplan, M., Golding, A., Alesi, C., Ammar, M., LeBlon, C.E, Guo, Y., Zhang, X., and Jedlicka, S.S. (2012): MC3T3 Preosteoblast Differentiation on Bone Morphogenetic Protein-2 Peptide Ormosils. The Journal of Materials Chemistry, 22:10672-10683.
  56. Hu, L., Fan, Z., Du, H., Ni, R., Zhang, S., Yin, K., Ye, J., Zhang, Y., Wei, X., Zhang, X., Gross, P. L., Kunapuli, S. P., and Ding, Z. (2011): BF061, a novel antiplatelet and antithrombotic agent targeting P2Y12 receptor and phosphodiesterase. Thrombosis and Haemostasis, 106: 1203-14.
  57. Zhang, S., Hu, L., Yu, X., Guo, Y., Zhang, Y., Niu, H., Jin, J., Bhavaraju, K., Du, H., Liu, J., Zhang, X., Kunapuli, S. P., and Ding, Z. (2010): BF0801, a novel adenine derivative, inhibits platelet activation via PDE inhibition and P2Y12 antagonism. Thrombosis and Haemostasis, 104:845-57.
  58. Du, D., Xu, F., Yu, L., Bao, H., Zhang, C., Lu, X., Yuan, H., Zhu, X., Zhang, X., and Chen, Z. (2010): The tight junction protein, occludin, regulates the directional migration of epithelial cells. Developmental Cell, 18:52-63.
  59. Kim, J., Zhang, C.-Z., Zhang, X., and Springer, T.A. (2010): A mechanically stabilized receptor-ligand flex-bond important in the vasculature. Nature, 466:992-5.
  60. Zhang, X., Halvorsen, K., Zhang, C.Z., Wong, W.P., and Springer, T.A. (2009): Mechanoenzymatic cleavage of the ultra-large vascular protein, von Willebrand Factor. Science, 324:1330-1334. (Featured paper, comments see Gebhardt, J. C. and Rief, M. “Force Signaling in Biology”, Science, 324:1278-1280.)
  61. Zhang, Q., Zhou, Y., Zhang, C.Z., Zhang, X., Lu, C., and Springer, T.A. (2009): Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor. PNAS, 106(23):9226-31.

    Prior to 2009
  62. Zhang, X.*, Wojcikiewicz, E., and Moy, V.T. (2006): Dynamic adhesion of T-lymphocytes to endothelial cells revealed by atomic force microscopy. Experimental Biology and Medicine, 231:1306-12.
  63. Wojcikiewicz, E., Abdulreda, M.H., Zhang, X., and Moy, V.T. (2006): Force spectroscopy of LFA-1 and its ligands, ICAM-1 and ICAM-2. Biomacromolecules, 7:3188-3195.
  64. Zhang, X., Craig, S.E., Kirby, H., Humphries, M.J., and Moy, V.T. (2004): Molecule basis for the dynamic strength of the integrin a4β1/VCAM-1 interaction. Biophysical Journal, 87:3470-3478.
  65. Zhang, X., Chen, A., DeLeon, D., Li, H., Noiri, E., Moy, V.T., and Goligorsky, M.S. (2004): Atomic force microscopy measurement of leukocyte-endothelial interaction. American Journal of Physiology-Heart and Circulatory Physiology, 286:H359-367.
  66. Zhang, X., Bogorin D.F., and Moy, V.T. (2004): Molecular basis of the dynamic strength of the sialyl Lewis x – selectin Interaction. ChemPhysChem, 4:100-107.
  67. Wojcikiewicz, E., Zhang, X., and Moy, V.T. (2004). Force and compliance measurements on living cells using atomic force microscopy. Biological Procedures Online, 6:1-9.
  68. Zhang, X. and Moy, V.T. (2004): Intermolecular forces of leukocyte adhesion molecules. Microscopy and Microanalysis, 10:1422-1423.
  69. Zhang, X.* and Moy, V.T. (2003): Cooperative adhesion of ligand-receptor bonds. Biophysical Chemistry, 104:271-278.
  70. Wojcikiewicz, E., Zhang, X., and Moy, V.T. (2003): Contributions of molecular binding events and cellular compliance to the modulation of leukocyte adhesion. Journal of Cell Science, 116:2531-2539.
  71. Zhang, X., Wojcikiewicz, E., and Moy, V.T. (2002): Force spectroscopy of the Leukocyte Function-Associated Antigen-1 (LFA-1)/Intercellular Adhesion Molecule-1 (ICAM-1) interaction. Biophysical Journal, 83:2270-2279.
  72. Micic, M., Zheng, Y., Moy, V.T., Zhang, X., Andreanopolous, F, Hua, F.Q., and Leblanc, R.M. (2002): Comparative studies of surface topography and mechanical properties of a novel photoswitchable, biocompatible PEG-NC based hydrogel. Colloids and Surfaces B: Biointerface, 27:147-158.
  73. Zhang, X., Wojcikiewicz, E., and Moy, V.T. (2002). Probing single ICAM-1/LFA-1 interactions under external forces. ScientificWorldJournal, 2:41-42.
  74. Lui, S.L., Chan, L.Y.Y., Zhang, X., Zhu, W., Chan, T.M., Fung, P.C.W., and Lai, K.N. (2001): Effect of mycophenolate mofetil on nitric oxide production and inducible nitric oxide synthase gene expression during renal ischaemia-reperfusion injury. Nephrology, Dialysis, Transplantation, 16:1577-1582.
  75. Zhang, X., Li, H., Jin, H., Ebin, Z., Brodsky, S., and Goligorsky, M.S. (2000): Effects of homocysteine on endothelial nitric oxide production. American Journal of Physiology-Renal Physiology, 279:F671-678.
  76. Ge, Z.D., Zhang, X., Fung, P.C.W., and He, G.W. (2000): Endothelium-dependent hyperpolarization under relaxation resistant to N(G)-nitro-L-arginine (L-NNA) and indomethacin in coronary micro-arteries. Cardiovascular Research, 46:547-556.
  77. Kuang, Z.Q., Zhang, J.X., Zhang, X., Liang, K.F., and Fung, P.C.W. (2000): Kinetic parameters in the thermoelastic martensitic transformation of Co. Solid State Communications, 14:231-235.
  78. Kuang, Z.Q., Zhang, J.X., Zhang, X., Liang, K.F., and Fung, P.C.W. (2000): Scaling behaviours in the thermoelastic martensitic transformation of Co. Scripta Materialia, 42:795-799.
  79. Chan, K.L., Zhang, X., Fung, P.C.W, Guo, W.H., and Tam, P.K.H. (1999): Role of nitric oxide in intestinal ischaemia-reperfusion injury studied using electron paramagnetic resonance. British Journal of Surgery, 86:1427-1432.80. 
  80. Lui, S.L., Zhang, X., Zhu, W., Lo, C.Y., Chan, T.M., Fung, C.W., and Lai, K.N. (1999): Demonstration of nitric oxide generation during renal ischemia-reperfusion injury. Transplantation Proceedings, 3:1020-1021.

Asterisk* denotes the corresponding author.

Names underlined are students/trainees of the Frank Zhang group.

Representative journal covers:


  1. Rico, F., Zhang, X., and Moy, V.T. (2011): Probing cellular adhesion at the single molecular level. Chapter 11 (p. 225-262) in Life at the Nanoscale: Atomic Force Microscopy of Live Cells (Yves Dufrêne, Ed.), Pan Stanford Publishing Ltd.
  2. Zhang, X.*, Rico F., Xu, A.J., and Moy, V.T. (2009): Atomic force microscopy of protein-protein interactions. Chapter 19 in Handbook of Single-Molecule Biophysics (Peter Hinterdorfer and Antoine van Oijen, Ed. ISBN: 978-0-387-76496-2), Springer Publishing (
  3. Zhang, X. and Moy, V.T. (2006): Intermolecular forces of leukocyte adhesion molecules. Chapter 9 (p. 159-168) in Force Microscopy: Application in Biology and Medicine (Bhanu P. Jena and Johann Karl H. Horber, Ed.), John Wiley & Sons Inc. Press.
  4. Zhang, X., Wojcikiewicz, E., Abdulreda, M., Chen, A., and Moy, V.T. (2005): Probing ligand-receptor interactions with atomic force microscopy. Chapter 21 (p. 399-413) in Protein-Protein Interactions: A Molecular Cloning Manual, 2nd Edition (Erica A. Golemis and Peter D. Adams, Ed.), Cold Spring Harbor Laboratory Press.
  5. Zhang, X., Chen, A., Wojcikiewicz, E., and Moy, V.T. (2002): Probing ligand-receptor interactions with atomic force microscopy. Chapter 13 (p. 241-254) in Protein-Protein Interactions: A Molecular Cloning Manual (Erica A. Golemis, Ed.), Cold Spring Harbor Laboratory Press. 

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