Developments in single photon emission computed tomography and PET-based HER2 molecular imaging for breast cancer

References

• Ross JS, Slodkowska EA, Symmans WF, Pusztai L, Ravdin PM, Hortobagyi GN. The HER-2 receptor and breast cancer: ten years of targeted anti-HER-2 therapy and personalized medicine. Oncologist 14(4), 320–368 (2009).
   PubMed Web of Science ®Google Scholar
• Schechter AL, Stern DF, Vaidyanathan L et al. The neu oncogene: an erb-B-related gene encoding a 185,000-Mr tumour antigen. Nature 312(5994), 513–516 (1984).
   PubMed Web of Science ®Google Scholar
• Akiyama T, Sudo C, Ogawara H, Toyoshima K, Yamamoto T. The product of the human c-erbB-2 gene: a 185-kilodalton glycoprotein with tyrosine kinase activity. Science 232(4758), 1644–1646 (1986).
   PubMed Web of Science ®Google Scholar
• King CR, Kraus MH, Aaronson SA. Amplification of a novel v-erbB-related gene in a human mammary carcinoma. Science 229(4717), 974–976 (1985).
   PubMed Web of Science ®Google Scholar
• Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, McGuire WL. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 235(4785), 177–182 (1987).
   PubMed Web of Science ®Google Scholar
• Owens MA, Horten BC, Da Silva MM. HER2 amplification ratios by fluorescence in situ hybridization and correlation with immunohistochemistry in a cohort of 6556 breast cancer tissues. Clin. Breast Cancer 5(1), 63–69 (2004).
   PubMedGoogle Scholar
• Citri A, Yarden Y. EGF-ERBB signalling: towards the systems level. Nat. Rev. Mol. Cell Biol. 7(7), 505–516 (2006).
   PubMed Web of Science ®Google Scholar
• Moasser MM. The oncogene HER2: its signaling and transforming functions and its role in human cancer pathogenesis. Oncogene 26(45), 6469–6487 (2007).
   PubMed Web of Science ®Google Scholar
• Nahta R, Yuan LX, Zhang B, Kobayashi R, Esteva FJ. Insulin-like growth factor-I receptor/human epidermal growth factor receptor 2 heterodimerization contributes to trastuzumab resistance of breast cancer cells. Cancer Res. 65(23), 11118–11128 (2005).
   PubMed Web of Science ®Google Scholar
• Shou J, Massarweh S, Osborne CK et al. Mechanisms of tamoxifen resistance: increased estrogen receptor-HER2/neu cross-talk in ER/HER2-positive breast cancer. J. Natl Cancer Inst. 96(12), 926–935 (2004).
   PubMed Web of Science ®Google Scholar
• Molina MA, Sáez R, Ramsey EE et al. NH(2)-terminal truncated HER-2 protein but not full-length receptor is associated with nodal metastasis in human breast cancer. Clin. Cancer Res. 8(2), 347–353 (2002).
   PubMed Web of Science ®Google Scholar
• Scaltriti M, Rojo F, Ocaña A et al. Expression of p95HER2, a truncated form of the HER2 receptor, and response to anti-HER2 therapies in breast cancer. J. Natl Cancer Inst. 99(8), 628–638 (2007).
   PubMed Web of Science ®Google Scholar
• Rosenthal SI, Depowski PL, Sheehan CE, Ross JS. Comparison of HER-2/neu oncogene amplification detected by fluorescence in situ hybridization in lobular and ductal breast cancer. Appl. Immunohistochem. Mol. Morphol. 10(1), 40–46 (2002).
   PubMedGoogle Scholar
• Fu W, Lobocki CA, Silberberg BK, Chelladurai M, Young SC. Molecular markers in Paget disease of the breast. J. Surg. Oncol. 77(3), 171–178 (2001).
   PubMed Web of Science ®Google Scholar
• Quénel N, Wafflart J, Bonichon F et al. The prognostic value of c-erbB2 in primary breast carcinomas: a study on 942 cases. Breast Cancer Res. Treat. 35(3), 283–291 (1995).
   PubMed Web of Science ®Google Scholar
• Niikura N, Liu J, Hayashi N et al. Loss of human epidermal growth factor receptor 2 (HER2) expression in metastatic sites of HER2-overexpressing primary breast tumors. J. Clin. Oncol. 30(6), 593–599 (2012).
   PubMed Web of Science ®Google Scholar
• Amir E, Clemons M, Purdie CA et al. Tissue confirmation of disease recurrence in breast cancer patients: pooled analysis of multi-centre, multi-disciplinary prospective studies. Cancer Treat. Rev. 38(6), 708–714 (2012).
   PubMed Web of Science ®Google Scholar
• Lin NU, Winer EP. Brain metastases: the HER2 paradigm. Clin. Cancer Res. 13(6), 1648–1655 (2007).
   PubMed Web of Science ®Google Scholar
• Ross JS. Breast cancer biomarkers and HER2 testing after 10 years of anti-HER2 therapy. Drug News Perspect. 22(2), 93–106 (2009).
   PubMed Web of Science ®Google Scholar
• Pegram MD, Pauletti G, Slamon DJ. HER-2/neu as a predictive marker of response to breast cancer therapy. Breast Cancer Res. Treat. 52(1–3), 65–77 (1998).
   PubMed Web of Science ®Google Scholar
• Moreno A, Lloveras B, Figueras A et al. Ductal carcinoma in situ of the breast: correlation between histologic classifications and biologic markers. Mod. Pathol. 10(11), 1088–1092 (1997).
   PubMedGoogle Scholar
• Wolff AC, Hammond ME, Schwartz JN et al.; American Society of Clinical Oncology/College of American Pathologists. Guideline recommendations for human epidermal growth factor receptor 2 testing in breast cancer. Arch. Pathol. Lab. Med. 131(1), 18–43 (2007).
   PubMed Web of Science ®Google Scholar
• Press MF, Hung G, Godolphin W, Slamon DJ. Sensitivity of HER-2/neu antibodies in archival tissue samples: potential source of error in immunohistochemical studies of oncogene expression. Cancer Res. 54(10), 2771–2777 (1994).
   PubMed Web of Science ®Google Scholar
• Vani K, Sompuram SR, Fitzgibbons P, Bogen SA. National HER2 proficiency test results using standardized quantitative controls: characterization of laboratory failures. Arch. Pathol. Lab. Med. 132(2), 211–216 (2008).
   PubMed Web of Science ®Google Scholar
• Jacobs TW, Gown AM, Yaziji H, Barnes MJ, Schnitt SJ. Specificity of HercepTest in determining HER-2/neu status of breast cancers using the United States Food and Drug Administration-approved scoring system. J. Clin. Oncol. 17(7), 1983–1987 (1999).
   PubMed Web of Science ®Google Scholar
• Powell WC, Hicks DG, Prescott N et al. A new rabbit monoclonal antibody (4B5) for the immunohistochemical (IHC) determination of the HER2 status in breast cancer: comparison with CB11, fluorescence in situ hybridization (FISH), and interlaboratory reproducibility. Appl. Immunohistochem. Mol. Morphol. 15(1), 94–102 (2007).
   PubMedGoogle Scholar
• Shah S, Chen B. Testing for HER2 in breast cancer: a continuing evolution. Patholog. Res. Int. 2011, 903202 (2011).
   Google Scholar
• Wolff AC, Hammond ME, Schwartz JN et al.; American Society of Clinical Oncology; College of American Pathologists. American Society of Clinical Oncology/College of American Pathologists guideline recommendations for human epidermal growth factor receptor 2 testing in breast cancer. J. Clin. Oncol. 25(1), 118–145 (2007).
   PubMed Web of Science ®Google Scholar
• Shah SS, Wang Y, Tull J, Zhang S. Effect of high copy number of HER2 associated with polysomy 17 on HER2 protein expression in invasive breast carcinoma. Diagn. Mol. Pathol. 18(1), 30–33 (2009).
   PubMedGoogle Scholar
• Yeh IT, Martin MA, Robetorye RS et al. Clinical validation of an array CGH test for HER2 status in breast cancer reveals that polysomy 17 is a rare event. Mod. Pathol. 22(9), 1169–1175 (2009).
   PubMedGoogle Scholar
• Tse CH, Hwang HC, Goldstein LC et al. Determining true HER2 gene status in breast cancers with polysomy by using alternative chromosome 17 reference genes: implications for anti-HER2 targeted therapy. J. Clin. Oncol. 29(31), 4168–4174 (2011).
   PubMed Web of Science ®Google Scholar
• Lal P, Salazar PA, Hudis CA, Ladanyi M, Chen B. HER-2 testing in breast cancer using immunohistochemical analysis and fluorescence in situ hybridization: a single-institution experience of 2,279 cases and comparison of dual-color and single-color scoring. Am. J. Clin. Pathol. 121(5), 631–636 (2004).
   PubMed Web of Science ®Google Scholar
• Yaziji H, Goldstein LC, Barry TS et al. HER-2 testing in breast cancer using parallel tissue-based methods. JAMA 291(16), 1972–1977 (2004).
   PubMed Web of Science ®Google Scholar
• Slamon DJ, Leyland-Jones B, Shak S et al. Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2. N. Engl. J. Med. 344(11), 783–792 (2001).
   PubMed Web of Science ®Google Scholar
• Marty M, Cognetti F, Maraninchi D et al. Randomized Phase II trial of the efficacy and safety of trastuzumab combined with docetaxel in patients with human epidermal growth factor receptor 2-positive metastatic breast cancer administered as first-line treatment: the M77001 study group. J. Clin. Oncol. 23(19), 4265–4274 (2005).
   PubMed Web of Science ®Google Scholar
• Slamon D, Eiermann W, Robert N et al.; Breast Cancer International Research Group. Adjuvant trastuzumab in HER2-positive breast cancer. N. Engl. J. Med. 365(14), 1273–1283 (2011).
   PubMed Web of Science ®Google Scholar
• Piccart-Gebhart MJ, Procter M, Leyland-Jones B et al.; Herceptin Adjuvant (HERA) Trial Study Team. Trastuzumab after adjuvant chemotherapy in HER2-positive breast cancer. N. Engl. J. Med. 353(16), 1659–1672 (2005).
   PubMed Web of Science ®Google Scholar
• Romond EH, Perez EA, Bryant J et al. Trastuzumab plus adjuvant chemotherapy for operable HER2-positive breast cancer. N. Engl. J. Med. 353(16), 1673–1684 (2005).
   PubMed Web of Science ®Google Scholar
• Joensuu H, Kellokumpu-Lehtinen PL, Bono P et al.; FinHer Study Investigators. Adjuvant docetaxel or vinorelbine with or without trastuzumab for breast cancer. N. Engl. J. Med. 354(8), 809–820 (2006).
   PubMed Web of Science ®Google Scholar
• Cameron D, Casey M, Press M et al. A Phase III randomized comparison of lapatinib plus capecitabine versus capecitabine alone in women with advanced breast cancer that has progressed on trastuzumab: updated efficacy and biomarker analyses. Breast Cancer Res. Treat. 112(3), 533–543 (2008).
   PubMed Web of Science ®Google Scholar
• Baselga J, Cortés J, Kim SB et al.; CLEOPATRA Study Group. Pertuzumab plus trastuzumab plus docetaxel for metastatic breast cancer. N. Engl. J. Med. 366(2), 109–119 (2012).
   PubMed Web of Science ®Google Scholar
• Mankoff DA. A definition of molecular imaging. J. Nuclear Med. 48(6), 18N–21N (2007).
   PubMed Web of Science ®Google Scholar
• Port ER, Yeung H, Gonen M et al. 18F-2-fluoro-2-deoxy-d-glucose positron emission tomography scanning affects surgical management in selected patients with high-risk, operable breast carcinoma. Ann. Surg. Oncol. 13(5), 677–684 (2006).
   PubMed Web of Science ®Google Scholar
• Osborne JR, Port E, Gonen M et al. 18F-FDG PET of locally invasive breast cancer and association of estrogen receptor status with standardized uptake value: microarray and immunohistochemical analysis. J. Nucl. Med. 51(4), 543–550 (2010).
   PubMedGoogle Scholar
• Lub-de Hooge MN, Kosterink JG, Perik PJ et al. Preclinical characterisation of 111In-DTPA-trastuzumab. Br. J. Pharmacol. 143(1), 99–106 (2004).
   PubMed Web of Science ®Google Scholar
• McLarty K, Cornelissen B, Scollard DA, Done SJ, Chun K, Reilly RM. Associations between the uptake of 111In-DTPA-trastuzumab, HER2 density and response to trastuzumab (Herceptin) in athymic mice bearing subcutaneous human tumour xenografts. Eur. J. Nucl. Med. Mol. Imaging 36(1), 81–93 (2009).
   PubMed Web of Science ®Google Scholar
• Perik PJ, Lub-De Hooge MN, Gietema JA et al. Indium-111-labeled trastuzumab scintigraphy in patients with human epidermal growth factor receptor 2-positive metastatic breast cancer. J. Clin. Oncol. 24(15), 2276–2282 (2006).
   PubMed Web of Science ®Google Scholar
• McLarty K, Cornelissen B, Cai Z et al. Micro-SPECT/CT with 111In-DTPA-pertuzumab sensitively detects trastuzumab-mediated HER2 downregulation and tumor response in athymic mice bearing MDA-MB-361 human breast cancer xenografts. J. Nucl. Med. 50(8), 1340–1348 (2009).
   PubMedGoogle Scholar
• Dijkers EC, Kosterink JG, Rademaker AP et al. Development and characterization of clinical-grade 89Zr-trastuzumab for HER2/neu immunoPET imaging. J. Nucl. Med. 50(6), 974–981 (2009).
   PubMed Web of Science ®Google Scholar
• Oude Munnink TH, Korte MA, Nagengast WB et al. (89)Zr-trastuzumab PET visualises HER2 downregulation by the HSP90 inhibitor NVP-AUY922 in a human tumour xenograft. Eur. J. Cancer 46(3), 678–684 (2010).
   PubMed Web of Science ®Google Scholar
• Dijkers EC, Oude Munnink TH, Kosterink JG et al. Biodistribution of 89Zr-trastuzumab and PET imaging of HER2-positive lesions in patients with metastatic breast cancer. Clin. Pharmacol. Ther. 87(5), 586–592 (2010).
   PubMed Web of Science ®Google Scholar
• Smith-Jones PM, Solit DB, Akhurst T, Afroze F, Rosen N, Larson SM. Imaging the pharmacodynamics of HER2 degradation in response to Hsp90 inhibitors. Nat. Biotechnol. 22(6), 701–706 (2004).
   PubMed Web of Science ®Google Scholar
• Smith-Jones PM, Solit D, Afroze F, Rosen N, Larson SM. Early tumor response to Hsp90 therapy using HER2 PET: comparison with 18F-FDG PET. J. Nucl. Med. 47(5), 793–796 (2006).
   PubMed Web of Science ®Google Scholar
• Akhurst T, Morris PG, Modi S et al. Positron emission tomography (PET) with radiolabeled F(ab´)2-trastuzumab fragments in patients (pts) with HER2-positive metastatic breast cancer (MBC): initial feasibility results. Presented at: 2008 Breast Cancer Symposium. Washington, DC, USA, 5–7 September 2008.
   Google Scholar
• Dennis MS, Jin H, Dugger D et al. Imaging tumors with an albumin-binding Fab, a novel tumor-targeting agent. Cancer Res. 67(1), 254–261 (2007).
   PubMed Web of Science ®Google Scholar
• Nilsson B, Moks T, Jansson B et al. A synthetic IgG-binding domain based on staphylococcal protein A. Protein Eng. 1(2), 107–113 (1987).
   PubMedGoogle Scholar
• Orlova A, Magnusson M, Eriksson TL et al. Tumor imaging using a picomolar affinity HER2 binding affibody molecule. Cancer Res. 66(8), 4339–4348 (2006).
   PubMed Web of Science ®Google Scholar
• Nord K, Gunneriusson E, Ringdahl J, Ståhl S, Uhlén M, Nygren PA. Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain. Nat. Biotechnol. 15(8), 772–777 (1997).
   PubMed Web of Science ®Google Scholar
• Orlova A, Tolmachev V, Pehrson R et al. Synthetic affibody molecules: a novel class of affinity ligands for molecular imaging of HER2-expressing malignant tumors. Cancer Res. 67(5), 2178–2186 (2007).
   PubMed Web of Science ®Google Scholar
• Orlova A, Wållberg H, Stone-Elander S, Tolmachev V. On the selection of a tracer for PET imaging of HER2-expressing tumors: direct comparison of a 124I-labeled affibody molecule and trastuzumab in a murine xenograft model. J. Nucl. Med. 50(3), 417–425 (2009).
   PubMed Web of Science ®Google Scholar
• Tolmachev V, Velikyan I, Sandström M, Orlova A. A HER2-binding affibody molecule labelled with 68Ga for PET imaging: direct in vivo comparison with the 111In-labelled analogue. Eur. J. Nucl. Med. Mol. Imaging 37(7), 1356–1367 (2010).
   PubMedGoogle Scholar
• Cheng Z, De Jesus OP, Kramer DJ et al. 64Cu-labeled affibody molecules for imaging of HER2 expressing tumors. Mol. Imaging Biol. 12(3), 316–324 (2010).
   PubMed Web of Science ®Google Scholar
• Ren G, Zhang R, Liu Z et al. A 2-helix small protein labeled with 68Ga for PET imaging of HER2 expression. J. Nucl. Med. 50(9), 1492–1499 (2009).
   PubMedGoogle Scholar
• Ren G, Webster JM, Liu Z et al. In vivo targeting of HER2-positive tumor using 2-helix affibody molecules. Amino Acids 43(1), 405–413 (2012).
   PubMedGoogle Scholar
• Kiesewetter DO, Krämer-Marek G, Ma Y, Capala J. Radiolabeling of HER2 specific Affibody® molecule with F-18. J. Fluor. Chem. 129(9), 799–805 (2008).
   PubMedGoogle Scholar
• Kramer-Marek G, Kiesewetter DO, Martiniova L, Jagoda E, Lee SB, Capala J. [18F]FBEM-ZHER2:342 – affibody molecule – a new molecular tracer for in vivo monitoring of HER2 expression by positron emission tomography. Eur. J. Nucl. Med. Mol. Imaging 35(5), 1008–1018 (2008).
   PubMed Web of Science ®Google Scholar
• Kramer-Marek G, Kiesewetter DO, Capala J. Changes in HER2 expression in breast cancer xenografts after therapy can be quantified using PET and (18)F-labeled affibody molecules. J. Nucl. Med. 50(7), 1131–1139 (2009).
   PubMedGoogle Scholar
• Ahlgren S, Wållberg H, Tran TA et al. Targeting of HER2-expressing tumors with a site-specifically 99mTc-labeled recombinant affibody molecule, ZHER2:2395, with C-terminally engineered cysteine. J. Nucl. Med. 50(5), 781–789 (2009).
   PubMed Web of Science ®Google Scholar
• Baum RP, Prasad V, Müller D et al. Molecular imaging of HER2-expressing malignant tumors in breast cancer patients using synthetic 111In- or 68Ga-labeled affibody molecules. J. Nucl. Med. 51(6), 892–897 (2010).
   PubMed Web of Science ®Google Scholar
• Tran T, Engfeldt T, Orlova A et al. (99m)Tc-maEEE-Z HER2:342, an affibody molecule-based tracer for the detection of HER2 expression in malignant tumors. Bioconjug. Chem. 18(6), 1956–1964 (2007).
   PubMed Web of Science ®Google Scholar
• Hofstrom C, Orlova A, Altai M, Wangsell F, Graslund T, Tolmachev V. Use of a HEHEHE purification tag instead of a hexahistidine tag improves biodistribution of affibody molecules site-specifically labeled with (99m)Tc, (111)In, and (125)I. J. Med. Chem. 54(11), 3817–3826 (2011).
   PubMed Web of Science ®Google Scholar
• Robinson MK, Shaller C, Garmestani K et al. Effective treatment of established human breast tumor xenografts in immunodeficient mice with a single dose of the alpha-emitting radioisotope astatine-211 conjugated to anti-HER2/neu diabodies. Clin. Cancer Res. 14(3), 875–882 (2008).
   PubMed Web of Science ®Google Scholar
• Miller J, Doss M, McQuillen R et al. Impact of expression system on the function of the C6.5 diabody PET radiotracer. Tumour Biol. 33(3), 617–627 (2012).
   PubMedGoogle Scholar
• Robinson MK, Doss M, Shaller C et al. Quantitative immuno-positron emission tomography imaging of HER2-positive tumor xenografts with an iodine-124 labeled anti-HER2 diabody. Cancer Res. 65(4), 1471–1478 (2005).
   PubMed Web of Science ®Google Scholar
• Reddy S, Shaller CC, Doss M et al. Evaluation of the anti-HER2 C6.5 diabody as a PET radiotracer to monitor HER2 status and predict response to trastuzumab treatment. Clin. Cancer Res. 17(6), 1509–1520 (2011).
   PubMedGoogle Scholar
• Bork P. Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally? Proteins 17(4), 363–374 (1993).
   PubMed Web of Science ®Google Scholar
• Lander ES, Linton LM, Birren B et al.; International Human Genome Sequencing Consortium. Initial sequencing and analysis of the human genome. Nature 409(6822), 860–921 (2001).
   PubMed Web of Science ®Google Scholar
• Sedgwick SG, Smerdon SJ. The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem. Sci. 24(8), 311–316 (1999).
   PubMed Web of Science ®Google Scholar
• Kobe B, Kajava AV. When protein folding is simplified to protein coiling: the continuum of solenoid protein structures. Trends Biochem. Sci. 25(10), 509–515 (2000).
   PubMed Web of Science ®Google Scholar
• Malek S, Huxford T, Ghosh G. Iκ Bα functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-κB. J. Biol. Chem. 273(39), 25427–25435 (1998).
   PubMed Web of Science ®Google Scholar
• Kohl A, Binz HK, Forrer P, Stumpp MT, Plückthun A, Grütter MG. Designed to be stable: crystal structure of a consensus ankyrin repeat protein. Proc. Natl Acad. Sci. USA 100(4), 1700–1705 (2003).
   PubMed Web of Science ®Google Scholar
• Binz HK, Stumpp MT, Forrer P, Amstutz P, Plückthun A. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J. Mol. Biol. 332(2), 489–503 (2003).
   PubMed Web of Science ®Google Scholar
• Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 21(23), 6387–6396 (2002).
   PubMed Web of Science ®Google Scholar
• Mosavi LK, Williams S, Peng Zy ZY. Equilibrium folding and stability of myotrophin: a model ankyrin repeat protein. J. Mol. Biol. 320(2), 165–170 (2002).
   PubMedGoogle Scholar
• Zahnd C, Pecorari F, Straumann N, Wyler E, Plückthun A. Selection and characterization of Her2 binding-designed ankyrin repeat proteins. J. Biol. Chem. 281(46), 35167–35175 (2006).
   PubMed Web of Science ®Google Scholar
• Zahnd C, Kawe M, Stumpp MT et al. Efficient tumor targeting with high-affinity designed ankyrin repeat proteins: effects of affinity and molecular size. Cancer Res. 70(4), 1595–1605 (2010).
   PubMed Web of Science ®Google Scholar
• Zahnd C, Wyler E, Schwenk JM et al. A designed ankyrin repeat protein evolved to picomolar affinity to Her2. J. Mol. Biol. 369(4), 1015–1028 (2007).
   PubMed Web of Science ®Google Scholar
• Vaneycken I, Devoogdt N, Van Gassen N et al. Preclinical screening of anti-HER2 nanobodies for molecular imaging of breast cancer. FASEB J. 25(7), 2433–2446 (2011).
   PubMed Web of Science ®Google Scholar
• D’Huyvetter M, Aerts A, Xavier C et al. Development of 177Lu-nanobodies for radioimmunotherapy of HER2-positive breast cancer: evaluation of different bifunctional chelators. Contrast Media Mol. Imaging 7(2), 254–264 (2012).
   PubMed Web of Science ®Google Scholar
• Holz JB. The TITAN trial – assessing the efficacy and safety of an anti-von Willebrand factor nanobody in patients with acquired thrombotic thrombocytopenic purpura. Transfus. Apher. Sci. 46(3), 343–346 (2012).
   PubMed Web of Science ®Google Scholar
• Huang B, Law MW, Khong PL. Whole-body PET/CT scanning: estimation of radiation dose and cancer risk. Radiology 251(1), 166–174 (2009).
   PubMed Web of Science ®Google Scholar