Fawzy Ali Saad is a Research Assistant Professor,Harvard Medical School,USA

Fawzy Ali Saad

Research Assistant Professor

Organizing Committee


Harvard Medical School


Fawzy Ali Saad was awarded a PhD fellowship from the Italian Ministry of Foreign Affairs to study the Molecular Genetics of Muscular Dystrophy. He earned a PhD in Human Molecular Genetics from Padua University School of Medicine. He completed his postdoctoral training in the field of bone matrix mineralization at the Department of Orthopaedic Surgery, Harvard Medical School. Thereafter, he was awarded an Assistant Professor Position at the Department of Orthopaedic Surgery, Albert Einstein College of Medicine. His research of interest aims at exploring the molecular mechanisms regulating certain aspects of skeletal components such as bone, cartilage, tendon and ligaments. He received a National Research Service Award from NIH and a Service Award from Boston Children’s Hospital; a Harvard Affiliated Hospital. He published more than 30 articles in per-reviewed International Journals.


1 Saad FA, Vitiello L, Merlini L, Mostacciuolo ML, Oliviero S, Danieli GA. A 3' consensus splice mutation in the human dystrophin gene detected by a screening for intra-exonic deletions. Hum Mol Genet 1:345- 346, 1992.

2 Fanin M, Hoffman EP, Saad FA, Martinuzzi A, Danieli GA. Dystrophin positive myoblastes in innervated muscle cultures from Duchenne and Becker muscular dystrophy patients. Neuromuscular Disorders

3:119-127, 1993. 3 Saad FA, Vita G, Mora M, Morandi L, Vitiello L, Oliviero S, Danieli GA. A novel nonsense mutation in the human dystrophin gene. Human Mutation 2:314-316, 1993.

4 Saad FA, Vitiello L, Oliviero S, Mostacciuolo ML, Danieli GA. Detection of unknown gene mutations by multiplex single strand conformation polymorphism. PCR Methods and Applications 3:60-62, 1993.

5 Mostacciuolo ML, Miorin M, Pegoraro E, Fanin M, Schiavon F, Vitiello L, Saad FA, Angelini C, Danieli GA. A reappraisal of the incidence rate of Duchenne and Becker muscular dystrophies, on the basis of molecular diagnosis. Neuroepidemiology 12:326-330, 1993.

6 Saad FA, Basque C, Vitiello L, Danieli GA. DXS997 localized to intron 48 of dystrophin. Hum Mol Genet 2:2199, 1993.

7 Saad FA, Galvagni F, Danieli GA. Rapid detection of human dystrophin gene mutations by multiplex semi-quantitave PCR. Basic and Applied Myology 3:229-231, 1993.

8 Galvagni F, Saad FA, Danieli GA, Miorin M, Vitiello L, Mostacciuolo ML, Angelini C. A study on duplications of the dystrophin gene: Evidence of a geographical difference in the distribution of breakpoints by intron. Hum Genet 94:83-87, 1994.

9 Saad FA, Vita G, Toffolatti L, Danieli GA. A possible missense mutation detected in the dystrophin gene by Double Strand Conformation Analysis. Neuromuscular Disorders 4:335-341, 1994.

10 Siciliano G, Fanin M, Angelini C, Pollina LE, Miorin M, Saad FA, Freda MP, Muratorio A. Prevalent cardiac involvement in dystrophin Becker type mutation. Neuromuscular Disorders 4:381-386, 1994.

11 Saad FA, Halliger B, Müller CR, Roberts RG, Danieli GA. Single base substitutions are detected by Double Strand Conformation Analysis. Nucleic Acids Research 22:4352-4353, 1994.

12 Schiavon F, Mostacciuolo ML, Saad FA, Merlini L, Siciliano G, Angelini C, Danieli GA. Nonradioactive detection of 17p11.2 duplication in CMT1A: a study on 78 patients. J Med Genet. 31:880-883, 1994.

13 Saad FA, Mostacciuolo ML, Trevisan CP, Tomelleri G, Angelini C, Abedel Salam E, Danieli GA. Novel mutations and polymorphisms in the human dystrophin gene detected by double strand conformation analysis. Human Mutation 9:188-190, 1997.

14 Girlanda P, Quartarone A, Buceti R, Sinicropi S, Macaione V, Saad FA, Messina L, Danieli GA, Ferreri G, Vita G. Extra-muscle involvement in dystrophinopathies: An electroretinography and evoked potential study. The Journal of Neurological Sciences 146:127-132, 1997.

15 Rugge M, Bovo D, Busatto G, Parenti AR, Saad FA, Guido M, Ancona E, Ninfo V, Ruol A, Shiao YH. P53 alterations but no human papillomavirus infection in preinvasive and advanced squamous esophageal cancer in Italy. Cancer Epidemiology Biomarkers Prevention 6:171-176, 1997.

16 Saad FA, Merlini L, Mostacciuolo ML, Danieli GA. A double missense mutation in exon 41 of the human dystrophin gene detected by double strand conformation analysis. The American Journal of Medical Genetics 80:99-102, 1998.

17 Jiang Z, Guo Z, Saad FA, Ellis J, Zacksenhaus E. Retinoblastoma gene promoter directs transgene expression exclusively to the nervous system. JBC 276:593-600, 2001.

18 Jane DT, Morvey L, Koblinski J, Saad FA, Sloane BF, Dufresne MJ. Evidence that E-box promoter elements and MyoD transcription factors play a role in the induction of cathepsin B gene expression during human myoblast differentiation. Biol Chem 383:1833-1844, 2002.

19 Hofstaetter JG, Saad FA, Samuel RE, Wunderlich L, Choi H-Y, Glimcher MJ. Differential expression of VEGF isoforms and receptors in knee joint menisci under systemic hypoxia. Biochem and Biophys Res Commun 324:667-672, 2004.

20 Hofstaetter JG, Wunderlich L, Samuel RE, Saad FA, Choi H-Y, Glimcher MJ. Systemic hypoxia alters gene expression levels of structural proteins and growth factors in knee joint cartilage. Biochem and Biophys Res Commun 330:386-394, 2005.

21 Saad FA, Salih E, Wunderlich L, Fluckiger R, Glimcher MJ. Prokaryotic expression of bone sialoprotein and identification of casein kinase II phosphorylation sites. Biochem and Biophys Res Commun 333:443- 447, 2005.

22 Hofstaetter JG, Saad FA, Sunk IG, Bobacz K, Friehs I, Glimcher MJ. Age-dependent expression of VEGF isoforms and receptors in the rabbit anterior cruciate ligament. Biochim Biophys Acta 1770:997- 1002, 2007.

23 Saad FA, Salih E, Glimcher MJ. Identification of osteopontin phosphorylation sites involved in bone remodeling and inhibition of pathological calcification. J Cell Biochem 103:852-856, 2008.

24 Evans CH, Liu FJ, Glatt V, Hoyland JA, Kirker-Head C, Walsh A, Betz O, Wells JW, Betz V, Porter RM, Saad FA, Gerstenfeld LC, Einhorn TA, Harris MB, Vrahas MS. Use of genetically modified muscle and fat grafts to repair defects in bone and cartilage. Eur Cell Mater 18:96-111, 2009.

25 Saad FA, Torres M, Wang H, Graham L. Intercellular lysyl oxidase: Effect of a specific inhibitor on nuclear mass in proliferating cells. Biochem Biophys Res ommun 396:944-949, 2010.

26 Vavken P, Saad FA, Murray MM. Age-dependence of expression of growth factor receptors in ACL fibroblasts. J Orthop Res 28:1107-1112, 2010.

27 Kaza E, Ablasser K, Poutias D, Griffiths ER, Saad FA, Hofstaetter JG, del Nido PJ, Friehs I. Upregulation of Soluble Vascular Endothelial Growth Factor Receptor-1 prevents angiogenesis in hypertrophied myocardium. Cardiovascular Research 89:410-418, 2011.

28 Saad FA, Hofstaetter JG. Proteomic analysis of mineralising osteoblasts identifies novel genes related to bone matrix mineralisation. Int Orthop 35:447-451, 2011.

29 Vavken P, Saad FA, Fleming BC, Murray MM. VEGF receptor expression by ACL fibroblasts affects functional healing of the ACL. Knee Surg Sports Traumatol Arthrosc 19:1675-1682, 2011.

30 Saad FA. Exploration for the molecular pathways that regulate bone matrix mineralization in the proteome era. Current Topics in Biochemical Research14:29-33, 2012.

31 Saad FA. Searching for the Molecular Pathways Regulating Bone Mineral Density in the Proteome and RNA Interference Era. J Orthopedic Rheumatol 1:7-13, 2013.

32 Saad FA, Leong DJ, Wanich TS, Gruson KI, Sun HB. Tendon stem cell: A possible solution for tendon injury repair and aging. Ann Orthop Rheumatol 1:105-106, 2013.

33 Clement C, Moncrieffe H, Lele A, Janow G, Becerra A, Bauli F, Saad FA, Perino G, Montagna C, Cobelli N, Hardin J, Stern L, Ilowite N, Porcelli S, Santambrogio L. Autoimmune response to transthyretin in Juvenile Idiopathic Arthritis. J Clin Invest Insight 1(2).e85633, 2016.


PhD in Human Molecular Genetics. Padua University School of Medicine, Padua, Italy.


Research of interest includes exploring the molecular mechanisms regulating certain aspects of skeletal components such as bone, cartilage, tendon and ligaments. Gene therapy using genetically reprogrammed stem cells to cure musculoskeletal injuries or dysfunction repairs. CRISPR/Cas9 gene editing. Drug discovery for metabolic bone diseases.


1989 – 1995 PhD fellowship from the Italian Ministry of Foreign Affairs; Department of Biology, Padua University School of Medicine, Italy.

2002 – 2004 NIH National Research Service Award; Department of Orthopaedic Surgery, Harvard Medical School and Boston Children’s Hospital.

2007 Service Award; Boston Children’s Hospital


I have collaborated with colleagues from different scientific backgrounds such as physicians and scientists from Italy, Germany, England, Canada, Austria, and USA


Journal of Orthopedics Rheumatology Annals of Orthopedics & Rheumatology