Milena Dimori
Researcher
Also affiliated: University of Milan (1992–1998)
Faculty Researcher
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Milena Dimori's research focuses on developing and utilizing animal models, primarily mice and swine, to investigate human genetic disorders, with a particular emphasis on osteogenesis imperfecta and Ehlers-Danlos syndrome. Her work examines the intricate relationship between skeletal defects and respiratory function, exploring how alterations in collagen type I impact lung development and physiological processes. Dimori's publications detail the creation of new mouse models to dissect specific genetic contributions to these conditions, such as the role of COL5A1 haploinsufficiency in classical Ehlers-Danlos syndrome and the effects of Rab33b missense mutations on bone resorption and protein glycosylation in Smith-McCort dysplasia. She also investigates the cellular mechanisms underlying bone mass regulation, including the role of autophagy in bone density. Dimori collaborates with researchers at the University of Arkansas for Medical Sciences, including Roy Morello, Melda Onal, Charles A. O’Brien, and Jeff D. Thostenson, with whom she has co-authored multiple publications.
Metrics
- h-index: 10
- Publications: 29
- Citations: 355
Selected Publications
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Dissecting primary versus secondary effects of osteogenesis imperfecta on abnormal lung development and function (2026)
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A new <i>Col1a1</i> conditional knock-in mouse model to study osteogenesis imperfecta (2024)
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A Rab33b missense mouse model for Smith-McCort dysplasia shows bone resorption defects and altered protein glycosylation (2023)
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Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta (2022)
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Haploinsufficiency of <i>Col5a1</i> causes intrinsic lung and respiratory changes in a mouse model of classical Ehlers‐Danlos syndrome (2022)
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Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass (2022)
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Dental and craniofacial defects in the <i>Crtap<sup>−/−</sup></i> mouse model of osteogenesis imperfecta type VII (2020)
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Respiratory defects in the <i>Crtap</i>KO mouse model of osteogenesis imperfecta (2020)
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The Osteocyte Transcriptome Is Extensively Dysregulated in Mouse Models of Osteogenesis Imperfecta (2019)
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Loss of RANKL in osteocytes dramatically increases cancellous bone mass in the osteogenesis imperfecta mouse (oim) (2018)
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Expression characterization and functional implication of the collagen-modifying Leprecan proteins in mouse gonadal tissue and mature sperm (2018)
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P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA (2017)
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Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation (2016)
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Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis (2013)
Collaboration Network
Top Collaborators
- Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta
- Haploinsufficiency of <i>Col5a1</i> causes intrinsic lung and respiratory changes in a mouse model of classical Ehlers‐Danlos syndrome
- A Rab33b missense mouse model for Smith-McCort dysplasia shows bone resorption defects and altered protein glycosylation
- A new <i>Col1a1</i> conditional knock-in mouse model to study osteogenesis imperfecta
- Dissecting primary versus secondary effects of osteogenesis imperfecta on abnormal lung development and function
- Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta
- Haploinsufficiency of <i>Col5a1</i> causes intrinsic lung and respiratory changes in a mouse model of classical Ehlers‐Danlos syndrome
- A new <i>Col1a1</i> conditional knock-in mouse model to study osteogenesis imperfecta
- Dissecting primary versus secondary effects of osteogenesis imperfecta on abnormal lung development and function
- Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta
- A new <i>Col1a1</i> conditional knock-in mouse model to study osteogenesis imperfecta
- Dissecting primary versus secondary effects of osteogenesis imperfecta on abnormal lung development and function
- Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
- A Rab33b missense mouse model for Smith-McCort dysplasia shows bone resorption defects and altered protein glycosylation
- Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
- A new <i>Col1a1</i> conditional knock-in mouse model to study osteogenesis imperfecta
- Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta
- Haploinsufficiency of <i>Col5a1</i> causes intrinsic lung and respiratory changes in a mouse model of classical Ehlers‐Danlos syndrome
- Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
- Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
- Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
- Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
- Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
- Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta
- Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta
- A Rab33b missense mouse model for Smith-McCort dysplasia shows bone resorption defects and altered protein glycosylation
- A Rab33b missense mouse model for Smith-McCort dysplasia shows bone resorption defects and altered protein glycosylation
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