Milena Dimori
Research Assistant
Also affiliated: University of Milan (1992–1998); University of Arkansas Medical Center (2024)
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: 359
Positions
-
Research Assistant publications 2013–2026University of Arkansas for Medical Sciences Institution web page
Selected Publications
-
Dissecting primary versus secondary effects of osteogenesis imperfecta on abnormal lung development and function (2026)
-
A new Col1a1 conditional knock-in mouse model to study osteogenesis imperfecta (2024)
-
A Rab33b missense mouse model for Smith-McCort dysplasia shows bone resorption defects and altered protein glycosylation (2023)
-
Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta (2022)
-
Haploinsufficiency of Col5a1 causes intrinsic lung and respiratory changes in a mouse model of classical Ehlers‐Danlos syndrome (2022)
-
Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass (2022)
-
Dental and craniofacial defects in the Crtap−/− mouse model of osteogenesis imperfecta type VII (2020)
-
Respiratory defects in the CrtapKO mouse model of osteogenesis imperfecta (2020)
-
The Osteocyte Transcriptome Is Extensively Dysregulated in Mouse Models of Osteogenesis Imperfecta (2019)
-
Loss of RANKL in osteocytes dramatically increases cancellous bone mass in the osteogenesis imperfecta mouse (oim) (2018)
-
Expression characterization and functional implication of the collagen-modifying Leprecan proteins in mouse gonadal tissue and mature sperm (2018)
-
P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA (2017)
-
Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation (2016)
-
Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis (2013)
Collaboration Network
Top Collaborators
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA
- Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis
- The Osteocyte Transcriptome Is Extensively Dysregulated in Mouse Models of Osteogenesis Imperfecta
- Loss of RANKL in osteocytes dramatically increases cancellous bone mass in the osteogenesis imperfecta mouse (oim)
Showing 5 of 13 shared publications
- Respiratory defects in the CrtapKO mouse model of osteogenesis imperfecta
- Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta
- Haploinsufficiency of Col5a1 causes intrinsic lung and respiratory changes in a mouse model of classical Ehlers‐Danlos syndrome
- A new Col1a1 conditional knock-in mouse model to study osteogenesis imperfecta
- Dissecting primary versus secondary effects of osteogenesis imperfecta on abnormal lung development and function
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- The Osteocyte Transcriptome Is Extensively Dysregulated in Mouse Models of Osteogenesis Imperfecta
- Loss of RANKL in osteocytes dramatically increases cancellous bone mass in the osteogenesis imperfecta mouse (oim)
- Expression characterization and functional implication of the collagen-modifying Leprecan proteins in mouse gonadal tissue and mature sperm
- The Osteocyte Transcriptome Is Extensively Dysregulated in Mouse Models of Osteogenesis Imperfecta
- Loss of RANKL in osteocytes dramatically increases cancellous bone mass in the osteogenesis imperfecta mouse (oim)
- Respiratory defects in the CrtapKO mouse model of osteogenesis imperfecta
- Expression characterization and functional implication of the collagen-modifying Leprecan proteins in mouse gonadal tissue and mature sperm
- Loss of RANKL in osteocytes dramatically increases cancellous bone mass in the osteogenesis imperfecta mouse (oim)
- Distinct type I collagen alterations cause intrinsic lung and respiratory defects of variable severity in mouse models of osteogenesis imperfecta
- A new Col1a1 conditional knock-in mouse model to study osteogenesis imperfecta
- Dissecting primary versus secondary effects of osteogenesis imperfecta on abnormal lung development and function
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis
- Expression characterization and functional implication of the collagen-modifying Leprecan proteins in mouse gonadal tissue and mature sperm
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis
- Expression characterization and functional implication of the collagen-modifying Leprecan proteins in mouse gonadal tissue and mature sperm
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA
- Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis
- Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis
- Expression characterization and functional implication of the collagen-modifying Leprecan proteins in mouse gonadal tissue and mature sperm
- Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis
- Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
- Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis
- Expression characterization and functional implication of the collagen-modifying Leprecan proteins in mouse gonadal tissue and mature sperm
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- Sc65 Is a Novel Endoplasmic Reticulum Protein That Regulates Bone Mass Homeostasis
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA
- Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation
- P3h3-null and Sc65-null Mice Phenocopy the Collagen Lysine Under-hydroxylation and Cross-linking Abnormality of Ehlers-Danlos Syndrome Type VIA
Similar Researchers
Based on overlapping research topics