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    • Osteogenesis Imperfecta
    • Darwin J Prockop
    • Darwin J Prockop: Influence Statistics

      Darwin J Prockop

      Darwin J Prockop

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      College of Medicine, Health Science Center, Texas A & M University | Institute for Regenerative Medicine, College of Medicine, Texas A&M University, College Station, Texas, ...

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      Darwin J Prockop:Expert Impact

      Concepts for whichDarwin J Prockophas direct influence:Osteogenesis imperfecta,Stem cells,Transgenic mice,Bone marrow,Stromal cells,Type procollagen,Triple helix,Collagen fibrils.

      Darwin J Prockop:KOL impact

      Concepts related to the work of other authors for whichfor which Darwin J Prockop has influence:Stem cells,Bone marrow,Osteogenic differentiation,Tissue engineering,Regenerative medicine,Cell therapy,Osteogenesis imperfecta.

      KOL Resume for Darwin J Prockop

      Year
      2019

      College of Medicine, Health Science Center, Texas A & M University

      2018

      Texas A&M Health Science Center College of Medicine

      2017

      Department of Molecular and Cellular Medicine, Texas A&M Health Science Center College of Medicine, College Station, TX 77843;

      Institute for Regenerative Medicine, College of Medicine, Texas AM University, 1114 TAMU, 206 Olsen Boulevard, College Station, TX 77845, USA

      2016

      Institute for Regenerative Medicine, College of Medicine, Texas A&M University System Health Science Center, Temple, TX 76502;

      2015

      Department of Medicine, Texas A&M Health Science Center Institute for Regenerative Medicine Temple Texas USA

      Institute for Regenerative Medicine at Scott & White, College of Medicine, Texas A&M Health Science Center, Temple, TX 76502

      2014

      Institute for Regenerative Medicine, Texas A&M Health Science Center, College of Medicine at Scott & White, Temple, Texas.

      2013

      Texas A&M Health Science Center College of Medicine Institute for Regenerative Medicine, Scott & White, Temple, Texas, USA

      2012

      Department of Medicine, Texas A&M Health Science College of Medicine, Institute for Regenerative Medicine at Scott & White, Temple, Texas, USA

      Institute for Regenerative Medicine, Texas A&M Health Science Center College of Medicine at Scott & White, Temple, Texas

      2011

      Texas A&M Health Science Center, College of Medicine, Institute for Regenerative Medicine at Scott & White, 5701 Airport Road, Module C, Temple, TX 76502, USA

      2010

      Texas A&M Health Science Center, College of Medicine, Institute for Regenerative Medicine at Scott & White, Temple, Texas.

      Center for Gene Therapy, Tulane University Health Sciences Center, New Orleans, Louisiana.

      2009

      Center for Gene Therapy, Tulane University School of Medicine, 70112, New Orleans, LA, USA

      Biomedical Sciences Graduate Program, Tulane University School of Medicine, New Orleans, Louisiana.

      2008

      Institute for Regenerative Medicine, Texas A&M Health Science Center, Temple, TX,76502, USA

      Center for Gene Therapy and Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, LA

      Biochemistry, and

      2007

      Tulane University Health Sciences Center Tulane Center for Gene Therapy New Orleans Louisiana USA

      2006

      Center for Gene Therapy, Tulane University Health Sciences Center, 1430 Tulane Avenue, New Orleans, LA 70112; and †Department of Medicine, Cardiovascular Research Institute, University of Vermont, 208 South Park Drive, Suite 2, Colchester, VT 05446

      Tulane School of Medicine, New Orleans, Louisiana, USA

      2005

      Center for Gene Therapy, Tulane University Health Sciences Center, New Orleans, LA 70112

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      Sample of concepts for which Darwin J Prockop is among the top experts in the world.
      Concept World rank
      enzyme isolated complexes #1
      uvirradiated fibroblasts #1
      pccollagen #1
      trans4hydroxyl #1
      510 residues #1
      chick embryos analogue #1
      concanavalin prolyl hydroxylase #1
      biosynthesis pyridines #1
      soluble biological #1
      cells fetal blood #1
      sulfated mucopolysaccharides collagen #1
      bmd chromosomes human #1
      hydroxyproline infused gelatin #1
      cleavage homotrimer #1
      production type procollagen #1
      embryo chromatography #1
      5 position intron #1
      tsg6dependent manner #1
      polypeptides precursor form #1
      protein procollagen polypeptides #1
      phenotype dna polymorphism #1
      osteogenesis imperfecta data #1
      342414 #1
      b220 lymphocytes #1
      14chydroxylysine #1
      mutated type #1
      col1a2 gene mutations #1
      40 μg ascorbate #1
      palpha2 palpha1 #1
      beneficial effects mscs #1
      intraduodenal hydrolysis gelatin #1
      glycine codon #1
      models beneficial effects #1
      cproteinase digestion #1
      gene therapy hmscs #1
      rhciibac data #1
      gluthamine #1
      paradigm mscs #1
      mmscs nucleofection #1
      marrow source #1
      therapeutic protein mscs #1
      typei procollagen exon #1
      human col9a1 #1
      myocardial infarction hmscs #1
      a1exosomes hippocampus #1
      mice heterozygous knockout #1
      loop activated mscs #1
      proα2 #1
      col1a2 locus #1
      underlying diffuse scatter #1
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      Prominent publications by Darwin J Prockop

      KOL-Index: 18308

      Experiments were carried out to test the hypothesis that a 19-year-old proband with a mild variant of Ehlers-Danlos syndrome type IV had a mutation in the gene for type III procollagen. cDNA and genomic DNA were analyzed by using the polymerase chain reaction and cloning of the products into M13 filamentous phage. A mutation was found that converted the codon for glycine 883 of the triple-helical domain in one allele for type III procollagen to a codon for aspartate. The polymerase chain ...

      Known for Type Iii Procollagen | Danlos Syndrome | Single Base Mutation | Codon Glycine | Thermal Stability
      KOL-Index: 16692

      Previous observations suggested that pNcollagen III, the partially processed form of type III procollagen, coats fibrils of collagen I and thereby helps regulate the diameter of fibrils formed by collagen I. The previous observations, however, did not exclude the possibility that pNcollagen III was deposited on preformed collagen I fibrils after the fibrils were assembled. Here, mixtures of pNcollagen III and collagen I were generated simultaneously by enzymatic cleavage of precursor ...

      Known for Pncollagen Iii | Collagen Fibrils | Previous Observations | Lateral Growth | True Copolymers
      KOL-Index: 15640

      Recent reports have demonstrated that a series of probands with severe osteogenesis imperfecta had single base mutations in one of the two structural genes for type I procollagen that substituted amino acids with bulkier side chains for glycine residues and decreased the melting temperature of the triple helix. Here we demonstrate that the type I procollagen synthesized by cultured fibroblasts from a proband with a severe form of osteogenesis imperfecta consisted of normal molecules and ...

      Known for Thermal Stability | Triple Helix | Osteogenesis Imperfecta | Glycine Substitutions | Type Procollagen
      KOL-Index: 15451

      Lenses of chick embryos and matrix-free cells obtained by enzymic dissociation of the embryonic lenses were incubated with [14C]proline, and the basement membrane collagen synthesized by the systems was partially characterized. The newly synthesized [14C]collagen obtained from intact lenses was found to be completely solubilized after denaturation and reduction with sodium dodecyl sulfate and mercaptoethanol. After treatment of the newly synthesized [14C]-collagen with pepsin, less than ...

      Known for Basement Membrane Collagen | Precursor Form | Α Chains | Embryonic Chick | Free Cells
      KOL-Index: 14965

      INTRODUCTION: Multipotent stromal cells (MSCs) are currently in clinical trials for a number of inflammatory diseases. Recent studies have demonstrated the ability of MSCs to attenuate inflammation in rodent models of acute lung injury (ALI) suggesting that MSCs may also be beneficial in treating ALI.

      METHODS: To better understand how human MSCs (hMSCs) may act in ALI, the lungs of immunocompetent mice were exposed to lipopolysaccharide (LPS) and four hours later bone marrow derived ...

      Known for Lung Injury | Induced Acute | Bronchoalveolar Lavage | Tumor Necrosis Factor | Mscs Ali
      KOL-Index: 14905

      The biosynthesis of collagen was studied both in vivo and in vitro in embryonic chick lens, a tissue in which all of the collagen is in the basement membrane of the lens capsule. Experiments in vivo demonstrated that only a small fraction of the total protein synthesized by the lens is collagen but that the rate of collagen synthesis increases significantly between about Day 18 and Day 20 of embryonic development. [14C]Proline was incorporated into basement membrane collagen by intact ...

      Known for Basement Membrane Collagen | Embryonic Chick | Free Cells | Polypeptide Chains | Protein Secretion
      KOL-Index: 14867

      Recent clinical observations have suggested that retinoids, which are in frequent use in dermatology, can affect the connective tissue metabolism in skin and other tissues. In this study, we examined the effects of several retinoids on the metabolism of collagen by human skin fibroblasts in culture. Incubation of cultured fibroblasts with all-trans-retinoic acid or 13-cis-retinoic acid, in 10(-5) M or higher concentrations, markedly reduced the procollagen production, as measured by ...

      Known for Retinoic Acid | Fibroblast Cultures | Gene Expression | Human Skin | Procollagen Production
      KOL-Index: 14776

      Nucleotide sequences were determined for two cloned cDNAs encoding for over three-fourths of the pro alpha 1 (I) chain of type I procollagen from man. Comparison with previously published data on amino acid sequences of the alpha 1 (I) chain of type I collagen made it possible to examine mutations in the transcribed products of the gene which have occurred during the evolution of man, calf, rat, mouse, and chick. Comparison of the nucleotide sequences with the corresponding sequences of ...

      Known for Nucleotide Sequences | Human Type | 1 Chain | Selective Pressure | Alpha 2i
      KOL-Index: 14763

      A fraction of the pro alpha 1(I) and pro alpha 2(I) chains in type I procollagen synthesized by the fibroblasts from a proband with a lethal variant of osteogenesis imperfecta were overmodified by posttranslational reactions. After digestion with pepsin, some of the alpha 1(I) chains were recovered as disulfide-linked dimers. Mapping of cyanogen bromide peptides indicated that the disulfide link was contained in alpha 1-CB6, the cyanogen bromide fragment containing amino acid residues ...

      Known for Type Procollagen | Lethal Variant | Osteogenesis Imperfecta | Single Base Mutation | Alpha 1i Chain
      KOL-Index: 14717

      The University of Vermont College of Medicine and the Vermont Lung Center, in collaboration with the NHLBI, Alpha-1 Foundation, American Thoracic Society, European Respiratory Society, International Society for Cell Therapy, and the Pulmonary Fibrosis Foundation, convened a workshop, "Stem Cells and Cell Therapies in Lung Biology and Lung Diseases," held July 29 to August 1, 2013 at the University of Vermont. The conference objectives were to review the current understanding of the role ...

      Known for Stem Cells | Lung Biology | Thoracic Society | University Vermont | Cell Therapy
      KOL-Index: 14516

      Two systems were used to generate collagen fibrils in vitro by enzymic cleavage of intermediates in the conversion of procollagen to collagen. In one system fibrils were generated by using procollagen NH2-terminal proteinase to cleave pNcollagen, the intermediate which contains the NH2-terminal but not the COOH-terminal propeptides found in procollagen. When pNcollagen was incubated with procollagen NH2-terminal proteinase, the NH2-terminal propeptides were enzymically cleaved from the ...

      Known for Collagen Fibrils | Enzymic Cleavage | Electron Microscopy | Nh2terminal Propeptides | Bone Morphogenetic
      KOL-Index: 14120

      Cartilage from chick embryos was incubated with 14C-proline and puromycin in order to prepare puromycin peptides which were substrates for the synthesis of 14C-hydroxyproline with protocollagen proline hydroxylase. Stable enzyme-substrate complexes were recovered when the substrate was mixed with the enzyme and the mixtures were examined by gel filtration. Although ascorbate, α-ketoglutarate, and ferrous iron are required for catalytic activity, formation of the enzyme-substrate ...

      Known for Polypeptide Substrate | Proline Hydroxylase | Affinity Enzyme | Cartilage Chick | Ascorbic Acid
      KOL-Index: 13861

      Recent reports indicated that vascular remodeling and angiogenesis are promoted by conditioned medium from the cells referred to as multipotent stromal cells (MSCs). However, the molecular events triggered by MSC-conditioned medium (CdM) were not defined. We examined the effects of CdM from human MSCs on cultures of primary human aortic endothelial cells (HAECs). The CdM inhibited hypoxia-induced apoptosis and cell death of HAECs. It also promoted tube formation by HAECs in an assay in ...

      Known for Conditioned Medium | Stromal Cell | Human Multipotent | Angiogenic Effects | Akt Pathway
      KOL-Index: 13515

      OBJECTIVE: Meniscal regeneration was previously shown to be enhanced by injection of mesenchymal stem/stromal cells (MSCs) but the mode of action of the MSCs was not established. The aim of this study was to define how injection of MSCs enhances meniscal regeneration.

      DESIGN: A hemi-meniscectomy model in rats was used. Rat-MSCs (rMSCs) or human-MSCs (hMSCs) were injected into the right knee joint after the surgery, and PBS was injected into the left. The groups were compared ...

      Known for Meniscal Regeneration | Indian Hedgehog | Stem Cell | Articular Injection | Human Mesenchymal
      KOL-Index: 13451

      Bone marrow stroma contains a unique cell population, referred to as marrow stromal cells (MSCs), capable of differentiating along multiple mesenchymal cell lineages. A standard liquid culture system has been developed to isolate MSCs from whole marrow by their adherence to plastic wherein the cells grow as clonal populations derived from a single precursor termed the colony-forming-unit fibroblast (CFU-F). Using this liquid culture system, we demonstrate that the relative abundance of ...

      Known for Inbred Mice | Bone Marrow | Stromal Cells | Plastic Adherent | Cell Differentiation

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      College of Medicine, Health Science Center, Texas A & M University | Institute for Regenerative Medicine, College of Medicine, Texas A&M University, College Station, Texas, USA, View further author information | Institute for Regenerative Medicine, D

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