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  1. Article: Ultrasonographic Validation for Needle Placement in the Tibialis Posterior Muscle.

    Albin, Stephanie R / Hoffman, Larisa R / MacDonald, Cameron W / Boriack, Micah / Heyn, Lauren / Schuler, Kaleb / Taylor, Annika / Walker, Jennie / Koppenhaver, Shane L / Reinking, Mark F

    International journal of sports physical therapy

    2021  Volume 16, Issue 6, Page(s) 1541–1547

    Abstract: Background: The tibialis posterior (TP) muscle plays an important role in normal foot function. Safe, efficacious therapeutic approaches addressing this muscle are necessary; however, the location of the muscle in the deep posterior compartment can ... ...

    Abstract Background: The tibialis posterior (TP) muscle plays an important role in normal foot function. Safe, efficacious therapeutic approaches addressing this muscle are necessary; however, the location of the muscle in the deep posterior compartment can create challenges.
    Purpose: The purpose of this study was to assess the accuracy of needle placement in the TP muscle and determine the needle placement in relation to the neurovascular structures located within the deep compartment.
    Design: Cross Sectional Study.
    Methods: Needle placement and ultrasound imaging were performed on 20 healthy individuals. A 50 mm or 60 mm needle was inserted between 30 - 50% of the tibial length measured from the medial tibiofemoral joint. The needle was inserted in a medial to lateral direction into the right extremity with the patient in right side lying. Placement of the needle into the TP muscle was verified with ultrasound imaging, and the shortest distance from the needle to the posterior tibial artery and tibial nerve was measured. The depth from the skin to the superficial border of the TP muscle was also measured.
    Results: Ultrasonography confirmed the needle filament was inserted into the TP muscle in all 20 individuals and did not penetrate the neurovascular bundle in any individual. The mean distance from the needle to the tibial nerve and posterior tibial artery was 10.0 + 4.7 mm and 10.2 + 4.7 mm respectively. The superficial border of the TP muscle from the skin was at a mean depth of 25.8 + 4.9 mm.
    Conclusion: This ultrasound imaging needle placement study supports placement of a solid filament needle into the TP muscle with avoidance of the neurovascular structures of the deep posterior compartment when placed from a medial to lateral direction at 30-50% of the tibial length.
    Level of evidence: 2b.
    Language English
    Publishing date 2021-12-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2628664-6
    ISSN 2159-2896
    ISSN 2159-2896
    DOI 10.26603/001c.29854
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Ultrasonographic Validation for Needle Placement in the Tibialis Posterior Muscle

    Stephanie R. Albin / Larisa R. Hoffman / Cameron W. MacDonald / Micah Boriack / Lauren Heyn / Kaleb Schuler / Annika Taylor / Jennie Walker / Shane L. Koppenhaver / Mark F. Reinking

    International Journal of Sports Physical Therapy, Vol 16, Iss

    2021  Volume 6

    Abstract: Background The tibialis posterior (TP) muscle plays an important role in normal foot function. Safe, efficacious therapeutic approaches addressing this muscle are necessary; however, the location of the muscle in the deep posterior compartment can ... ...

    Abstract # Background The tibialis posterior (TP) muscle plays an important role in normal foot function. Safe, efficacious therapeutic approaches addressing this muscle are necessary; however, the location of the muscle in the deep posterior compartment can create challenges. # Purpose The purpose of this study was to assess the accuracy of needle placement in the TP muscle and determine the needle placement in relation to the neurovascular structures located within the deep compartment. # Design Cross Sectional Study. # Methods Needle placement and ultrasound imaging were performed on 20 healthy individuals. A 50 mm or 60 mm needle was inserted between 30 - 50% of the tibial length measured from the medial tibiofemoral joint. The needle was inserted in a medial to lateral direction into the right extremity with the patient in right side lying. Placement of the needle into the TP muscle was verified with ultrasound imaging, and the shortest distance from the needle to the posterior tibial artery and tibial nerve was measured. The depth from the skin to the superficial border of the TP muscle was also measured. # Results Ultrasonography confirmed the needle filament was inserted into the TP muscle in all 20 individuals and did not penetrate the neurovascular bundle in any individual. The mean distance from the needle to the tibial nerve and posterior tibial artery was 10.0 + 4.7 mm and 10.2 + 4.7 mm respectively. The superficial border of the TP muscle from the skin was at a mean depth of 25.8 + 4.9 mm. # Conclusion This ultrasound imaging needle placement study supports placement of a solid filament needle into the TP muscle with avoidance of the neurovascular structures of the deep posterior compartment when placed from a medial to lateral direction at 30-50% of the tibial length. # Level of Evidence 2b
    Keywords Sports medicine ; RC1200-1245
    Language English
    Publishing date 2021-12-01T00:00:00Z
    Publisher North American Sports Medicine Institute
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: A Mass Spectrometric Assay of METTL3/METTL14 Methyltransferase Activity.

    Buker, Shane M / Gurard-Levin, Zachary A / Wheeler, Benjamin D / Scholle, Michael D / Case, April W / Hirsch, Jeffrey L / Ribich, Scott / Copeland, Robert A / Boriack-Sjodin, P Ann

    SLAS discovery : advancing life sciences R & D

    2019  Volume 25, Issue 4, Page(s) 361–371

    Abstract: A variety of covalent modifications of RNA have been identified and demonstrated to affect RNA processing, stability, and translation. Methylation of adenosine at the N6 position ( ... ...

    Abstract A variety of covalent modifications of RNA have been identified and demonstrated to affect RNA processing, stability, and translation. Methylation of adenosine at the N6 position (m
    MeSH term(s) Adenosine/analogs & derivatives ; Adenosine/genetics ; Adenosine/pharmacology ; Drug Discovery/trends ; Gene Expression Regulation, Developmental/drug effects ; Humans ; Mass Spectrometry/methods ; Methylation/drug effects ; Methyltransferases/genetics ; Multiprotein Complexes/antagonists & inhibitors ; Multiprotein Complexes/genetics ; RNA Processing, Post-Transcriptional/drug effects ; RNA Processing, Post-Transcriptional/genetics ; RNA Stability/drug effects ; RNA Stability/genetics ; RNA, Messenger/drug effects ; RNA, Messenger/genetics ; S-Adenosylhomocysteine/pharmacology
    Chemical Substances Multiprotein Complexes ; RNA, Messenger ; S-Adenosylhomocysteine (979-92-0) ; METTL14 protein, human (EC 2.1.1.-) ; Methyltransferases (EC 2.1.1.-) ; METTL3 protein, human (EC 2.1.1.62) ; Adenosine (K72T3FS567) ; sinefungin (W2U467CIIL)
    Language English
    Publishing date 2019-10-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2885123-7
    ISSN 2472-5560 ; 2472-5552
    ISSN (online) 2472-5560
    ISSN 2472-5552
    DOI 10.1177/2472555219878408
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: CLN-3 protein is expressed in the pancreatic somatostatin-secreting delta cells.

    Boriack, R L / Bennett, M J

    European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society

    2001  Volume 5 Suppl A, Page(s) 99–102

    Abstract: Juvenile neuronal ceroid lipofuscinosis (JNCL) is a severe autosomal recessive neurodegenerative disorder resulting from mutations in the CLN3 gene. The gene product is a 438-amino acid hydrophobic peptide of unknown function containing five ... ...

    Abstract Juvenile neuronal ceroid lipofuscinosis (JNCL) is a severe autosomal recessive neurodegenerative disorder resulting from mutations in the CLN3 gene. The gene product is a 438-amino acid hydrophobic peptide of unknown function containing five transmembrane domains. In order to study the tissue distribution of the peptide, polyclonal antibodies were raised in rabbits to three epitopes and were affinity purified before use. All three antibodies were used together for immunocytochemical staining of human pancreas. This staining showed localization in pancreatic islet cells. Double labelling of the tissue indicated that cells staining for the CLN3 protein were also positive for somatostatin.
    MeSH term(s) Animals ; Antibodies ; Child ; Epitopes/immunology ; Humans ; Immunohistochemistry ; Membrane Glycoproteins ; Molecular Chaperones ; Neuronal Ceroid-Lipofuscinoses/metabolism ; Protein Biosynthesis ; Proteins/analysis ; Proteins/immunology ; Rabbits ; Somatostatin/metabolism ; Somatostatin-Secreting Cells/chemistry ; Somatostatin-Secreting Cells/metabolism
    Chemical Substances Antibodies ; CLN3 protein, human ; Epitopes ; Membrane Glycoproteins ; Molecular Chaperones ; Proteins ; Somatostatin (51110-01-1)
    Language English
    Publishing date 2001-12-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1397146-3
    ISSN 1090-3798
    ISSN 1090-3798
    DOI 10.1053/ejpn.2000.0443
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Erythrocyte membrane reacylation in juvenile neuronal ceroid-lipofuscinosis: measurement of membrane-bound carnitine palmitoyl transferase, acyl-CoA synthetase, and lysophospholipid: acyl-CoA acyltransferase activities.

    Bennett, M J / Boriack, R L

    American journal of medical genetics

    1995  Volume 57, Issue 2, Page(s) 304–306

    Abstract: In order to study the biochemical mechanisms responsible for the membrane fatty acid deficiency in juvenile neuronal ceroid-lipofuscinosis, we have analyzed the reacylation pathway in isolated erythrocyte membranes in 5 patients. We studied membrane ... ...

    Abstract In order to study the biochemical mechanisms responsible for the membrane fatty acid deficiency in juvenile neuronal ceroid-lipofuscinosis, we have analyzed the reacylation pathway in isolated erythrocyte membranes in 5 patients. We studied membrane carnitine palmitoyl transferase, and developed a combined assay to study acyl-CoA synthetase and lysophospholipid acyl-CoA acyltransferase activities. There were no significant differences between control and patient membranes, suggesting that abnormalities in these 3 putative candidate enzymes are not responsible for the disease.
    MeSH term(s) 1-Acylglycerophosphocholine O-Acyltransferase/blood ; Carnitine O-Palmitoyltransferase/blood ; Child ; Coenzyme A Ligases/blood ; Erythrocyte Membrane/enzymology ; Humans ; Neuronal Ceroid-Lipofuscinoses/blood ; Neuronal Ceroid-Lipofuscinoses/enzymology ; Reference Values ; Repressor Proteins ; Saccharomyces cerevisiae Proteins
    Chemical Substances Repressor Proteins ; Saccharomyces cerevisiae Proteins ; Carnitine O-Palmitoyltransferase (EC 2.3.1.21) ; 1-Acylglycerophosphocholine O-Acyltransferase (EC 2.3.1.23) ; Coenzyme A Ligases (EC 6.2.1.-) ; FAA2 protein, S cerevisiae (EC 6.2.1.3) ; long-chain-fatty-acid-CoA ligase (EC 6.2.1.3)
    Language English
    Publishing date 1995-06-05
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 133387-2
    ISSN 0148-7299
    ISSN 0148-7299
    DOI 10.1002/ajmg.1320570239
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Wilms tumor in a child with L-2-hydroxyglutaric aciduria.

    Rogers, Robert E / Deberardinis, Ralph J / Klesse, Laura J / Boriack, Richard L / Margraf, Linda R / Rakheja, Dinesh

    Pediatric and developmental pathology : the official journal of the Society for Pediatric Pathology and the Paediatric Pathology Society

    2010  Volume 13, Issue 5, Page(s) 408–411

    Abstract: We report a male infant with L-2-hydroxyglutaric aciduria and Wilms tumor. L-2-hydroxyglutaric ... of an extracranial tumor associated with L-2-hydroxyglutaric aciduria. This observation potentially widens the tumor ... spectrum in this metabolic disorder and may lead to further insight into the relationship between L-2 ...

    Abstract We report a male infant with L-2-hydroxyglutaric aciduria and Wilms tumor. L-2-hydroxyglutaric aciduria is a rare, autosomal-recessive, inborn error of metabolism characterized by a variable degree of progressive encephalopathy. Of the fewer than 100 cases reported in the literature, at least 9 patients have developed tumors of the central nervous system. To our knowledge, the present case is the 1st example of an extracranial tumor associated with L-2-hydroxyglutaric aciduria. This observation potentially widens the tumor spectrum in this metabolic disorder and may lead to further insight into the relationship between L-2-hydroxyglutaric acid and cellular transformation.
    MeSH term(s) Antineoplastic Combined Chemotherapy Protocols/therapeutic use ; Brain Diseases, Metabolic, Inborn/complications ; Dactinomycin/administration & dosage ; Humans ; Infant ; Kidney Neoplasms/complications ; Kidney Neoplasms/therapy ; Male ; Nephrectomy ; Vincristine/administration & dosage ; Wilms Tumor/complications ; Wilms Tumor/therapy
    Chemical Substances Dactinomycin (1CC1JFE158) ; Vincristine (5J49Q6B70F)
    Language English
    Publishing date 2010-09
    Publishing country United States
    Document type Case Reports ; Journal Article
    ZDB-ID 1463498-3
    ISSN 1615-5742 ; 1093-5266
    ISSN (online) 1615-5742
    ISSN 1093-5266
    DOI 10.2350/09-12-0768-CR.1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Polyunsaturated fatty acids reverse the lysosomal storage and accumulation of subunit 9 of mitochondrial F1F0-ATP synthase in cultured lymphoblasts from patients with Batten disease.

    Bennett, M J / Boriack, R L / Boustany, R M

    Journal of inherited metabolic disease

    1997  Volume 20, Issue 3, Page(s) 457–460

    MeSH term(s) Cell Line ; Enzyme Inhibitors/pharmacology ; Fatty Acids, Unsaturated/pharmacology ; Gentamicins/pharmacology ; Humans ; Infant, Newborn ; Lymphocytes/drug effects ; Lymphocytes/enzymology ; Lymphocytes/metabolism ; Mitochondria/drug effects ; Mitochondria/enzymology ; Mitochondria/metabolism ; Neuronal Ceroid-Lipofuscinoses/enzymology ; Proton-Translocating ATPases/antagonists & inhibitors ; Proton-Translocating ATPases/metabolism
    Chemical Substances Enzyme Inhibitors ; Fatty Acids, Unsaturated ; Gentamicins ; Proton-Translocating ATPases (EC 3.6.3.14)
    Language English
    Publishing date 1997-08-15
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 438341-2
    ISSN 1573-2665 ; 0141-8955
    ISSN (online) 1573-2665
    ISSN 0141-8955
    DOI 10.1023/a:1005387608456
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: In-utero and post-delivery supplementation of motor neuron degeneration mutant mice with polyunsaturated fatty acids does not alter the clinical or pathological course.

    Bennett, M J / Boriack, R L / Birch, D G

    Neuropediatrics

    1997  Volume 28, Issue 1, Page(s) 82–84

    Abstract: We have studied the effects of polyunsaturated fatty acid (PUFA) supplementation in utero and throughout life in mnd mutant mice, a proposed model for juvenile neuronal ceroid lipofuscinosis (CLN-3). Unlike our earlier in-vitro studies in humans with CLN- ...

    Abstract We have studied the effects of polyunsaturated fatty acid (PUFA) supplementation in utero and throughout life in mnd mutant mice, a proposed model for juvenile neuronal ceroid lipofuscinosis (CLN-3). Unlike our earlier in-vitro studies in humans with CLN-3, and in-vitro studies in CLN-3 lymphoblasts, we saw no beneficial effects in electroretinographic, electron microscopic or clinical studies in the mnd mice. Electron microscopy of brain revealed a pattern which was not consistent with the characteristic ceroid patterns in CLN-3. Our data suggest that the mnd mouse is not responsive to PUFA supplementation and may not be an appropriate animal model for CLN-3.
    MeSH term(s) Animals ; Animals, Newborn ; Brain/pathology ; Disease Models, Animal ; Fatty Acids, Unsaturated/administration & dosage ; Female ; Male ; Mice ; Mice, Neurologic Mutants ; Microscopy, Electron ; Neuronal Ceroid-Lipofuscinoses/diet therapy ; Neuronal Ceroid-Lipofuscinoses/genetics ; Neuronal Ceroid-Lipofuscinoses/pathology ; Pregnancy
    Chemical Substances Fatty Acids, Unsaturated
    Language English
    Publishing date 1997-02
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 573291-8
    ISSN 1439-1899 ; 0174-304X
    ISSN (online) 1439-1899
    ISSN 0174-304X
    DOI 10.1055/s-2007-973678
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Impaired mitochondrial fatty acid oxidative flux in fibroblasts from a patient with malonyl-CoA decarboxylase deficiency.

    Bennett, M J / Harthcock, P A / Boriack, R L / Cohen, J C

    Molecular genetics and metabolism

    2001  Volume 73, Issue 3, Page(s) 276–279

    Abstract: Malonyl-CoA decarboxylase deficiency is a rare inborn error of metabolism. It has been suggested but never demonstrated that many of the clinical features arise due to inhibition of mitochondrial fatty acid oxidation by accumulated malonyl-CoA. We ... ...

    Abstract Malonyl-CoA decarboxylase deficiency is a rare inborn error of metabolism. It has been suggested but never demonstrated that many of the clinical features arise due to inhibition of mitochondrial fatty acid oxidation by accumulated malonyl-CoA. We studied the oxidation of fatty acids in cultured skin fibroblasts from a recently described patient with malonyl-CoA decarboxylase deficiency. There was a marked reduction in the oxidation of palmitic and myristic acids both under baseline conditions and when the cells were cultured in the presence of high concentrations of acetate, a malonyl-CoA precursor. These results suggest that there is inhibition of fatty acid oxidation in malonyl-CoA decarboxylase deficiency and that this inhibition may be related to some of the clinical phenotypes.
    MeSH term(s) Carboxy-Lyases/deficiency ; Carnitine O-Palmitoyltransferase/metabolism ; Cells, Cultured ; Child ; DNA, Complementary/metabolism ; Exons ; Fatty Acids/metabolism ; Fibroblasts/metabolism ; Humans ; Male ; Mitochondria/metabolism ; Myristic Acids/metabolism ; Oxygen/metabolism ; Palmitic Acid/metabolism ; Phenotype ; Skin/cytology
    Chemical Substances DNA, Complementary ; Fatty Acids ; Myristic Acids ; Palmitic Acid (2V16EO95H1) ; Carnitine O-Palmitoyltransferase (EC 2.3.1.21) ; Carboxy-Lyases (EC 4.1.1.-) ; malonyl-CoA decarboxylase (EC 4.1.1.9) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2001-07
    Publishing country United States
    Document type Case Reports ; Journal Article
    ZDB-ID 1418518-0
    ISSN 1096-7206 ; 1096-7192
    ISSN (online) 1096-7206
    ISSN 1096-7192
    DOI 10.1006/mgme.2001.3196
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Oxidation of alpha-ketoglutarate is required for reductive carboxylation in cancer cells with mitochondrial defects.

    Mullen, Andrew R / Hu, Zeping / Shi, Xiaolei / Jiang, Lei / Boroughs, Lindsey K / Kovacs, Zoltan / Boriack, Richard / Rakheja, Dinesh / Sullivan, Lucas B / Linehan, W Marston / Chandel, Navdeep S / DeBerardinis, Ralph J

    Cell reports

    2014  Volume 7, Issue 5, Page(s) 1679–1690

    Abstract: Mammalian cells generate citrate by decarboxylating pyruvate in the mitochondria to supply the tricarboxylic acid (TCA) cycle. In contrast, hypoxia and other impairments of mitochondrial function induce an alternative pathway that produces citrate by ... ...

    Abstract Mammalian cells generate citrate by decarboxylating pyruvate in the mitochondria to supply the tricarboxylic acid (TCA) cycle. In contrast, hypoxia and other impairments of mitochondrial function induce an alternative pathway that produces citrate by reductively carboxylating α-ketoglutarate (AKG) via NADPH-dependent isocitrate dehydrogenase (IDH). It is unknown how cells generate reducing equivalents necessary to supply reductive carboxylation in the setting of mitochondrial impairment. Here, we identified shared metabolic features in cells using reductive carboxylation. Paradoxically, reductive carboxylation was accompanied by concomitant AKG oxidation in the TCA cycle. Inhibiting AKG oxidation decreased reducing equivalent availability and suppressed reductive carboxylation. Interrupting transfer of reducing equivalents from NADH to NADPH by nicotinamide nucleotide transhydrogenase increased NADH abundance and decreased NADPH abundance while suppressing reductive carboxylation. The data demonstrate that reductive carboxylation requires bidirectional AKG metabolism along oxidative and reductive pathways, with the oxidative pathway producing reducing equivalents used to operate IDH in reverse.
    MeSH term(s) Animals ; Cell Line ; Cell Line, Tumor ; Citric Acid Cycle ; Cricetinae ; Cricetulus ; Fumarate Hydratase/genetics ; Humans ; Isocitrate Dehydrogenase/metabolism ; Ketoglutaric Acids/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Mutation ; NAD/metabolism ; NADP Transhydrogenase, AB-Specific/metabolism ; Neoplasms/genetics ; Neoplasms/metabolism ; Oxidation-Reduction
    Chemical Substances Ketoglutaric Acids ; NAD (0U46U6E8UK) ; Isocitrate Dehydrogenase (EC 1.1.1.41) ; NADP Transhydrogenase, AB-Specific (EC 1.6.1.2) ; Fumarate Hydratase (EC 4.2.1.2)
    Language English
    Publishing date 2014-05-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2014.04.037
    Database MEDical Literature Analysis and Retrieval System OnLINE

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