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  1. Book ; Thesis: Mitochondrial transmembrane carriers in mitochondriocytopathies

    Huizing, Marjan

    1998  

    Author's details door Marjan Huizing
    Language English
    Size 143 S. : Ill., graph. Darst.
    Publishing country Netherlands
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Nijmegen, Kath. Univ., Diss., 1998
    Note Zsfassung in niederländ. Sprache
    HBZ-ID HT008401322
    ISBN 90-901-1340-1 ; 978-90-901-1340-1
    Database Catalogue ZB MED Medicine, Health

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  2. Article ; Online: Inherited disorders of lysosomal membrane transporters.

    Huizing, Marjan / Gahl, William A

    Biochimica et biophysica acta. Biomembranes

    2020  Volume 1862, Issue 12, Page(s) 183336

    Abstract: Disorders caused by defects in lysosomal membrane transporters form a distinct subgroup of lysosomal storage disorders (LSDs). To date, defects in only 10 lysosomal membrane transporters have been associated with inherited disorders. The clinical ... ...

    Abstract Disorders caused by defects in lysosomal membrane transporters form a distinct subgroup of lysosomal storage disorders (LSDs). To date, defects in only 10 lysosomal membrane transporters have been associated with inherited disorders. The clinical presentations of these diseases resemble the phenotypes of other LSDs; they are heterogeneous and often present in children with neurodegenerative manifestations. However, for pathomechanistic and therapeutic studies, lysosomal membrane transport defects should be distinguished from LSDs caused by defective hydrolytic enzymes. The involved proteins differ in function, localization, and lysosomal targeting, and the diseases themselves differ in their stored material and therapeutic approaches. We provide an overview of the small group of disorders of lysosomal membrane transporters, emphasizing discovery, pathomechanism, clinical features, diagnostic methods and therapeutic aspects. We discuss common aspects of lysosomal membrane transporter defects that can provide the basis for preclinical research into these disorders.
    MeSH term(s) Amino Acid Transport Systems, Neutral/genetics ; Amino Acid Transport Systems, Neutral/metabolism ; Cystinosis/genetics ; Cystinosis/pathology ; Histiocytosis/genetics ; Histiocytosis/pathology ; Humans ; Lysosomal Storage Diseases/genetics ; Lysosomal Storage Diseases/pathology ; Lysosomes/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Nucleoside Transport Proteins/genetics ; Nucleoside Transport Proteins/metabolism ; Organic Anion Transporters/genetics ; Organic Anion Transporters/metabolism ; Sialic Acid Storage Disease/genetics ; Sialic Acid Storage Disease/pathology ; Symporters/genetics ; Symporters/metabolism
    Chemical Substances Amino Acid Transport Systems, Neutral ; CTNS protein, human ; Membrane Transport Proteins ; Nucleoside Transport Proteins ; Organic Anion Transporters ; SLC29A3 protein, human ; Symporters ; sialic acid transport proteins
    Language English
    Publishing date 2020-05-08
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2020.183336
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  3. Article ; Online: Spectrum of

    Morimoto, Marie / Nicoli, Elena-Raluca / Kuptanon, Chulaluck / Roney, Joseph C / Serra-Vinardell, Jenny / Sharma, Prashant / Adams, David R / Gallin, John I / Holland, Steven M / Rosenzweig, Sergio D / Barbot, Jose / Ciccone, Carla / Huizing, Marjan / Toro, Camilo / Gahl, William A / Introne, Wendy J / Malicdan, May Christine V

    Journal of medical genetics

    2024  Volume 61, Issue 3, Page(s) 212–223

    Abstract: Introduction: Chediak-Higashi syndrome (CHS) is a rare autosomal recessive disorder characterised by partial oculocutaneous albinism, a bleeding diathesis, immunological dysfunction and neurological impairment. Bi-allelic loss-of-function variants in !## ...

    Abstract Introduction: Chediak-Higashi syndrome (CHS) is a rare autosomal recessive disorder characterised by partial oculocutaneous albinism, a bleeding diathesis, immunological dysfunction and neurological impairment. Bi-allelic loss-of-function variants in
    Methods: To further our understanding of the pathogenesis of CHS, we conducted clinical evaluations on individuals with CHS enrolled in our natural history study. Using genomic DNA Sanger sequencing, we identified novel pathogenic
    Results: Our investigation unveiled 11 novel pathogenic
    Conclusion: The identification of novel pathogenic
    MeSH term(s) Humans ; Chediak-Higashi Syndrome/genetics ; Chediak-Higashi Syndrome/diagnosis ; Chediak-Higashi Syndrome/pathology ; Mutation ; Proteins/genetics ; Mutation, Missense ; Base Sequence ; Vesicular Transport Proteins/genetics
    Chemical Substances Proteins ; LYST protein, human ; Vesicular Transport Proteins
    Language English
    Publishing date 2024-02-21
    Publishing country England
    Document type Review ; Journal Article
    ZDB-ID 220881-7
    ISSN 1468-6244 ; 0022-2593
    ISSN (online) 1468-6244
    ISSN 0022-2593
    DOI 10.1136/jmg-2023-109420
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  4. Article ; Online: Population Pharmacokinetic Model of N-acetylmannosamine (ManNAc) and N-acetylneuraminic acid (Neu5Ac) in Subjects with GNE Myopathy.

    Van Wart, Scott / Mager, Donald E / Bednasz, Cindy J / Huizing, Marjan / Carrillo, Nuria

    Drugs in R&D

    2021  Volume 21, Issue 2, Page(s) 189–202

    Abstract: Background: GNE myopathy is a rare genetic muscle disease resulting from deficiency in an enzyme critical for the biosynthesis of N-acetylneuraminic acid (Neu5Ac, sialic acid). The uncharged Neu5Ac precursor, N-acetylmannosamine (ManNAc), is under ... ...

    Abstract Background: GNE myopathy is a rare genetic muscle disease resulting from deficiency in an enzyme critical for the biosynthesis of N-acetylneuraminic acid (Neu5Ac, sialic acid). The uncharged Neu5Ac precursor, N-acetylmannosamine (ManNAc), is under development as an orphan drug for treating GNE myopathy.
    Methods: A semi-mechanistic population pharmacokinetic model was developed to simultaneously characterize plasma ManNAc and its metabolite Neu5Ac following oral administration of ManNAc to subjects with GNE myopathy. Plasma ManNAc and Neu5Ac pharmacokinetic data were obtained from two clinical studies (ClinicalTrials.gov identifiers NCT01634750, NCT02346461) and were simultaneously modeled using NONMEM.
    Results: ManNAc and Neu5Ac plasma concentrations were obtained from 34 subjects with GNE myopathy (16 male, 18 female, median age 39.5 years). The model parameter estimates included oral absorption rate (k
    Conclusions: This population pharmacokinetic model can be used to evaluate ManNAc dosing regimens and to calculate Neu5Ac production and exposure following oral administration of ManNAc in subjects with GNE myopathy.
    MeSH term(s) Adult ; Distal Myopathies ; Female ; Hexosamines ; Humans ; Male ; Muscular Diseases ; N-Acetylneuraminic Acid
    Chemical Substances Hexosamines ; N-Acetylneuraminic Acid (GZP2782OP0) ; N-acetylmannosamine (X80PR7P73R)
    Language English
    Publishing date 2021-04-24
    Publishing country New Zealand
    Document type Journal Article
    ZDB-ID 2020476-0
    ISSN 1179-6901 ; 1174-5886
    ISSN (online) 1179-6901
    ISSN 1174-5886
    DOI 10.1007/s40268-021-00343-6
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  5. Article ; Online: Elevated plasma free sialic acid levels in individuals with reduced glomerular filtration rates.

    Fuentes, Federico / Carrillo, Nuria / Wilkins, Kenneth J / Blake, Jodi / Leoyklang, Petcharat / Gahl, William A / Kopp, Jeffrey B / Huizing, Marjan

    Kidney360

    2021  Volume 1, Issue 9, Page(s) 957–961

    MeSH term(s) Glomerular Filtration Rate ; Hexosamines ; Humans ; N-Acetylneuraminic Acid ; Renal Insufficiency
    Chemical Substances Hexosamines ; N-Acetylneuraminic Acid (GZP2782OP0)
    Language English
    Publishing date 2021-05-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ISSN 2641-7650
    ISSN (online) 2641-7650
    DOI 10.34067/kid.0002122020
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  6. Article ; Online: GNE Myopathy: Etiology, Diagnosis, and Therapeutic Challenges.

    Carrillo, Nuria / Malicdan, May C / Huizing, Marjan

    Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics

    2018  Volume 15, Issue 4, Page(s) 900–914

    Abstract: GNE myopathy, previously known as hereditary inclusion body myopathy (HIBM), or Nonaka myopathy, is a rare autosomal recessive muscle disease characterized by progressive skeletal muscle atrophy. It has an estimated prevalence of 1 to 9:1,000,000. GNE ... ...

    Abstract GNE myopathy, previously known as hereditary inclusion body myopathy (HIBM), or Nonaka myopathy, is a rare autosomal recessive muscle disease characterized by progressive skeletal muscle atrophy. It has an estimated prevalence of 1 to 9:1,000,000. GNE myopathy is caused by mutations in the GNE gene which encodes the rate-limiting enzyme of sialic acid biosynthesis. The pathophysiology of the disease is not entirely understood, but hyposialylation of muscle glycans is thought to play an essential role. The typical presentation is bilateral foot drop caused by weakness of the anterior tibialis muscles with onset in early adulthood. The disease slowly progresses over the next decades to involve skeletal muscles throughout the body, with relative sparing of the quadriceps until late stages of the disease. The diagnosis of GNE myopathy should be considered in young adults presenting with bilateral foot drop. Histopathologic findings on muscle biopsies include fiber size variation, atrophic fibers, lack of inflammation, and the characteristic "rimmed" vacuoles on modified Gomori trichome staining. The diagnosis is confirmed by the presence of pathogenic (mostly missense) mutations in both alleles of the GNE gene. Although there is no approved therapy for this disease, preclinical and clinical studies of several potential therapies are underway, including substrate replacement and gene therapy-based strategies. However, developing therapies for GNE myopathy is complicated by several factors, including the rare incidence of disease, limited preclinical models, lack of reliable biomarkers, and slow disease progression.
    MeSH term(s) Animals ; Humans ; Magnetic Resonance Imaging ; Multienzyme Complexes/genetics ; Muscular Diseases/diagnosis ; Muscular Diseases/etiology ; Muscular Diseases/genetics ; Muscular Diseases/therapy ; Mutation/genetics
    Chemical Substances Multienzyme Complexes ; UDP-N-acetylglucosamine 2-epimerase - N-acetylmannosamine kinase
    Language English
    Publishing date 2018-08-31
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 2316693-9
    ISSN 1878-7479 ; 1933-7213
    ISSN (online) 1878-7479
    ISSN 1933-7213
    DOI 10.1007/s13311-018-0671-y
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  7. Article ; Online: Free sialic acid storage disorder: Progress and promise.

    Huizing, Marjan / Hackbarth, Mary E / Adams, David R / Wasserstein, Melissa / Patterson, Marc C / Walkley, Steven U / Gahl, William A

    Neuroscience letters

    2021  Volume 755, Page(s) 135896

    Abstract: Lysosomal free sialic acid storage disorder (FSASD) is an extremely rare, autosomal recessive, neurodegenerative, multisystemic disorder caused by defects in the lysosomal sialic acid membrane exporter SLC17A5 (sialin). SLC17A5 defects cause free sialic ... ...

    Abstract Lysosomal free sialic acid storage disorder (FSASD) is an extremely rare, autosomal recessive, neurodegenerative, multisystemic disorder caused by defects in the lysosomal sialic acid membrane exporter SLC17A5 (sialin). SLC17A5 defects cause free sialic acid and some other acidic hexoses to accumulate in lysosomes, resulting in enlarged lysosomes in some cell types and 10-100-fold increased urinary excretion of free sialic acid. Clinical features of FSASD include coarse facial features, organomegaly, and progressive neurodegenerative symptoms with cognitive impairment, cerebellar ataxia and muscular hypotonia. Central hypomyelination with cerebellar atrophy and thinning of the corpus callosum are also prominent disease features. Around 200 FSASD cases are reported worldwide, with the clinical spectrum ranging from a severe infantile onset form, often lethal in early childhood, to a mild, less severe form with subjects living into adulthood, also called Salla disease. The pathobiology of FSASD remains poorly understood and FSASD is likely underdiagnosed. Known patients have experienced a diagnostic delay due to the rarity of the disorder, absence of routine urine sialic acid testing, and non-specific clinical symptoms, including developmental delay, ataxia and infantile hypomyelination. There is no approved therapy for FSASD. We initiated a multidisciplinary collaborative effort involving worldwide academic clinical and scientific FSASD experts, the National Institutes of Health (USA), and the FSASD patient advocacy group (Salla Treatment and Research [S.T.A.R.] Foundation) to overcome the scientific, clinical and financial challenges facing the development of new treatments for FSASD. We aim to collect data that incentivize industry to further develop, obtain approval for, and commercialize FSASD treatments. This review summarizes current aspects of FSASD diagnosis, prevalence, etiology, and disease models, as well as challenges on the path to therapeutic approaches for FSASD.
    MeSH term(s) Animals ; Genetic Therapy/trends ; Humans ; N-Acetylneuraminic Acid/genetics ; N-Acetylneuraminic Acid/metabolism ; Organic Anion Transporters/genetics ; Organic Anion Transporters/metabolism ; Sialic Acid Storage Disease/diagnostic imaging ; Sialic Acid Storage Disease/genetics ; Sialic Acid Storage Disease/metabolism ; Sialic Acid Storage Disease/therapy ; Stem Cell Transplantation/trends ; Symporters/genetics ; Symporters/metabolism
    Chemical Substances Organic Anion Transporters ; Symporters ; sialic acid transport proteins ; N-Acetylneuraminic Acid (GZP2782OP0)
    Language English
    Publishing date 2021-04-20
    Publishing country Ireland
    Document type Journal Article ; Review
    ZDB-ID 194929-9
    ISSN 1872-7972 ; 0304-3940
    ISSN (online) 1872-7972
    ISSN 0304-3940
    DOI 10.1016/j.neulet.2021.135896
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  8. Article ; Online: Genetic variants associated with Hermansky-Pudlak syndrome.

    Merideth, Melissa A / Introne, Wendy J / Wang, Jennifer A / O'Brien, Kevin J / Huizing, Marjan / Gochuico, Bernadette R

    Platelets

    2019  Volume 31, Issue 4, Page(s) 544–547

    Abstract: Hermansky-Pudlak syndrome (HPS) is a rare autosomal recessive disorder characterized by defective biogenesis of lysosome-related organelles. Clinical manifestations include a bleeding diathesis due to a platelet delta storage pool deficiency, ... ...

    Abstract Hermansky-Pudlak syndrome (HPS) is a rare autosomal recessive disorder characterized by defective biogenesis of lysosome-related organelles. Clinical manifestations include a bleeding diathesis due to a platelet delta storage pool deficiency, oculocutaneous albinism, inflammatory bowel disease, neutropenia, and pulmonary fibrosis. Ten genes associated with HPS are identified to date, and each gene encodes a protein subunit of either Biogenesis of Lysosome-related Organelles Complex (BLOC)-1, BLOC-2, BLOC-3, or the Adaptor Protein-3 complex. Several genetic variants and phenotypic heterogeneities are reported in individuals with HPS, who generally exhibit easy bruisability and increased bleeding. Desmopressin, pro-coagulants, or platelet transfusion may be used as prophylaxis or treatment for excessive bleeding in patients with HPS. However, response to desmopressin can be variable. Platelets are effective in preventing or treating bleeding in individuals with HPS, but platelets should be transfused judiciously to limit alloimmunization in patients with HPS who are at risk of developing pulmonary fibrosis and may be potential candidates for lung transplantation. The discovery of new genes associated with HPS in people with excessive bleeding and hypopigmentation of unknown etiology may be facilitated by the use of next-generation sequencing or panel-based genetic testing.
    MeSH term(s) Aminocaproic Acid/pharmacology ; Antifibrinolytic Agents/pharmacology ; Blood Platelets/metabolism ; Blood Platelets/ultrastructure ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Contusions/genetics ; Deamino Arginine Vasopressin/therapeutic use ; Hemorrhage/genetics ; Hermanski-Pudlak Syndrome/drug therapy ; Hermanski-Pudlak Syndrome/genetics ; Hermanski-Pudlak Syndrome/physiopathology ; Humans ; Hypopigmentation/genetics ; Lysosomes/genetics ; Lysosomes/metabolism ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Proteins/genetics ; Proteins/metabolism ; Tranexamic Acid/pharmacology
    Chemical Substances Antifibrinolytic Agents ; BLOC1S1 protein, human ; BLOC1S2 protein, human ; BLOC1S3 protein, human ; Carrier Proteins ; Nerve Tissue Proteins ; Proteins ; Tranexamic Acid (6T84R30KC1) ; Deamino Arginine Vasopressin (ENR1LLB0FP) ; Aminocaproic Acid (U6F3787206)
    Language English
    Publishing date 2019-09-05
    Publishing country England
    Document type Journal Article
    ZDB-ID 1034283-7
    ISSN 1369-1635 ; 0953-7104
    ISSN (online) 1369-1635
    ISSN 0953-7104
    DOI 10.1080/09537104.2019.1663810
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    Zs.A 2888: Show issues Location:
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  9. Article ; Online: The BEACH is hot: a LYST of emerging roles for BEACH-domain containing proteins in human disease.

    Cullinane, Andrew R / Schäffer, Alejandro A / Huizing, Marjan

    Traffic (Copenhagen, Denmark)

    2013  Volume 14, Issue 7, Page(s) 749–766

    Abstract: BEACH (named after 'Beige and Chediak-Higashi') is a conserved ∼280 residue domain, present in nine human BEACH domain containing proteins (BDCPs). Most BDCPs are large, containing a PH-like domain for membrane association preceding their BEACH domain, ... ...

    Abstract BEACH (named after 'Beige and Chediak-Higashi') is a conserved ∼280 residue domain, present in nine human BEACH domain containing proteins (BDCPs). Most BDCPs are large, containing a PH-like domain for membrane association preceding their BEACH domain, and containing WD40 and other domains for ligand binding. Recent studies found that mutations in individual BDCPs cause several human diseases. BDCP alterations affect lysosome size (LYST and NSMAF), apoptosis (NSMAF), autophagy (LYST, WDFY3, LRBA), granule size (LYST, NBEAL2, NBEA) or synapse formation (NBEA). However, the roles of each BDCP in these membrane events remain controversial. After reviewing studies on individual BDCPs, we propose a unifying hypothesis that BDCPs act as scaffolding proteins that facilitate membrane events, including both fission and fusion, determined by their binding partners. BDCPs may also bind each other, enabling fusion or fission of vesicles that are not necessarily of the same type. Such mechanisms explain why different BDCPs may have roles in autophagy; each BDCP is specific for the cell type or the cargo, but not necessarily specific for attaching to the autophagosome. Further elucidation of these mechanisms, preferably carrying out the same experiment on multiple BDCPs, and possibly using patients' cells, may identify potential targets for therapy.
    MeSH term(s) Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Adaptor Proteins, Vesicular Transport/chemistry ; Adaptor Proteins, Vesicular Transport/genetics ; Adaptor Proteins, Vesicular Transport/metabolism ; Amino Acid Sequence ; Animals ; Chediak-Higashi Syndrome/genetics ; Disease/genetics ; Humans ; Lysosomes/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Polymorphism, Single Nucleotide ; Protein Structure, Tertiary/genetics
    Chemical Substances Adaptor Proteins, Signal Transducing ; Adaptor Proteins, Vesicular Transport ; Membrane Proteins
    Language English
    Publishing date 2013-04-24
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1111/tra.12069
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  10. Article: Hereditary inclusion body myopathy: a decade of progress.

    Huizing, Marjan / Krasnewich, Donna M

    Biochimica et biophysica acta

    2009  Volume 1792, Issue 9, Page(s) 881–887

    Abstract: Hereditary Inclusion Body Myopathy (HIBM) is an autosomal recessive, quadriceps sparing type commonly referred to as HIBM but also termed h-IBM or Inclusion Body Myopathy 2 (IBM2). The clinical manifestations begin with muscle weakness progressing over ... ...

    Abstract Hereditary Inclusion Body Myopathy (HIBM) is an autosomal recessive, quadriceps sparing type commonly referred to as HIBM but also termed h-IBM or Inclusion Body Myopathy 2 (IBM2). The clinical manifestations begin with muscle weakness progressing over the next 10-20 years uniquely sparing the quadriceps until the most advanced stage of the disease. Histopathology of an HIBM muscle biopsy shows rimmed vacuoles on Gomori's trichrome stain, small fibers in groups and tubulofilaments without evidence of inflammation. In affected individuals distinct mutations have been identified in the GNE gene, which encodes the bifunctional enzyme uridine diphospho-N-acetylglucosamine (UDP-GlcNAc) 2-epimerase/N-acetyl-mannosamine (ManNAc) kinase (GNE/MNK). GNE/MNK catalyzes the first two committed steps in the biosynthesis of acetylneuraminic acid (Neu5Ac), an abundant and functionally important sugar. The generation of HIBM animal models has led to novel insights into both the disease and the role of GNE/MNK in pathophysiology. Recent advances in therapeutic approaches for HIBM, including administration of N-acetyl-mannosamine (ManNAc), a precursor of Neu5Ac will be discussed.
    MeSH term(s) Animals ; Disease Models, Animal ; Humans ; Mice ; Multienzyme Complexes/genetics ; Muscle, Skeletal/pathology ; Mutation, Missense ; Myositis, Inclusion Body/genetics ; Myositis, Inclusion Body/pathology ; N-Acetylneuraminic Acid/metabolism
    Chemical Substances Multienzyme Complexes ; UDP-N-acetylglucosamine 2-epimerase - N-acetylmannosamine kinase ; N-Acetylneuraminic Acid (GZP2782OP0)
    Language English
    Publishing date 2009-07-24
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 60-7
    ISSN 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbadis.2009.07.001
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