The effects of the inactivation of Hydroxyproline dehydrogenase on urinary oxalate and glycolate excretion in mouse models of primary hyperoxaluria
The major clinical manifestation of the Primary Hyperoxalurias (PH) is increased production of oxalate, as a consequence of genetic mutations that lead to aberrant glyoxylate and hydroxyproline metabolism. Hyperoxaluria can lead to the formation of calcium-oxalate kidney stones, nephrocalcinosis and...
Saved in:
Published in | Biochimica et biophysica acta. Molecular basis of disease Vol. 1866; no. 3; p. 165633 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.03.2020
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | The major clinical manifestation of the Primary Hyperoxalurias (PH) is increased production of oxalate, as a consequence of genetic mutations that lead to aberrant glyoxylate and hydroxyproline metabolism. Hyperoxaluria can lead to the formation of calcium-oxalate kidney stones, nephrocalcinosis and renal failure. Current therapeutic approaches rely on organ transplants and more recently modifying the pathway of oxalate synthesis using siRNA therapy. We have recently reported that the metabolism of trans-4-hydroxy-L-proline (Hyp), an amino acid derived predominantly from collagen metabolism, is a significant source of oxalate production in individuals with PH2 and PH3. Thus, the first enzyme in the Hyp degradation pathway, hydroxyproline dehydrogenase (HYPDH), represents a promising therapeutic target for reducing endogenous oxalate production in these individuals. This is supported by the observation that individuals with inherited mutations in HYPDH (PRODH2 gene) have no pathological consequences. The creation of mouse models that do not express HYPDH will facilitate research evaluating HYPDH as a target. We describe the phenotype of the Prodh2 knock out mouse model and show that the lack of HYPDH in PH mouse models results in lower levels of urinary oxalate excretion, consistent with our previous metabolic tracer and siRNA-based knockdown studies. The double knockout mouse, Grhpr KO (PH2 model) and Prodh2 KO, prevented calcium-oxalate crystal deposition in the kidney, when placed on a 1% Hyp diet. These observations support the use of the Grhpr KO mice to screen HYPDH inhibitors in vivo. Altogether these data support HYPDH as an attractive therapeutic target for PH2 and PH3 patients.
[Display omitted]
•Hydroxproline metabolism contributes to oxalate production.•Hydroxyproline dehydrogenase (HYPDH) is a target for treating primary hyperoxaluria.•Deletion of HYPDH in mice increases hydroxyproline in urine and plasma.•Urine oxalate and glycolate levels can be lowered by deletion of HYPDH.•Loss of HYPDH can protect GRHPR KO mice from calcium oxalate crystal formation. |
---|---|
AbstractList | The major clinical manifestation of the Primary Hyperoxalurias (PH) is increased production of oxalate, as a consequence of genetic mutations that lead to aberrant glyoxylate and hydroxyproline metabolism. Hyperoxaluria can lead to the formation of calcium-oxalate kidney stones, nephrocalcinosis and renal failure. Current therapeutic approaches rely on organ transplants and more recently modifying the pathway of oxalate synthesis using siRNA therapy. We have recently reported that the metabolism of trans-4-hydroxy-L-proline (Hyp), an amino acid derived predominantly from collagen metabolism, is a significant source of oxalate production in individuals with PH2 and PH3. Thus, the first enzyme in the Hyp degradation pathway, hydroxyproline dehydrogenase (HYPDH), represents a promising therapeutic target for reducing endogenous oxalate production in these individuals. This is supported by the observation that individuals with inherited mutations in HYPDH (PRODH2 gene) have no pathological consequences. The creation of mouse models that do not express HYPDH will facilitate research evaluating HYPDH as a target. We describe the phenotype of the Prodh2 knock out mouse model and show that the lack of HYPDH in PH mouse models results in lower levels of urinary oxalate excretion, consistent with our previous metabolic tracer and siRNA-based knockdown studies. The double knockout mouse, Grhpr KO (PH2 model) and Prodh2 KO, prevented calcium-oxalate crystal deposition in the kidney, when placed on a 1% Hyp diet. These observations support the use of the Grhpr KO mice to screen HYPDH inhibitors in vivo. Altogether these data support HYPDH as an attractive therapeutic target for PH2 and PH3 patients.
[Display omitted]
•Hydroxproline metabolism contributes to oxalate production.•Hydroxyproline dehydrogenase (HYPDH) is a target for treating primary hyperoxaluria.•Deletion of HYPDH in mice increases hydroxyproline in urine and plasma.•Urine oxalate and glycolate levels can be lowered by deletion of HYPDH.•Loss of HYPDH can protect GRHPR KO mice from calcium oxalate crystal formation. The major clinical manifestation of the Primary Hyperoxalurias (PH) is increased production of oxalate, as a consequence of genetic mutations that lead to aberrant glyoxylate and hydroxyproline metabolism. Hyperoxaluria can lead to the formation of calcium-oxalate kidney stones, nephrocalcinosis and renal failure. Current therapeutic approaches rely on organ transplants and more recently modifying the pathway of oxalate synthesis using siRNA therapy. We have recently reported that the metabolism of trans-4-hydroxy-L-proline (Hyp), an amino acid derived predominantly from collagen metabolism, is a significant source of oxalate production in individuals with PH2 and PH3. Thus, the first enzyme in the Hyp degradation pathway, hydroxyproline dehydrogenase (HYPDH), represents a promising therapeutic target for reducing endogenous oxalate production in these individuals. This is supported by the observation that individuals with inherited mutations in HYPDH (PRODH2 gene) have no pathological consequences. The creation of mouse models that do not express HYPDH will facilitate research evaluating HYPDH as a target. We describe the phenotype of the Prodh2 knock out mouse model and show that the lack of HYPDH in PH mouse models results in lower levels of urinary oxalate excretion, consistent with our previous metabolic tracer and siRNA-based knockdown studies. The double knockout mouse, Grhpr KO (PH2 model) and Prodh2 KO, prevented calcium-oxalate crystal deposition in the kidney, when placed on a 1% Hyp diet. These observations support the use of the Grhpr KO mice to screen HYPDH inhibitors in vivo. Altogether these data support HYPDH as an attractive therapeutic target for PH2 and PH3 patients. The major clinical manifestation of the Primary Hyperoxalurias (PH) is increased production of oxalate, as a consequence of genetic mutations that lead to aberrant glyoxylate and hydroxyproline metabolism. Hyperoxaluria can lead to the formation of calcium-oxalate kidney stones, nephrocalcinosis and renal failure. Current therapeutic approaches rely on organ transplants and more recently modifying the pathway of oxalate synthesis using siRNA therapy. We have recently reported that the metabolism of trans-4-hydroxy-L-proline (Hyp), an amino acid derived predominantly from collagen metabolism, is a significant source of oxalate production in individuals with PH2 and PH3. Thus, the first enzyme in the Hyp degradation pathway, hydroxyproline dehydrogenase (HYPDH), represents a promising therapeutic target for reducing endogenous oxalate production in these individuals. This is supported by the observation that individuals with inherited mutations in HYPDH ( PRODH2 gene) have no pathological consequences. The creation of mouse models that do not express HYPDH will facilitate research evaluating HYPDH as a target. We describe the phenotype of the Prodh2 knock out mouse model and show that the lack of HYPDH in PH mouse models results in lower levels of urinary oxalate excretion, consistent with our previous metabolic tracer and siRNA-based knockdown studies. The double knockout mouse, Grhpr KO (PH2 model) and Prodh2 KO, prevented calcium-oxalate crystal deposition in the kidney, when placed on a 1% Hyp diet. These observations support the use of the Grhpr KO mice to screen HYPDH inhibitors in vivo . Altogether these data support HYPDH as an attractive therapeutic target for PH2 and PH3 patients. |
ArticleNumber | 165633 |
Author | Fargue, Sonia Challa, Anil Buchalski, Brianna Lowther, W. Todd Holmes, Ross P. Wood, Kyle D. Knight, John |
AuthorAffiliation | a Department of Urology, University of Alabama at Birmingham, 720 20 th Street South, Birmingham, AL, 35294 c Department of Biochemistry, Center for Structural Biology, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157 b Department of Genetics, University of Alabama at Birmingham, 720 20 th Street South, Birmingham, AL, 35294 |
AuthorAffiliation_xml | – name: a Department of Urology, University of Alabama at Birmingham, 720 20 th Street South, Birmingham, AL, 35294 – name: c Department of Biochemistry, Center for Structural Biology, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157 – name: b Department of Genetics, University of Alabama at Birmingham, 720 20 th Street South, Birmingham, AL, 35294 |
Author_xml | – sequence: 1 givenname: Brianna surname: Buchalski fullname: Buchalski, Brianna organization: Department of Urology, University of Alabama at Birmingham, 720 20th Street South, Birmingham, AL, 35294, United States of America – sequence: 2 givenname: Kyle D. surname: Wood fullname: Wood, Kyle D. organization: Department of Urology, University of Alabama at Birmingham, 720 20th Street South, Birmingham, AL, 35294, United States of America – sequence: 3 givenname: Anil surname: Challa fullname: Challa, Anil organization: Department of Genetics, University of Alabama at Birmingham, 720 20th Street South, Birmingham, AL 35294, United States of America – sequence: 4 givenname: Sonia surname: Fargue fullname: Fargue, Sonia organization: Department of Urology, University of Alabama at Birmingham, 720 20th Street South, Birmingham, AL, 35294, United States of America – sequence: 5 givenname: Ross P. surname: Holmes fullname: Holmes, Ross P. organization: Department of Urology, University of Alabama at Birmingham, 720 20th Street South, Birmingham, AL, 35294, United States of America – sequence: 6 givenname: W. Todd surname: Lowther fullname: Lowther, W. Todd email: tlowther@wakehealth.edu organization: Department of Biochemistry, Center for Structural Biology, Wake Forest School of Medicine, Medical Center Blvd., Winston-Salem, NC 27157, United States of America – sequence: 7 givenname: John surname: Knight fullname: Knight, John email: johnknight@uabmc.edu organization: Department of Urology, University of Alabama at Birmingham, 720 20th Street South, Birmingham, AL, 35294, United States of America |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31821850$$D View this record in MEDLINE/PubMed |
BookMark | eNp9kc9uGyEQxlHlqHb-vEFV8QLrwrJm4VKpspqkUqRcXCk3xMKsjbUGC9aW9zn6wmXtNG0u5YJmmN83M3zXaOKDB4Q-UTKnhPIv23nTaOvSvCRUzilfcMY-oBkVtSxKTl4maEZkuSiqiskpuk5pS_LhNfmIpoyKkooFmaFfqw1gaFswfcKhxX0Ondemd0fdu-DH3ONgYzgN-xg65wFb2IyJNXidAOeSQ8xEHHA46U73gLW3eN0NJpwjOJkIZynn8S4cMrMLFrpzu310uxHdDHuII5-19C26anWX4O71vkE_77-vlo_F0_PDj-W3p8JUnPUF5C1oRXipW9FoybgWrWyAyNpKyiy3jLCKEUJzHWkMF0LUjZStaZisFlawG_T1ors_NDuwBnwfdadeZ1JBO_X-xbuNWoejqklVSzYKVBcBE0NKEdo3lhI1mqS26mKSGk1SF5My9vnfvm_QH1f-DpZ_CY4OokrGgTdgXcxGKRvc_zv8BurEq8Y |
CitedBy_id | crossref_primary_10_3390_jpm11020074 crossref_primary_10_2139_ssrn_4017356 crossref_primary_10_1016_j_ejmech_2022_114396 crossref_primary_10_1038_s41392_023_01311_z crossref_primary_10_1016_j_bbadis_2023_166848 crossref_primary_10_1111_febs_16164 crossref_primary_10_1016_j_heliyon_2022_e09232 crossref_primary_10_1016_j_bbrep_2021_101138 crossref_primary_10_3390_ijms23021005 crossref_primary_10_1007_s00467_020_04817_8 crossref_primary_10_1097_MNH_0000000000000987 |
Cites_doi | 10.1152/ajprenal.00473.2011 10.1016/j.ajhg.2010.07.023 10.1016/j.bbadis.2012.06.014 10.1038/ki.2009.32 10.1681/ASN.2017040390 10.1038/nprot.2013.143 10.1016/j.bbadis.2016.02.004 10.1042/BJ20051397 10.1146/annurev.bi.49.070180.005041 10.1681/ASN.2014070698 10.1073/pnas.0607218103 10.2215/CJN.02810315 10.1042/BJ20141159 10.1007/s10545-016-9940-2 10.1038/sj.ki.5001699 10.1371/journal.pone.0069152 10.1007/s00240-016-0868-7 10.1152/ajpgi.00331.2011 10.1155/2012/819202 10.1046/j.1523-1755.2002.00468.x 10.1074/jbc.M702181200 10.1007/s00109-012-0930-z 10.1371/journal.pone.0155812 10.1016/j.bbadis.2015.12.001 10.1007/s11010-006-9276-6 10.1177/0004563216677101 10.1681/ASN.2016030338 10.1016/j.ymthe.2018.05.016 |
ContentType | Journal Article |
Copyright | 2019 Elsevier B.V. Copyright © 2019 Elsevier B.V. All rights reserved. |
Copyright_xml | – notice: 2019 Elsevier B.V. – notice: Copyright © 2019 Elsevier B.V. All rights reserved. |
DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 5PM |
DOI | 10.1016/j.bbadis.2019.165633 |
DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef |
DatabaseTitleList | MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Chemistry Biology |
EISSN | 1879-260X |
EndPage | 165633 |
ExternalDocumentID | 10_1016_j_bbadis_2019_165633 31821850 S0925443919303618 |
Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NIDDK NIH HHS grantid: R01 DK054468 – fundername: NIDDK NIH HHS grantid: R01 DK083527 – fundername: NIDDK NIH HHS grantid: K08 DK115833 – fundername: NIDDK NIH HHS grantid: K01 DK114332 – fundername: NCI NIH HHS grantid: P30 CA012197 – fundername: NIDDK NIH HHS grantid: P60 DK079626 – fundername: NIAMS NIH HHS grantid: P30 AR048311 – fundername: NIDDK NIH HHS grantid: P30 DK074038 – fundername: NCI NIH HHS grantid: P30 CA013148 |
GroupedDBID | --- --K --M .~1 0R~ 1B1 1RT 1~. 1~5 23N 4.4 457 4G. 53G 5GY 5RE 5VS 7-5 71M 8P~ 9JM AACTN AAEDT AAEDW AAFTH AAIAV AAIKJ AAKOC AALRI AAOAW AAQFI AAXUO ABBQC ABGSF ABLVK ABMAC ABMZM ABUDA ABVKL ABYKQ ACDAQ ACIUM ACRLP ADBBV ADEZE ADUVX AEBSH AEHWI AEKER AEXQZ AFKWA AFTJW AFXIZ AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJOXV AJRQY ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ANZVX AXJTR BKOJK BLXMC BNPGV CS3 DOVZS EBS EFJIC EFLBG EO8 EO9 EP2 EP3 FDB FIRID FNPLU FYGXN G-Q GBLVA IXB J1W KOM LCYCR LX3 M41 MO0 N9A O-L O9- OAUVE OK1 OZT P-8 P-9 PC. Q38 ROL RPZ SDF SDG SDP SES SPCBC SSH SSU SSZ T5K ~G- 0SF AAXKI ADVLN CGR CUY CVF ECM EIF NPM 3O- 6I. AAQXK AAYXX ABEFU ABFNM ABXDB ADMUD AFJKZ AGHFR ASPBG AVWKF AZFZN CITATION EJD FEDTE FGOYB G-2 HLW HVGLF HZ~ IHE NCXOZ R2- SBG SEW UQL WUQ XJT XPP 5PM |
ID | FETCH-LOGICAL-c463t-e31814062af8ba936a8f9be097d913d6d303430013180bc68887b99fcb3945d83 |
IEDL.DBID | AIKHN |
ISSN | 0925-4439 |
IngestDate | Tue Sep 17 21:04:11 EDT 2024 Thu Sep 26 18:49:41 EDT 2024 Wed Oct 16 00:39:30 EDT 2024 Tue Feb 20 19:34:12 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 3 |
Keywords | Primary hyperoxaluria Hydroxyproline metabolism Glycolate Oxalate Mouse models Kidney stone |
Language | English |
License | Copyright © 2019 Elsevier B.V. All rights reserved. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c463t-e31814062af8ba936a8f9be097d913d6d303430013180bc68887b99fcb3945d83 |
Notes | A. Challa: Investigation, Methodology, Writing – original draft, Writing – Review & editing. CRediT authorship contribution statement W.T. Lowther: Conceptualization, Methodology, Formal analysis, Funding Acquisition, Project Administration, Writing – original draft, Writing – Review & editing. Contributed equally to this work. B. Buchalski: Investigation, Methodology, Data curation, Formal analysis, Writing – original draft, Writing – Review & editing. KD. Wood: Investigation, Methodology, Data curation, Formal analysis, Writing – original draft, Writing – Review & editing. S. Fargue: Investigation, Methodology, Data curation, Formal analysis, Writing – original draft, Writing – Review & editing. R.P. Holmes: Conceptualization, Methodology, Formal analysis, Funding Acquisition, Project Administration, Writing – original draft, Writing – Review & editing. J. Knight: Conceptualization, Methodology, Formal analysis, Funding Acquisition, Project Administration, Writing – original draft, Writing – Review & editing. |
OpenAccessLink | https://doi.org/10.1016/j.bbadis.2019.165633 |
PMID | 31821850 |
PageCount | 1 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_7047938 crossref_primary_10_1016_j_bbadis_2019_165633 pubmed_primary_31821850 elsevier_sciencedirect_doi_10_1016_j_bbadis_2019_165633 |
PublicationCentury | 2000 |
PublicationDate | 2020-03-01 |
PublicationDateYYYYMMDD | 2020-03-01 |
PublicationDate_xml | – month: 03 year: 2020 text: 2020-03-01 day: 01 |
PublicationDecade | 2020 |
PublicationPlace | Netherlands |
PublicationPlace_xml | – name: Netherlands |
PublicationTitle | Biochimica et biophysica acta. Molecular basis of disease |
PublicationTitleAlternate | Biochim Biophys Acta Mol Basis Dis |
PublicationYear | 2020 |
Publisher | Elsevier B.V |
Publisher_xml | – name: Elsevier B.V |
References | Huang, Martinez-Del Campo, Balskus (bb0170) 2018; 9 M’Dimegh, Aquaviva-Bourdain, Omezzine, Souche, M’Barek, Abidi, Gargah, Abroug, Bouslama (bb0120) 2017; 31 Belostotsky, Seboun, Idelson, Milliner, Becker-Cohen, Rinat, Monico, Feinstein, Ben-Shalom, Magen, Weissman, Charon, Frishberg (bb0100) 2010; 87 Fargue, Milliner, Knight, Olson, Lowther, Holmes (bb0015) 2018; 29 Pitt, Willis, Tzanakos, Belostotsky, Frishberg (bb0130) 2015; 15 Li, Knight, Lowther, Holmes (bb0065) 2015; 1852 Cooper, Pandhare, Donald, Phang (bb0035) 2008; 283 Raimondi, Ciribilli, Monti, Bisio, Pollegioni, Fronza, Inga, Campomenosi (bb0040) 2013; 8 Staufner, Haack, Feyh, Gramer, Raga, Terrile, Sauer, Okun, Fang-Hoffmann, Mayatepek, Prokisch, Hoffmann, Kolker (bb0050) 2016; 39 Hoppe, Beck, Milliner (bb0105) 2009; 75 Richard, Blouin, Harambat, Llanas, Bouchet, Acquaviva, de la Faille (bb0115) 2017; 54 Hopp, Cogal, Bergstralh, Seide, Olson, Meek, Lieske, Milliner, Harris (bb0125) 2015; 26 Adams, Frank (bb0010) 1980; 49 Lange, Wood, Knight, Assimos, Holmes (bb0145) 2012; 2012 Knight, Madduma-Liyanage, Mobley, Assimos, Holmes (bb0155) 2016; 44 Fargue, Knight, Holmes, Rumsby, Danpure (bb0080) 2016; 1862 Jiang, Johnson, Knight, Callahan, Riedel, Holmes, Lowther (bb0085) 2012; 302 Hu, Donald, Yu, Lin, Liu, Steel, Obie, Valle, Phang (bb0045) 2007; 295 E.L. Williams, D. Bockenhauer, W.G. van't Hoff, N. Johri, C. Laing, M.D. Sinha, R. Unwin, A. Viljoen, G. Rumsby, The enzyme 4-hydroxy-2-oxoglutarate aldolase is deficient in primary hyperoxaluria type 3, Nephrol Dial Transplant, 27 (2012) 3191–3195. Challa, Boitet, Turner, Johnson, Kennedy, Downs, Hymel, Gross, Kesterson (bb0075) 2016; 11 Liebow, Li, Racie, Hettinger, Bettencourt, Najafian, Haslett, Fitzgerald, Holmes, Erbe, Querbes, Knight (bb0160) 2017; 28 Phang, Hu, Valle (bb0005) 2001 Li, Knight, Fargue, Buchalski, Guan, Inscho, Liebow, Fitzgerald, Querbes, Lowther, Holmes (bb0140) 2016; 1862 Lai, Pursell, Gierut, Saxena, Zhou, Dills, Diwanji, Dutta, Koser, Nazef, Storr, Kim, Martin-Higueras, Salido, Wang, Abrams, Dudek, Brown (bb0165) 2018; 26 Belostotsky, Pitt, Frishberg (bb0020) 2012; 90 Ran, Hsu, Wright, Agarwala, Scott, Zhang (bb0070) 2013; 8 Knight, Holmes, Cramer, Takayama, Salido (bb0060) 2012; 302 Monico, Persson, Ford, Rumsby, Milliner (bb0110) 2002; 62 Behnam, Williams, Brink, Rumsby, Danpure (bb0090) 2006; 394 Zhao, Bergstralh, Mehta, Vaughan, Olson, Seide, Meek, Cogal, Lieske, Milliner (bb9000) 2016 Khan, Glenton, Byer (bb0095) 2006; 70 Knight, Hinsdale, Holmes (bb0150) 2012; 421 Riedel, Knight, Murray, Milliner, Holmes, Lowther (bb0025) 2012; 1822 Summitt, Johnson, Jonsson, Parsonage, Holmes, Lowther (bb0030) 2015; 466 Salido, Li, Lu, Wang, Santana, Roy-Chowdhury, Torres, Shapiro, Roy-Chowdhury (bb0055) 2006; 103 32073946 - J Urol. 2020 May;203(5):876 Khan (10.1016/j.bbadis.2019.165633_bb0095) 2006; 70 Zhao (10.1016/j.bbadis.2019.165633_bb9000) 2016 Belostotsky (10.1016/j.bbadis.2019.165633_bb0100) 2010; 87 Pitt (10.1016/j.bbadis.2019.165633_bb0130) 2015; 15 Hu (10.1016/j.bbadis.2019.165633_bb0045) 2007; 295 Staufner (10.1016/j.bbadis.2019.165633_bb0050) 2016; 39 Knight (10.1016/j.bbadis.2019.165633_bb0155) 2016; 44 Jiang (10.1016/j.bbadis.2019.165633_bb0085) 2012; 302 Knight (10.1016/j.bbadis.2019.165633_bb0150) 2012; 421 Adams (10.1016/j.bbadis.2019.165633_bb0010) 1980; 49 Fargue (10.1016/j.bbadis.2019.165633_bb0015) 2018; 29 Fargue (10.1016/j.bbadis.2019.165633_bb0080) 2016; 1862 Challa (10.1016/j.bbadis.2019.165633_bb0075) 2016; 11 10.1016/j.bbadis.2019.165633_bb0135 Raimondi (10.1016/j.bbadis.2019.165633_bb0040) 2013; 8 Summitt (10.1016/j.bbadis.2019.165633_bb0030) 2015; 466 Salido (10.1016/j.bbadis.2019.165633_bb0055) 2006; 103 Monico (10.1016/j.bbadis.2019.165633_bb0110) 2002; 62 Hopp (10.1016/j.bbadis.2019.165633_bb0125) 2015; 26 Liebow (10.1016/j.bbadis.2019.165633_bb0160) 2017; 28 Huang (10.1016/j.bbadis.2019.165633_bb0170) 2018; 9 Li (10.1016/j.bbadis.2019.165633_bb0065) 2015; 1852 Lai (10.1016/j.bbadis.2019.165633_bb0165) 2018; 26 Phang (10.1016/j.bbadis.2019.165633_bb0005) 2001 Belostotsky (10.1016/j.bbadis.2019.165633_bb0020) 2012; 90 Riedel (10.1016/j.bbadis.2019.165633_bb0025) 2012; 1822 Hoppe (10.1016/j.bbadis.2019.165633_bb0105) 2009; 75 M’Dimegh (10.1016/j.bbadis.2019.165633_bb0120) 2017; 31 Ran (10.1016/j.bbadis.2019.165633_bb0070) 2013; 8 Li (10.1016/j.bbadis.2019.165633_bb0140) 2016; 1862 Behnam (10.1016/j.bbadis.2019.165633_bb0090) 2006; 394 Knight (10.1016/j.bbadis.2019.165633_bb0060) 2012; 302 Cooper (10.1016/j.bbadis.2019.165633_bb0035) 2008; 283 Richard (10.1016/j.bbadis.2019.165633_bb0115) 2017; 54 Lange (10.1016/j.bbadis.2019.165633_bb0145) 2012; 2012 |
References_xml | – volume: 2012 start-page: 819202 year: 2012 ident: bb0145 article-title: Glyoxal formation and its role in endogenous oxalate synthesis publication-title: Adv Urol contributor: fullname: Holmes – volume: 11 year: 2016 ident: bb0075 article-title: Novel hypomorphic alleles of the mouse tyrosinase gene induced by CRISPR-Cas9 nucleases cause non-albino pigmentation phenotypes publication-title: PLoS One contributor: fullname: Kesterson – volume: 283 start-page: 10485 year: 2008 end-page: 10492 ident: bb0035 article-title: A novel function for hydroxyproline oxidase in apoptosis through generation of reactive oxygen species publication-title: J. Biol. Chem. contributor: fullname: Phang – volume: 9 start-page: 437 year: 2018 end-page: 451 ident: bb0170 article-title: Anaerobic 4-hydroxyproline utilization: discovery of a new glycyl radical enzyme in the human gut microbiome uncovers a widespread microbial metabolic activity publication-title: Gut Microbes contributor: fullname: Balskus – volume: 29 start-page: 1615 year: 2018 end-page: 1623 ident: bb0015 article-title: Hydroxyproline metabolism and oxalate synthesis in primary hyperoxaluria publication-title: J. Am. Soc. Nephrol. contributor: fullname: Holmes – volume: 103 start-page: 18249 year: 2006 end-page: 18254 ident: bb0055 article-title: Alanine-glyoxylate aminotransferase-deficient mice, a model for primary hyperoxaluria that responds to adenoviral gene transfer publication-title: Proc. Natl. Acad. Sci. U. S. A. contributor: fullname: Roy-Chowdhury – volume: 8 year: 2013 ident: bb0040 article-title: P53 family members modulate the expression of PRODH, but not PRODH2, via intronic p53 response elements publication-title: PlosOne contributor: fullname: Campomenosi – volume: 1822 start-page: 1544 year: 2012 end-page: 1552 ident: bb0025 article-title: 4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition publication-title: Biochim Biophys Acta contributor: fullname: Lowther – volume: 15 start-page: 1 year: 2015 end-page: 6 ident: bb0130 article-title: 4-hydroxyglutamate is a biomarker for primary hyperoxaluria type 3 publication-title: JIMD reports contributor: fullname: Frishberg – volume: 394 start-page: 409 year: 2006 end-page: 416 ident: bb0090 article-title: Reconstruction of human hepatocyte glyoxylate metabolic pathways in stably transformed Chinese-hamster ovary cells publication-title: Biochem. J. contributor: fullname: Danpure – volume: 8 start-page: 2281 year: 2013 end-page: 2308 ident: bb0070 article-title: Genome engineering using the CRISPR-Cas9 system publication-title: Nat. Protoc. contributor: fullname: Zhang – volume: 70 start-page: 914 year: 2006 end-page: 923 ident: bb0095 article-title: Modeling of hyperoxaluric calcium oxalate nephrolithiasis: experimental induction of hyperoxaluria by hydroxy-L-proline publication-title: Kidney Int. contributor: fullname: Byer – volume: 421 start-page: 121 year: 2012 end-page: 124 ident: bb0150 publication-title: Glycolate and 2-phosphoglycolate content of tissues measured by ion chromatography coupled to mass spectrometry contributor: fullname: Holmes – start-page: 1821 year: 2001 end-page: 1838 ident: bb0005 article-title: Disorders of proline and hydroxyproline metabolism publication-title: The Metabolic and Molecular Bases of Inherited Disease contributor: fullname: Valle – volume: 39 start-page: 625 year: 2016 end-page: 632 ident: bb0050 article-title: Genetic cause and prevalence of hydroxyprolinemia publication-title: J. Inherit. Metab. Dis. contributor: fullname: Kolker – volume: 302 start-page: F688 year: 2012 end-page: F693 ident: bb0060 article-title: Hydroxyproline metabolism in mouse models of primary hyperoxaluria publication-title: Am J Physiol Renal Physiol contributor: fullname: Salido – volume: 466 start-page: 273 year: 2015 end-page: 281 ident: bb0030 article-title: Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria publication-title: Biochem. J. contributor: fullname: Lowther – volume: 62 start-page: 392 year: 2002 end-page: 400 ident: bb0110 article-title: Potential mechanisms of marked hyperoxaluria not due to primary hyperoxaluria I or II publication-title: Kid Intl contributor: fullname: Milliner – volume: 44 start-page: 289 year: 2016 end-page: 297 ident: bb0155 article-title: Ascorbic acid intake and oxalate synthesis publication-title: Urolithiasis contributor: fullname: Holmes – start-page: 119 year: 2016 end-page: 126 ident: bb9000 publication-title: CJASN contributor: fullname: Milliner – volume: 49 start-page: 1005 year: 1980 end-page: 1061 ident: bb0010 article-title: Metabolism of proline and the hydroxyprolines publication-title: Annu. Rev. Biochem. contributor: fullname: Frank – volume: 1862 start-page: 233 year: 2016 end-page: 239 ident: bb0140 article-title: Metabolism of (13)C5-hydroxyproline in mouse models of primary Hyperoxaluria and its inhibition by RNAi therapeutics targeting liver glycolate oxidase and hydroxyproline dehydrogenase publication-title: Biochim. Biophys. Acta contributor: fullname: Holmes – volume: 31 year: 2017 ident: bb0120 article-title: HOGA1 gene mutations of primary hyperoxaluria type 3 in Tunisian patients publication-title: J. Clin. Lab. Anal. contributor: fullname: Bouslama – volume: 87 start-page: 392 year: 2010 end-page: 399 ident: bb0100 article-title: Mutations in DHDPSL are responsible for primary hyperoxaluria type III publication-title: Am. J. Hum. Genet. contributor: fullname: Frishberg – volume: 1862 start-page: 1055 year: 2016 end-page: 1062 ident: bb0080 article-title: Effects of alanine:glyoxylate aminotransferase variants and pyridoxine sensitivity on oxalate metabolism in a cell-based cytotoxicity assay publication-title: Biochim. Biophys. Acta contributor: fullname: Danpure – volume: 54 start-page: 406 year: 2017 end-page: 411 ident: bb0115 article-title: Late diagnosis of primary hyperoxaluria type III publication-title: Ann. Clin. Biochem. contributor: fullname: de la Faille – volume: 1852 start-page: 2700 year: 2015 end-page: 2705 ident: bb0065 article-title: Hydroxyproline metabolism in a mouse model of primary hyperoxaluria type 3 publication-title: Biochem Biophys ACTA contributor: fullname: Holmes – volume: 26 start-page: 2559 year: 2015 end-page: 2570 ident: bb0125 article-title: Phenotype-genotype correlations and estimated carrier frequencies of primary hyperoxaluria publication-title: J. Am. Soc. Nephrol. contributor: fullname: Harris – volume: 302 start-page: G637 year: 2012 end-page: G643 ident: bb0085 article-title: Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria publication-title: Am J Physiol Gastro Liver Physiol contributor: fullname: Lowther – volume: 75 start-page: 1264 year: 2009 end-page: 1271 ident: bb0105 article-title: The primary hyperoxalurias publication-title: Kidney Int. contributor: fullname: Milliner – volume: 295 start-page: 85 year: 2007 end-page: 92 ident: bb0045 article-title: Overexpression of proline oxidase induces proline-dependent and mitochondria-mediated apoptosis publication-title: Mol. Cell. Biochem. contributor: fullname: Phang – volume: 26 start-page: 1983 year: 2018 end-page: 1995 ident: bb0165 article-title: Specific inhibition of hepatic lactate dehydrogenase reduces oxalate production in mouse models of primary Hyperoxaluria publication-title: Mol. Ther. contributor: fullname: Brown – volume: 90 start-page: 1497 year: 2012 end-page: 1504 ident: bb0020 article-title: Primary hyperoxaluria type III—a model for studying perturbations in glyoxylate metabolism publication-title: J. Mol. Med. contributor: fullname: Frishberg – volume: 28 start-page: 494 year: 2017 end-page: 503 ident: bb0160 article-title: An investigational RNAi therapeutic targeting glycolate oxidase reduces oxalate production in models of primary hyperoxaluria publication-title: J. Am. Soc. Nephrol. contributor: fullname: Knight – volume: 302 start-page: F688 year: 2012 ident: 10.1016/j.bbadis.2019.165633_bb0060 article-title: Hydroxyproline metabolism in mouse models of primary hyperoxaluria publication-title: Am J Physiol Renal Physiol doi: 10.1152/ajprenal.00473.2011 contributor: fullname: Knight – volume: 87 start-page: 392 year: 2010 ident: 10.1016/j.bbadis.2019.165633_bb0100 article-title: Mutations in DHDPSL are responsible for primary hyperoxaluria type III publication-title: Am. J. Hum. Genet. doi: 10.1016/j.ajhg.2010.07.023 contributor: fullname: Belostotsky – ident: 10.1016/j.bbadis.2019.165633_bb0135 – volume: 1822 start-page: 1544 year: 2012 ident: 10.1016/j.bbadis.2019.165633_bb0025 article-title: 4-Hydroxy-2-oxoglutarate aldolase inactivity in primary hyperoxaluria type 3 and glyoxylate reductase inhibition publication-title: Biochim Biophys Acta doi: 10.1016/j.bbadis.2012.06.014 contributor: fullname: Riedel – volume: 75 start-page: 1264 year: 2009 ident: 10.1016/j.bbadis.2019.165633_bb0105 article-title: The primary hyperoxalurias publication-title: Kidney Int. doi: 10.1038/ki.2009.32 contributor: fullname: Hoppe – volume: 29 start-page: 1615 year: 2018 ident: 10.1016/j.bbadis.2019.165633_bb0015 article-title: Hydroxyproline metabolism and oxalate synthesis in primary hyperoxaluria publication-title: J. Am. Soc. Nephrol. doi: 10.1681/ASN.2017040390 contributor: fullname: Fargue – volume: 8 start-page: 2281 year: 2013 ident: 10.1016/j.bbadis.2019.165633_bb0070 article-title: Genome engineering using the CRISPR-Cas9 system publication-title: Nat. Protoc. doi: 10.1038/nprot.2013.143 contributor: fullname: Ran – volume: 1862 start-page: 1055 year: 2016 ident: 10.1016/j.bbadis.2019.165633_bb0080 article-title: Effects of alanine:glyoxylate aminotransferase variants and pyridoxine sensitivity on oxalate metabolism in a cell-based cytotoxicity assay publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbadis.2016.02.004 contributor: fullname: Fargue – volume: 394 start-page: 409 year: 2006 ident: 10.1016/j.bbadis.2019.165633_bb0090 article-title: Reconstruction of human hepatocyte glyoxylate metabolic pathways in stably transformed Chinese-hamster ovary cells publication-title: Biochem. J. doi: 10.1042/BJ20051397 contributor: fullname: Behnam – start-page: 1821 year: 2001 ident: 10.1016/j.bbadis.2019.165633_bb0005 article-title: Disorders of proline and hydroxyproline metabolism contributor: fullname: Phang – volume: 421 start-page: 121 year: 2012 ident: 10.1016/j.bbadis.2019.165633_bb0150 publication-title: Glycolate and 2-phosphoglycolate content of tissues measured by ion chromatography coupled to mass spectrometry contributor: fullname: Knight – volume: 49 start-page: 1005 year: 1980 ident: 10.1016/j.bbadis.2019.165633_bb0010 article-title: Metabolism of proline and the hydroxyprolines publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.bi.49.070180.005041 contributor: fullname: Adams – volume: 26 start-page: 2559 year: 2015 ident: 10.1016/j.bbadis.2019.165633_bb0125 article-title: Phenotype-genotype correlations and estimated carrier frequencies of primary hyperoxaluria publication-title: J. Am. Soc. Nephrol. doi: 10.1681/ASN.2014070698 contributor: fullname: Hopp – volume: 103 start-page: 18249 year: 2006 ident: 10.1016/j.bbadis.2019.165633_bb0055 article-title: Alanine-glyoxylate aminotransferase-deficient mice, a model for primary hyperoxaluria that responds to adenoviral gene transfer publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0607218103 contributor: fullname: Salido – start-page: 119 year: 2016 ident: 10.1016/j.bbadis.2019.165633_bb9000 publication-title: CJASN doi: 10.2215/CJN.02810315 contributor: fullname: Zhao – volume: 466 start-page: 273 year: 2015 ident: 10.1016/j.bbadis.2019.165633_bb0030 article-title: Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria publication-title: Biochem. J. doi: 10.1042/BJ20141159 contributor: fullname: Summitt – volume: 15 start-page: 1 year: 2015 ident: 10.1016/j.bbadis.2019.165633_bb0130 article-title: 4-hydroxyglutamate is a biomarker for primary hyperoxaluria type 3 publication-title: JIMD reports contributor: fullname: Pitt – volume: 39 start-page: 625 year: 2016 ident: 10.1016/j.bbadis.2019.165633_bb0050 article-title: Genetic cause and prevalence of hydroxyprolinemia publication-title: J. Inherit. Metab. Dis. doi: 10.1007/s10545-016-9940-2 contributor: fullname: Staufner – volume: 70 start-page: 914 year: 2006 ident: 10.1016/j.bbadis.2019.165633_bb0095 article-title: Modeling of hyperoxaluric calcium oxalate nephrolithiasis: experimental induction of hyperoxaluria by hydroxy-L-proline publication-title: Kidney Int. doi: 10.1038/sj.ki.5001699 contributor: fullname: Khan – volume: 8 year: 2013 ident: 10.1016/j.bbadis.2019.165633_bb0040 article-title: P53 family members modulate the expression of PRODH, but not PRODH2, via intronic p53 response elements publication-title: PlosOne doi: 10.1371/journal.pone.0069152 contributor: fullname: Raimondi – volume: 44 start-page: 289 year: 2016 ident: 10.1016/j.bbadis.2019.165633_bb0155 article-title: Ascorbic acid intake and oxalate synthesis publication-title: Urolithiasis doi: 10.1007/s00240-016-0868-7 contributor: fullname: Knight – volume: 302 start-page: G637 year: 2012 ident: 10.1016/j.bbadis.2019.165633_bb0085 article-title: Metabolism of [13C5]hydroxyproline in vitro and in vivo: implications for primary hyperoxaluria publication-title: Am J Physiol Gastro Liver Physiol doi: 10.1152/ajpgi.00331.2011 contributor: fullname: Jiang – volume: 31 year: 2017 ident: 10.1016/j.bbadis.2019.165633_bb0120 article-title: HOGA1 gene mutations of primary hyperoxaluria type 3 in Tunisian patients publication-title: J. Clin. Lab. Anal. contributor: fullname: M’Dimegh – volume: 2012 start-page: 819202 year: 2012 ident: 10.1016/j.bbadis.2019.165633_bb0145 article-title: Glyoxal formation and its role in endogenous oxalate synthesis publication-title: Adv Urol doi: 10.1155/2012/819202 contributor: fullname: Lange – volume: 62 start-page: 392 year: 2002 ident: 10.1016/j.bbadis.2019.165633_bb0110 article-title: Potential mechanisms of marked hyperoxaluria not due to primary hyperoxaluria I or II publication-title: Kid Intl doi: 10.1046/j.1523-1755.2002.00468.x contributor: fullname: Monico – volume: 283 start-page: 10485 year: 2008 ident: 10.1016/j.bbadis.2019.165633_bb0035 article-title: A novel function for hydroxyproline oxidase in apoptosis through generation of reactive oxygen species publication-title: J. Biol. Chem. doi: 10.1074/jbc.M702181200 contributor: fullname: Cooper – volume: 90 start-page: 1497 year: 2012 ident: 10.1016/j.bbadis.2019.165633_bb0020 article-title: Primary hyperoxaluria type III—a model for studying perturbations in glyoxylate metabolism publication-title: J. Mol. Med. doi: 10.1007/s00109-012-0930-z contributor: fullname: Belostotsky – volume: 9 start-page: 437 year: 2018 ident: 10.1016/j.bbadis.2019.165633_bb0170 article-title: Anaerobic 4-hydroxyproline utilization: discovery of a new glycyl radical enzyme in the human gut microbiome uncovers a widespread microbial metabolic activity publication-title: Gut Microbes contributor: fullname: Huang – volume: 11 year: 2016 ident: 10.1016/j.bbadis.2019.165633_bb0075 article-title: Novel hypomorphic alleles of the mouse tyrosinase gene induced by CRISPR-Cas9 nucleases cause non-albino pigmentation phenotypes publication-title: PLoS One doi: 10.1371/journal.pone.0155812 contributor: fullname: Challa – volume: 1862 start-page: 233 year: 2016 ident: 10.1016/j.bbadis.2019.165633_bb0140 article-title: Metabolism of (13)C5-hydroxyproline in mouse models of primary Hyperoxaluria and its inhibition by RNAi therapeutics targeting liver glycolate oxidase and hydroxyproline dehydrogenase publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbadis.2015.12.001 contributor: fullname: Li – volume: 295 start-page: 85 year: 2007 ident: 10.1016/j.bbadis.2019.165633_bb0045 article-title: Overexpression of proline oxidase induces proline-dependent and mitochondria-mediated apoptosis publication-title: Mol. Cell. Biochem. doi: 10.1007/s11010-006-9276-6 contributor: fullname: Hu – volume: 1852 start-page: 2700 year: 2015 ident: 10.1016/j.bbadis.2019.165633_bb0065 article-title: Hydroxyproline metabolism in a mouse model of primary hyperoxaluria type 3 publication-title: Biochem Biophys ACTA contributor: fullname: Li – volume: 54 start-page: 406 year: 2017 ident: 10.1016/j.bbadis.2019.165633_bb0115 article-title: Late diagnosis of primary hyperoxaluria type III publication-title: Ann. Clin. Biochem. doi: 10.1177/0004563216677101 contributor: fullname: Richard – volume: 28 start-page: 494 year: 2017 ident: 10.1016/j.bbadis.2019.165633_bb0160 article-title: An investigational RNAi therapeutic targeting glycolate oxidase reduces oxalate production in models of primary hyperoxaluria publication-title: J. Am. Soc. Nephrol. doi: 10.1681/ASN.2016030338 contributor: fullname: Liebow – volume: 26 start-page: 1983 year: 2018 ident: 10.1016/j.bbadis.2019.165633_bb0165 article-title: Specific inhibition of hepatic lactate dehydrogenase reduces oxalate production in mouse models of primary Hyperoxaluria publication-title: Mol. Ther. doi: 10.1016/j.ymthe.2018.05.016 contributor: fullname: Lai |
SSID | ssj0000670 |
Score | 2.4109657 |
Snippet | The major clinical manifestation of the Primary Hyperoxalurias (PH) is increased production of oxalate, as a consequence of genetic mutations that lead to... |
SourceID | pubmedcentral crossref pubmed elsevier |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 165633 |
SubjectTerms | Amino Acid Sequence Animals Base Sequence Calcium - metabolism Disease Models, Animal Female Glycolate Glycolates - metabolism Glycolates - urine Humans Hydroxyproline - metabolism Hyperoxaluria, Primary - metabolism Kidney - metabolism Kidney stone Male Mice Mice, Inbred C57BL Mice, Knockout Mouse models Oxalate Oxalates - metabolism Oxalates - urine Oxidoreductases - metabolism Primary hyperoxaluria Proline Oxidase - metabolism |
Title | The effects of the inactivation of Hydroxyproline dehydrogenase on urinary oxalate and glycolate excretion in mouse models of primary hyperoxaluria |
URI | https://dx.doi.org/10.1016/j.bbadis.2019.165633 https://www.ncbi.nlm.nih.gov/pubmed/31821850 https://pubmed.ncbi.nlm.nih.gov/PMC7047938 |
Volume | 1866 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9wwEB7Boqq9VC190cfKh17DJtix4yOsipZCUdWWam-RX2FToewKLRK58Cf6hzvjJIg9IfUUxY_Y8kxmxqOZbwA-S2utNoZ-JMUTIas00VapxHme86CcFY4c-t_O5exCfJ3n8y2YDrkwFFbZy_5Opkdp3bdM-tOcrOp68jPVBK_FNZogKIazYht2UB0JMYKdw5PT2flDgRxdLTg-oQlDBl0M87LW-JpwuzO9T0g0nD-qoTajJx-oo-MX8Ly3I9lht9WXsBWaXXjSVZZsd-HpdCjk9gr-IiuwPm6DLSuGJh-rG0po6Nyx1DZrPcWzrGINn8B8WFADMhcqOYZDyCdvrlu2vDVXaJ0y03h2edUiF9FbuHWUDInj6oaRLyGwWGEnLrfq8CzYoiVMcpyP3zKv4eL4y6_pLOlrMSROSL5OyFWKdzF5YKrCGs2lKSptQ6qV1xn30iMNBI_oPUVqncSLtbJaV85yLXJf8DcwapZNeAes8k7ioYs8q1Ih8qADt1wpl3NUnIHne5AM51_2WyyHWLQ_ZUevkuhVdvTaAzUQqdxgnRK1wiMz33akvF8Hd482T57iNzeIfD-A0Lg3e5p6EVG5FYH18-L9f-_mAzw7oMt8DHD7CKP19U34hBbP2o5he_8uGyNfH_0-PaPn9MfZ93HP59h7Mj_6B8jnCII |
link.rule.ids | 230,315,786,790,891,3525,4521,24144,27600,27955,27956,45618,45696,45712,45907 |
linkProvider | Elsevier |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9xADB5RqopeqvIo0AedA9d0s3gemWO7Ktq2wKUg7S2aV9gglF2hrUR-B38Ye5Ig9oTUYyaeyWjs2B7L_szYsXLOGWvpR9KQCVXlmXFaZz6AhKi9E54C-ucXanolfs_kbINNhloYSqvsdX-n05O27kdG_WmOlnU9-psbgtcCgy4IquFx8Yq9FhLvelTFN_vxXB2nQAtSZ0Q-1M-lJC_nbKgJtXtsvhEODcCL9mk9d_KZMTp9z971XiT_3m10m23EZoe96fpKtjtsazK0cdtlDygIvM_a4IuKo8PH64bKGbpgLI1N20DZLMvUwSfyEOc0gKKFJo4jCUXk7V3LF_f2Fn1TbpvAr29blCF6iveeSiGRrm44RRIiT_110ueWHZoFn7eESI7zcS27x65Of15OplnfiSHzQsEqo0Ap3sTUia0KZw0oW1TGxdzoYMYQVEAOCEjYPUXuvMJrtXbGVN6BETIU8IFtNosmHjBeBa_w0IUcV7kQMpoIDrT2EtBsRpCHLBvOv-y3WA6ZaDdlx6-S-FV2_DpkemBSuSY4JdqEF2bud6x8-g7uHj0emeOaa0x-IiAs7vU3TT1PmNyaoPqh-Pjfu_nKtqaX52fl2a-LP5_Y2xO61qdUt89sc3X3L35B32fljpJsPwKqrAU4 |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=The+Effects+of+the+Inactivation+of+Hydroxyproline+Dehydrogenase+on+Urinary+Oxalate+and+Glycolate+Excretion+in+Mouse+Models+of+Primary+Hyperoxaluria&rft.jtitle=Biochimica+et+biophysica+acta.+Molecular+basis+of+disease&rft.au=Buchalski%2C+Brianna&rft.au=Wood%2C+Kyle+D&rft.au=Challa%2C+Anil&rft.au=Fargue%2C+Sonia&rft.date=2020-03-01&rft.issn=0925-4439&rft.eissn=1879-260X&rft.volume=1866&rft.issue=3&rft.spage=165633&rft.epage=165633&rft_id=info:doi/10.1016%2Fj.bbadis.2019.165633&rft_id=info%3Apmid%2F31821850&rft.externalDBID=PMC7047938 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0925-4439&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0925-4439&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0925-4439&client=summon |