PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23232983-9 2013 The metabolic production of glutamate from proline proceeds by proline dehydrogenase (PRODH), producing superoxide. Proline 43-50 proline dehydrogenase 1 Homo sapiens 98-103 23462603-10 2013 CONCLUSION: We found that distinct molecular alterations of the PRODH gene result in abnormal proline levels. Proline 94-101 proline dehydrogenase 1 Homo sapiens 64-69 22886911-1 2012 Proline dehydrogenase (oxidase, PRODH/POX), the first enzyme in the proline degradative pathway, plays a special role in tumorigenesis and tumor development. Proline 68-75 proline dehydrogenase 1 Homo sapiens 32-37 22886911-1 2012 Proline dehydrogenase (oxidase, PRODH/POX), the first enzyme in the proline degradative pathway, plays a special role in tumorigenesis and tumor development. Proline 68-75 proline dehydrogenase 1 Homo sapiens 38-41 22886911-2 2012 Proline metabolism catalyzed by PRODH/POX is closely linked with the tricarboxylic acid (TCA) cycle and urea cycle. Proline 0-7 proline dehydrogenase 1 Homo sapiens 32-37 22886911-2 2012 Proline metabolism catalyzed by PRODH/POX is closely linked with the tricarboxylic acid (TCA) cycle and urea cycle. Proline 0-7 proline dehydrogenase 1 Homo sapiens 38-41 22886911-4 2012 Importantly, by catalyzing proline to P5C, PRODH/POX donates electrons into the electron transport chain to generate ROS or ATP. Proline 27-34 proline dehydrogenase 1 Homo sapiens 43-48 22886911-4 2012 Importantly, by catalyzing proline to P5C, PRODH/POX donates electrons into the electron transport chain to generate ROS or ATP. Proline 27-34 proline dehydrogenase 1 Homo sapiens 49-52 22885468-1 2012 Proline dehydrogenase (oxidase, PRODH/POX), the first enzyme in the pathway of proline catabolism, has been identified as a mitochondrial, metabolic tumor suppressor, which is downregulated in a variety of human tumors. Proline 79-86 proline dehydrogenase 1 Homo sapiens 32-37 22885468-1 2012 Proline dehydrogenase (oxidase, PRODH/POX), the first enzyme in the pathway of proline catabolism, has been identified as a mitochondrial, metabolic tumor suppressor, which is downregulated in a variety of human tumors. Proline 79-86 proline dehydrogenase 1 Homo sapiens 38-41 22796327-0 2012 Proline dehydrogenase is essential for proline protection against hydrogen peroxide-induced cell death. Proline 39-46 proline dehydrogenase 1 Homo sapiens 0-21 22796327-2 2012 Proline is oxidized to glutamate in the mitochondria, with the rate-limiting step catalyzed by proline dehydrogenase (PRODH). Proline 0-7 proline dehydrogenase 1 Homo sapiens 95-116 22796327-2 2012 Proline is oxidized to glutamate in the mitochondria, with the rate-limiting step catalyzed by proline dehydrogenase (PRODH). Proline 0-7 proline dehydrogenase 1 Homo sapiens 118-123 22796327-3 2012 PRODH expression is inducible by p53, leading to increased proline oxidation, reactive oxygen species formation, and induction of apoptosis. Proline 59-66 proline dehydrogenase 1 Homo sapiens 0-5 22796327-7 2012 Inhibition or siRNA-mediated knockdown of PRODH abolished proline protection against oxidative stress, whereas knockdown of Delta(1)-pyrroline-5-carboxylate reductase, a key enzyme in proline biosynthesis, had no impact on proline protection. Proline 58-65 proline dehydrogenase 1 Homo sapiens 42-47 22796327-11 2012 The role of PRODH in proline-mediated protection was validated in the prostate carcinoma cell line PC3. Proline 21-28 proline dehydrogenase 1 Homo sapiens 12-17 22796327-13 2012 The results provide evidence that PRODH is essential in proline protection against hydrogen peroxide-mediated cell death and that proline/PRODH helps activate Akt in cancer cells. Proline 56-63 proline dehydrogenase 1 Homo sapiens 34-39 22796327-13 2012 The results provide evidence that PRODH is essential in proline protection against hydrogen peroxide-mediated cell death and that proline/PRODH helps activate Akt in cancer cells. Proline 130-137 proline dehydrogenase 1 Homo sapiens 138-143 22609800-1 2012 Proline is a readily released stress substrate that can be metabolized by proline oxidase (POX) to generate either reactive oxygen species (ROS) to induce apoptosis or autophagy or ATP during times of nutrient stress. Proline 0-7 proline dehydrogenase 1 Homo sapiens 74-89 22609800-1 2012 Proline is a readily released stress substrate that can be metabolized by proline oxidase (POX) to generate either reactive oxygen species (ROS) to induce apoptosis or autophagy or ATP during times of nutrient stress. Proline 0-7 proline dehydrogenase 1 Homo sapiens 91-94 22609800-7 2012 Under low-glucose and combined low-glucose and hypoxic conditions, proline catabolized by POX was used preferentially for ATP production, whereas under hypoxia, POX mediated autophagic signaling for survival by generating ROS. Proline 67-74 proline dehydrogenase 1 Homo sapiens 90-93 22615405-5 2012 Proline oxidase, also known as proline dehydrogenase (POX/PRODH), the first enzyme in proline catabolism, is a mitochondrial tumor suppressor that inhibits proliferation and induces apoptosis. Proline 31-38 proline dehydrogenase 1 Homo sapiens 54-57 22615405-5 2012 Proline oxidase, also known as proline dehydrogenase (POX/PRODH), the first enzyme in proline catabolism, is a mitochondrial tumor suppressor that inhibits proliferation and induces apoptosis. Proline 31-38 proline dehydrogenase 1 Homo sapiens 58-63 22089387-1 2012 Dye-linked L-proline dehydrogenase (ProDH) catalyzes the oxidation of L-proline to (1)-pyrroline-5-carboxylate (P5C) in the presence of artificial electron acceptors. Proline 11-20 proline dehydrogenase 1 Homo sapiens 36-41 22201764-3 2012 ProDH is not only essential for proline catabolism but also plays key roles in providing energy, shuttling redox potential between cellular compartments and reactive oxygen species production. Proline 32-39 proline dehydrogenase 1 Homo sapiens 0-5 21738766-5 2011 People with 22q11DS are vulnerable for haploinsufficiency of PRODH, a gene that codes for an enzyme converting proline into glutamate. Proline 111-118 proline dehydrogenase 1 Homo sapiens 61-66 20545884-1 2010 Proline accumulation in response to abiotic stress is controlled partially by transcriptional regulation of key enzymes including Delta1-pyrroline-carboxylate synthetase1 (P5CS1), proline dehydrogenase (ProDH), ornithine amino transferase (OAT) and Delta1-pyrroline-carboxylate dehydrogenase (P5CDH). Proline 0-7 proline dehydrogenase 1 Homo sapiens 180-201 20545884-1 2010 Proline accumulation in response to abiotic stress is controlled partially by transcriptional regulation of key enzymes including Delta1-pyrroline-carboxylate synthetase1 (P5CS1), proline dehydrogenase (ProDH), ornithine amino transferase (OAT) and Delta1-pyrroline-carboxylate dehydrogenase (P5CDH). Proline 0-7 proline dehydrogenase 1 Homo sapiens 203-208 20545884-5 2010 ProDH downregulation by low water potential and upregulation by stress release was not impaired in aba2-1, p5cs1 or p5cs1/aba2-1 compared with wild type despite differing ABA and proline levels in these mutants. Proline 179-186 proline dehydrogenase 1 Homo sapiens 0-5 19654292-3 2009 Proline oxidase (POX), catalyzing the first step in proline catabolism, is induced by p53 and can regulate cell survival as well as mediate programmed cell death. Proline 52-59 proline dehydrogenase 1 Homo sapiens 0-15 19654292-3 2009 Proline oxidase (POX), catalyzing the first step in proline catabolism, is induced by p53 and can regulate cell survival as well as mediate programmed cell death. Proline 52-59 proline dehydrogenase 1 Homo sapiens 17-20 19415679-2 2009 Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (POX), a mitochondrial inner membrane enzyme, can generate ATP. Proline 0-7 proline dehydrogenase 1 Homo sapiens 219-234 19415679-2 2009 Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (POX), a mitochondrial inner membrane enzyme, can generate ATP. Proline 0-7 proline dehydrogenase 1 Homo sapiens 236-239 19415679-2 2009 Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (POX), a mitochondrial inner membrane enzyme, can generate ATP. Proline 172-179 proline dehydrogenase 1 Homo sapiens 219-234 19415679-2 2009 Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (POX), a mitochondrial inner membrane enzyme, can generate ATP. Proline 172-179 proline dehydrogenase 1 Homo sapiens 236-239 19415679-2 2009 Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (POX), a mitochondrial inner membrane enzyme, can generate ATP. Proline 172-179 proline dehydrogenase 1 Homo sapiens 219-234 19415679-2 2009 Proline metabolism is especially important in nutrient stress because proline is readily available from the breakdown of extracellular matrix (ECM), and the degradation of proline through the proline cycle initiated by proline oxidase (POX), a mitochondrial inner membrane enzyme, can generate ATP. Proline 172-179 proline dehydrogenase 1 Homo sapiens 236-239 19140736-1 2009 Proline dehydrogenase (PRODH) catalyzes the oxidation of l-proline to Delta-1-pyrroline-5-carboxylate. Proline 57-66 proline dehydrogenase 1 Homo sapiens 0-21 19140736-1 2009 Proline dehydrogenase (PRODH) catalyzes the oxidation of l-proline to Delta-1-pyrroline-5-carboxylate. Proline 57-66 proline dehydrogenase 1 Homo sapiens 23-28 18794809-1 2008 Proline oxidase (POX), a flavoenzyme localized at the inner mitochondrial membrane, catalyzes the first step of proline degradation by converting proline to pyrroline-5-carboxylate (P5C). Proline 112-119 proline dehydrogenase 1 Homo sapiens 0-15 18794809-1 2008 Proline oxidase (POX), a flavoenzyme localized at the inner mitochondrial membrane, catalyzes the first step of proline degradation by converting proline to pyrroline-5-carboxylate (P5C). Proline 112-119 proline dehydrogenase 1 Homo sapiens 17-20 18794809-1 2008 Proline oxidase (POX), a flavoenzyme localized at the inner mitochondrial membrane, catalyzes the first step of proline degradation by converting proline to pyrroline-5-carboxylate (P5C). Proline 146-153 proline dehydrogenase 1 Homo sapiens 0-15 18794809-1 2008 Proline oxidase (POX), a flavoenzyme localized at the inner mitochondrial membrane, catalyzes the first step of proline degradation by converting proline to pyrroline-5-carboxylate (P5C). Proline 146-153 proline dehydrogenase 1 Homo sapiens 17-20 18794809-2 2008 POX is markedly elevated during p53-induced apoptosis and generates proline-dependent reactive oxygen species (ROS), specifically superoxide radicals, to induce apoptosis through both mitochondrial and death receptor pathways. Proline 68-75 proline dehydrogenase 1 Homo sapiens 0-3 18794809-11 2008 Thus, POX metabolism of substrate proline affects multiple signaling pathways, modulating both apoptosis and tumor growth, and could be an attractive target to metabolically control the cancer phenotypes. Proline 34-41 proline dehydrogenase 1 Homo sapiens 6-9 18401543-3 2008 proline dehydrogenase (POX/PRODH), catalyzes the first step in proline degradation and uses proline to generate ATP for survival or reactive oxygen species for programmed cell death. Proline 0-7 proline dehydrogenase 1 Homo sapiens 27-32 18401543-3 2008 proline dehydrogenase (POX/PRODH), catalyzes the first step in proline degradation and uses proline to generate ATP for survival or reactive oxygen species for programmed cell death. Proline 63-70 proline dehydrogenase 1 Homo sapiens 27-32 18806116-4 2008 Studies show that the proline-utilizing enzyme, proline oxidase (POX)/proline dehydrogenase (PRODH), responds to genotoxic, inflammatory, and nutrient stress. Proline 22-29 proline dehydrogenase 1 Homo sapiens 48-63 18806116-4 2008 Studies show that the proline-utilizing enzyme, proline oxidase (POX)/proline dehydrogenase (PRODH), responds to genotoxic, inflammatory, and nutrient stress. Proline 22-29 proline dehydrogenase 1 Homo sapiens 65-68 18806116-4 2008 Studies show that the proline-utilizing enzyme, proline oxidase (POX)/proline dehydrogenase (PRODH), responds to genotoxic, inflammatory, and nutrient stress. Proline 22-29 proline dehydrogenase 1 Homo sapiens 93-98 18806116-6 2008 Special functions include the use of proline by POX/PRODH to generate superoxide radicals that initiate apoptosis by intrinsic and extrinsic pathways. Proline 37-44 proline dehydrogenase 1 Homo sapiens 48-51 18806116-6 2008 Special functions include the use of proline by POX/PRODH to generate superoxide radicals that initiate apoptosis by intrinsic and extrinsic pathways. Proline 37-44 proline dehydrogenase 1 Homo sapiens 52-57 18806117-1 2008 l-Proline concentration is primarily related to the balance of enzymatic activities of proline dehydrogenase [proline oxidase (POX)] and Delta-1-pyrroline-5-carboxylate (P5C) reductase. Proline 0-9 proline dehydrogenase 1 Homo sapiens 127-130 18287100-4 2008 The first steps in the degradation of proline and hydroxyproline are catalyzed by proline oxidase (POX) and hydroxyproline oxidase (OH-POX), respectively. Proline 38-45 proline dehydrogenase 1 Homo sapiens 99-102 18287100-4 2008 The first steps in the degradation of proline and hydroxyproline are catalyzed by proline oxidase (POX) and hydroxyproline oxidase (OH-POX), respectively. Proline 38-45 proline dehydrogenase 1 Homo sapiens 135-138 18036351-4 2008 Overexpression of proline dehydrogenase (PRODH), a mitochondrial flavoenzyme that oxidizes proline, resulted in 6-fold lower intracellular proline content and decreased cell survival relative to control cells. Proline 18-25 proline dehydrogenase 1 Homo sapiens 41-46 18036351-4 2008 Overexpression of proline dehydrogenase (PRODH), a mitochondrial flavoenzyme that oxidizes proline, resulted in 6-fold lower intracellular proline content and decreased cell survival relative to control cells. Proline 91-98 proline dehydrogenase 1 Homo sapiens 18-39 18036351-4 2008 Overexpression of proline dehydrogenase (PRODH), a mitochondrial flavoenzyme that oxidizes proline, resulted in 6-fold lower intracellular proline content and decreased cell survival relative to control cells. Proline 91-98 proline dehydrogenase 1 Homo sapiens 41-46 18036351-5 2008 Cells overexpressing PRODH were rescued by pipecolate, an analog that mimics the antioxidant properties of proline, and by tetrahydro-2-furoic acid, a specific inhibitor of PRODH. Proline 107-114 proline dehydrogenase 1 Homo sapiens 21-26 17412540-1 2007 Hyperprolinemia type I (HPI) results from a deficiency of proline oxidase (POX), involved in the first step in the conversion of proline to glutamate. Proline 5-12 proline dehydrogenase 1 Homo sapiens 58-73 17412540-1 2007 Hyperprolinemia type I (HPI) results from a deficiency of proline oxidase (POX), involved in the first step in the conversion of proline to glutamate. Proline 5-12 proline dehydrogenase 1 Homo sapiens 75-78 17344208-1 2007 Proline dehydrogenase (PRODH) and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) catalyze the two-step oxidation of proline to glutamate. Proline 124-131 proline dehydrogenase 1 Homo sapiens 23-28 16874462-1 2007 Proline oxidase (POX), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of proline to pyrroline- 5-carboxylate (P5C). Proline 104-111 proline dehydrogenase 1 Homo sapiens 0-15 16874462-1 2007 Proline oxidase (POX), a mitochondrial inner-membrane protein, catalyzes the rate-limiting oxidation of proline to pyrroline- 5-carboxylate (P5C). Proline 104-111 proline dehydrogenase 1 Homo sapiens 17-20 16874462-4 2007 To further investigate the molecular basis of POX-induced apoptosis, we utilized the DLD-1.POX cells to show that cells overproducing POX exhibit an L-proline-dependent apoptotic response. Proline 149-158 proline dehydrogenase 1 Homo sapiens 46-49 16874462-4 2007 To further investigate the molecular basis of POX-induced apoptosis, we utilized the DLD-1.POX cells to show that cells overproducing POX exhibit an L-proline-dependent apoptotic response. Proline 149-158 proline dehydrogenase 1 Homo sapiens 91-94 16874462-4 2007 To further investigate the molecular basis of POX-induced apoptosis, we utilized the DLD-1.POX cells to show that cells overproducing POX exhibit an L-proline-dependent apoptotic response. Proline 149-158 proline dehydrogenase 1 Homo sapiens 91-94 16874462-5 2007 The apoptotic effect is specific for L-proline, detectable at 0.2 mM, maximal at 1 mM, and occurs during 48-72 h following the addition of L-proline to cells with maximally induced POX. Proline 37-46 proline dehydrogenase 1 Homo sapiens 181-184 16874462-5 2007 The apoptotic effect is specific for L-proline, detectable at 0.2 mM, maximal at 1 mM, and occurs during 48-72 h following the addition of L-proline to cells with maximally induced POX. Proline 139-148 proline dehydrogenase 1 Homo sapiens 181-184 16874462-7 2007 We conclude that in the presence of proline, high POX activity is sufficient to induce mitochondria-mediated apoptosis. Proline 36-43 proline dehydrogenase 1 Homo sapiens 50-53 16619034-2 2006 We have shown that POX generated proline-dependent reactive oxygen species (ROS), specifically superoxide radicals, and induced apoptosis through the mitochondrial (intrinsic) pathway. Proline 33-40 proline dehydrogenase 1 Homo sapiens 19-22 15662599-1 2005 PRODH maps to 22q11 in the region deleted in the velocardiofacial syndrome/DiGeorge syndrome (VCFS/DGS) and encodes proline oxidase (POX), a mitochondrial inner-membrane enzyme that catalyzes the first step in the proline degradation pathway. Proline 116-123 proline dehydrogenase 1 Homo sapiens 0-5 15662599-1 2005 PRODH maps to 22q11 in the region deleted in the velocardiofacial syndrome/DiGeorge syndrome (VCFS/DGS) and encodes proline oxidase (POX), a mitochondrial inner-membrane enzyme that catalyzes the first step in the proline degradation pathway. Proline 116-123 proline dehydrogenase 1 Homo sapiens 133-136 12217952-4 2002 In addition, two heterozygous PRODH missense mutations (L441P and L289M), detected in 3 of 63 schizophrenic patients but in none among 68 controls, were also associated with increased plasma proline levels. Proline 191-198 proline dehydrogenase 1 Homo sapiens 30-35 11280728-1 2001 The p53-dependent initiation of apoptosis is accompanied by the induction of proline oxidase (POX), a mitochondrial enzyme catalyzing the conversion of proline to pyrroline-5-carboxylate with the concomitant transfer of electrons to cytochrome c. Proline 77-84 proline dehydrogenase 1 Homo sapiens 94-97 11280728-4 2001 In cells expressing POX, the addition of proline increases reactive oxygen species (ROS) generation in a concentration-dependent manner; glutamate, a downstream product of proline oxidation, had no effect. Proline 41-48 proline dehydrogenase 1 Homo sapiens 20-23 11280728-4 2001 In cells expressing POX, the addition of proline increases reactive oxygen species (ROS) generation in a concentration-dependent manner; glutamate, a downstream product of proline oxidation, had no effect. Proline 172-179 proline dehydrogenase 1 Homo sapiens 20-23 11280728-8 2001 Again, we found a proline-dependent ROS increase with POX expression. Proline 18-25 proline dehydrogenase 1 Homo sapiens 54-57 11280728-9 2001 We hypothesize that proline oxidation supports the generation of ROS by donating reducing potential to an electron transport chain altered either by p53-dependent mechanisms or by overexpression of POX. Proline 20-27 proline dehydrogenase 1 Homo sapiens 198-201 33818628-2 2021 The process is catalysed by proline dehydrogenase/proline oxidase (PRODH/POX), a mitochondrial flavin-dependent enzyme converting proline into 1-pyrroline-5-carboxylate (P5C). Proline 28-35 proline dehydrogenase 1 Homo sapiens 67-72 33818628-2 2021 The process is catalysed by proline dehydrogenase/proline oxidase (PRODH/POX), a mitochondrial flavin-dependent enzyme converting proline into 1-pyrroline-5-carboxylate (P5C). Proline 28-35 proline dehydrogenase 1 Homo sapiens 73-76 33818628-11 2021 These aspects of proline metabolism are discussed in the review as an approach to understand complex regulatory mechanisms driving PRODH/POX-dependent apoptosis/survival. Proline 17-24 proline dehydrogenase 1 Homo sapiens 131-136 33818628-11 2021 These aspects of proline metabolism are discussed in the review as an approach to understand complex regulatory mechanisms driving PRODH/POX-dependent apoptosis/survival. Proline 17-24 proline dehydrogenase 1 Homo sapiens 137-140 34943229-5 2021 PRODH/POX is a mitochondrial enzyme that converts proline into pyrroline-5-carboxylate (P5C). Proline 50-57 proline dehydrogenase 1 Homo sapiens 0-5 34943229-5 2021 PRODH/POX is a mitochondrial enzyme that converts proline into pyrroline-5-carboxylate (P5C). Proline 50-57 proline dehydrogenase 1 Homo sapiens 6-9 34943229-7 2021 However, the critical factor in driving PRODH/POX-dependent functions is proline availability. Proline 73-80 proline dehydrogenase 1 Homo sapiens 40-45 34943229-7 2021 However, the critical factor in driving PRODH/POX-dependent functions is proline availability. Proline 73-80 proline dehydrogenase 1 Homo sapiens 46-49 34943229-14 2021 The review also discusses the role of interconversion of proline/glutamate/ornithine in supporting proline to PRODH/POX-dependent functions. Proline 57-64 proline dehydrogenase 1 Homo sapiens 110-115 34943229-14 2021 The review also discusses the role of interconversion of proline/glutamate/ornithine in supporting proline to PRODH/POX-dependent functions. Proline 57-64 proline dehydrogenase 1 Homo sapiens 116-119 34943229-14 2021 The review also discusses the role of interconversion of proline/glutamate/ornithine in supporting proline to PRODH/POX-dependent functions. Proline 99-106 proline dehydrogenase 1 Homo sapiens 110-115 34943229-14 2021 The review also discusses the role of interconversion of proline/glutamate/ornithine in supporting proline to PRODH/POX-dependent functions. Proline 99-106 proline dehydrogenase 1 Homo sapiens 116-119 34085157-2 2021 POX expression and proline availability are considered an underlying mechanism for differential POX functions. Proline 19-26 proline dehydrogenase 1 Homo sapiens 96-99 34085157-1 2021 Proline oxidase (POX) is mitochondrial proline-degrading enzyme of dual apoptosis/survival function. Proline 39-46 proline dehydrogenase 1 Homo sapiens 0-15 34085157-1 2021 Proline oxidase (POX) is mitochondrial proline-degrading enzyme of dual apoptosis/survival function. Proline 39-46 proline dehydrogenase 1 Homo sapiens 17-20 34283310-2 2021 Proline dehydrogenase (PRODH) enzyme, which catalyzes the first step of proline catabolism, has diverse functional roles in regulating many pathophysiological processes, including apoptosis, autophagy, cell senescence, and cancer metastasis. Proline 72-79 proline dehydrogenase 1 Homo sapiens 0-21 34283310-2 2021 Proline dehydrogenase (PRODH) enzyme, which catalyzes the first step of proline catabolism, has diverse functional roles in regulating many pathophysiological processes, including apoptosis, autophagy, cell senescence, and cancer metastasis. Proline 72-79 proline dehydrogenase 1 Homo sapiens 23-28 34390414-8 2021 The degradation of proline occurs in the mitochondria and involves an oxidation step catalyzed by proline dehydrogenase/proline oxidase (PRODH/POX). Proline 19-26 proline dehydrogenase 1 Homo sapiens 137-142 34752700-3 2021 Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. Proline 161-168 proline dehydrogenase 1 Homo sapiens 11-32 34752700-3 2021 Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. Proline 161-168 proline dehydrogenase 1 Homo sapiens 259-280 34752700-3 2021 Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. Proline 161-168 proline dehydrogenase 1 Homo sapiens 282-287 34752700-3 2021 Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. Proline 193-200 proline dehydrogenase 1 Homo sapiens 11-32 34752700-3 2021 Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. Proline 193-200 proline dehydrogenase 1 Homo sapiens 259-280 34752700-3 2021 Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. Proline 193-200 proline dehydrogenase 1 Homo sapiens 282-287 34752700-4 2021 PutA is shown here to catalyze the FAD-dependent PRODH oxidation of both T4C and T2C with catalytic efficiencies significantly higher than with proline. Proline 144-151 proline dehydrogenase 1 Homo sapiens 49-54 34769188-9 2021 The conversion of P5C to proline is catalyzed by P5C reductase (PYCR), while proline to P5C by proline dehydrogenase/oxidase (PRODH/POX). Proline 25-32 proline dehydrogenase 1 Homo sapiens 126-131 34769188-9 2021 The conversion of P5C to proline is catalyzed by P5C reductase (PYCR), while proline to P5C by proline dehydrogenase/oxidase (PRODH/POX). Proline 77-84 proline dehydrogenase 1 Homo sapiens 126-131 34682765-4 2021 PRODH/POX degrades proline yielding reactive oxygen species (ROS). Proline 19-26 proline dehydrogenase 1 Homo sapiens 0-5 34682765-4 2021 PRODH/POX degrades proline yielding reactive oxygen species (ROS). Proline 19-26 proline dehydrogenase 1 Homo sapiens 6-9 34682765-9 2021 The data suggest that TGZ-induced apoptosis in MDA-MB-231 cells cultured in medium without estradiol or deprived of ERbeta is mediated by PRODH/POX and the process is facilitated by proline availability for PRODH/POX by TGZ-dependent inhibition of collagen biosynthesis. Proline 182-189 proline dehydrogenase 1 Homo sapiens 207-212 34682765-9 2021 The data suggest that TGZ-induced apoptosis in MDA-MB-231 cells cultured in medium without estradiol or deprived of ERbeta is mediated by PRODH/POX and the process is facilitated by proline availability for PRODH/POX by TGZ-dependent inhibition of collagen biosynthesis. Proline 182-189 proline dehydrogenase 1 Homo sapiens 213-216 34577574-11 2021 In MCF-7 breast cancer cells, Cx affected proline metabolism through upregulation of proline biosynthesis, PRODH/POX and PYCRs expressions, PEPD activity, and downregulation of collagen biosynthesis. Proline 42-49 proline dehydrogenase 1 Homo sapiens 107-112 34577574-11 2021 In MCF-7 breast cancer cells, Cx affected proline metabolism through upregulation of proline biosynthesis, PRODH/POX and PYCRs expressions, PEPD activity, and downregulation of collagen biosynthesis. Proline 42-49 proline dehydrogenase 1 Homo sapiens 113-116 34067570-7 2021 Additionally, proline dose-dependently enhanced the mRNA expression of proline transporters (solute carrier family (SLC) 6A20, SLC36A1, SLC36A2, SLC38A1, and SLC38A2), elevated proline concentration, and protein abundance of proline dehydrogenase (PRODH). Proline 14-21 proline dehydrogenase 1 Homo sapiens 225-246 34067570-7 2021 Additionally, proline dose-dependently enhanced the mRNA expression of proline transporters (solute carrier family (SLC) 6A20, SLC36A1, SLC36A2, SLC38A1, and SLC38A2), elevated proline concentration, and protein abundance of proline dehydrogenase (PRODH). Proline 14-21 proline dehydrogenase 1 Homo sapiens 248-253 35216470-2 2022 PRODH/POX is a mitochondrial enzyme-degrading proline that is implicated in the regulation of cancer cell survival/apoptosis. Proline 46-53 proline dehydrogenase 1 Homo sapiens 0-5 35216470-2 2022 PRODH/POX is a mitochondrial enzyme-degrading proline that is implicated in the regulation of cancer cell survival/apoptosis. Proline 46-53 proline dehydrogenase 1 Homo sapiens 6-9 35216470-7 2022 Of interest is an MET-dependent increase in the concentration of proline, which is a substrate for PRODH/POX. Proline 65-72 proline dehydrogenase 1 Homo sapiens 99-104 35216470-7 2022 Of interest is an MET-dependent increase in the concentration of proline, which is a substrate for PRODH/POX. Proline 65-72 proline dehydrogenase 1 Homo sapiens 105-108 35163433-4 2022 PRODH/POX is a mitochondrial enzyme that catalyzes proline degradation, during which ATP or reactive oxygen species (ROS) are generated. Proline 51-58 proline dehydrogenase 1 Homo sapiens 0-5 35163433-4 2022 PRODH/POX is a mitochondrial enzyme that catalyzes proline degradation, during which ATP or reactive oxygen species (ROS) are generated. Proline 51-58 proline dehydrogenase 1 Homo sapiens 6-9 35163433-6 2022 Simultaneously, the NSAIDs inhibited collagen biosynthesis, supporting proline for PRODH/POX-induced ROS-dependent apoptosis (as demonstrated by an increase in the expression of apoptosis markers). Proline 71-78 proline dehydrogenase 1 Homo sapiens 83-88 35163433-6 2022 Simultaneously, the NSAIDs inhibited collagen biosynthesis, supporting proline for PRODH/POX-induced ROS-dependent apoptosis (as demonstrated by an increase in the expression of apoptosis markers). Proline 71-78 proline dehydrogenase 1 Homo sapiens 89-92 35018940-0 2022 Structure-affinity relationships of reversible proline analog inhibitors targeting proline dehydrogenase. Proline 47-54 proline dehydrogenase 1 Homo sapiens 83-104 35018940-1 2022 Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent oxidation of L-proline to Delta1-pyrroline-5-carboxylate. Proline 58-65 proline dehydrogenase 1 Homo sapiens 0-21 35018940-1 2022 Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent oxidation of L-proline to Delta1-pyrroline-5-carboxylate. Proline 58-65 proline dehydrogenase 1 Homo sapiens 23-28 35018940-1 2022 Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent oxidation of L-proline to Delta1-pyrroline-5-carboxylate. Proline 109-118 proline dehydrogenase 1 Homo sapiens 0-21 35018940-1 2022 Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent oxidation of L-proline to Delta1-pyrroline-5-carboxylate. Proline 109-118 proline dehydrogenase 1 Homo sapiens 23-28 35018940-3 2022 Here, we studied the inhibition of PRODH by 18 proline-like compounds to understand the structural and chemical features responsible for the affinity of the best-known inhibitor, S-(-)-tetrahydro-2-furoic acid (1). Proline 47-54 proline dehydrogenase 1 Homo sapiens 35-40 33646427-8 2021 Two of the enzymes in the proline biosynthetic pathway, pyrroline-5-carboxylate reductase (PYCR1) and Aldehyde Dehydrogenase 18 Family Member A1 (ALDH18A1), are upregulated in liver cancer of both human and animal models, while proline catabolic enzymes, such as proline dehydrogenase (PRODH) are downregulated. Proline 26-33 proline dehydrogenase 1 Homo sapiens 263-284 33646427-8 2021 Two of the enzymes in the proline biosynthetic pathway, pyrroline-5-carboxylate reductase (PYCR1) and Aldehyde Dehydrogenase 18 Family Member A1 (ALDH18A1), are upregulated in liver cancer of both human and animal models, while proline catabolic enzymes, such as proline dehydrogenase (PRODH) are downregulated. Proline 26-33 proline dehydrogenase 1 Homo sapiens 286-291 33646427-8 2021 Two of the enzymes in the proline biosynthetic pathway, pyrroline-5-carboxylate reductase (PYCR1) and Aldehyde Dehydrogenase 18 Family Member A1 (ALDH18A1), are upregulated in liver cancer of both human and animal models, while proline catabolic enzymes, such as proline dehydrogenase (PRODH) are downregulated. Proline 228-235 proline dehydrogenase 1 Homo sapiens 263-284 33646427-8 2021 Two of the enzymes in the proline biosynthetic pathway, pyrroline-5-carboxylate reductase (PYCR1) and Aldehyde Dehydrogenase 18 Family Member A1 (ALDH18A1), are upregulated in liver cancer of both human and animal models, while proline catabolic enzymes, such as proline dehydrogenase (PRODH) are downregulated. Proline 228-235 proline dehydrogenase 1 Homo sapiens 286-291 33424902-4 2020 The difficulty to isolate ProDH in active form has led several researchers to erroneously report proline-dependent NAD+ reduction at pH 10 as ProDH activity. Proline 97-104 proline dehydrogenase 1 Homo sapiens 26-31 33424902-4 2020 The difficulty to isolate ProDH in active form has led several researchers to erroneously report proline-dependent NAD+ reduction at pH 10 as ProDH activity. Proline 97-104 proline dehydrogenase 1 Homo sapiens 142-147 33294127-4 2020 Proline dehydrogenase (PRODH) is located on the inner mitochondrial membrane and is an enzyme that catalyzes the first step of proline catabolism, which plays an important role in improving the cellular redox state. Proline 127-134 proline dehydrogenase 1 Homo sapiens 0-21 33294127-4 2020 Proline dehydrogenase (PRODH) is located on the inner mitochondrial membrane and is an enzyme that catalyzes the first step of proline catabolism, which plays an important role in improving the cellular redox state. Proline 127-134 proline dehydrogenase 1 Homo sapiens 23-28 33294127-6 2020 This study is aimed at investigating whether enhancing proline metabolism by overexpressing PRODH can ameliorate hypoxia-induced injury in cardiomyocytes and to reveal the related altered metabolites and mechanistic pathway via untargeted metabolomics analysis. Proline 55-62 proline dehydrogenase 1 Homo sapiens 92-97 33294127-7 2020 Methods and Results: First, through public database analysis and RT-qPCR and western blot analyses in a cardiomyocyte hypoxia model, we found that the expression of the proline-degrading enzyme PRODH was downregulated after myocardial infarction and hypoxia exposure. Proline 169-176 proline dehydrogenase 1 Homo sapiens 194-199 33294127-9 2020 Enhanced proline metabolism induced by PRODH overexpression reduced the levels of reactive oxidative stress and apoptosis, whereas PRODH knockdown had the opposite effects. Proline 9-16 proline dehydrogenase 1 Homo sapiens 39-44 33083024-2 2020 Pyrroline-5-carboxylate reductase (PYCR) and proline dehydrogenase (PRODH) enzymes, which catalyze the last step in proline biosynthesis and the first step of its catabolism, respectively, have been extensively associated with the progression of several malignancies, and have been exposed as potential targets for anticancer drug development. Proline 45-52 proline dehydrogenase 1 Homo sapiens 68-73 32710395-3 2020 PRODH/POX catalyzes conversion of proline into Delta1-pyrroline-5-carboxylate releasing ATP or reactive oxygen species for autophagy/apoptosis. Proline 34-41 proline dehydrogenase 1 Homo sapiens 0-5 32918543-1 2020 BACKGROUND/AIMS: Proline availability for proline dehydrogenase/proline oxidase (PRODH/POX) may represent switching mechanism between PRODH/POX-dependent apoptosis and autophagy. Proline 17-24 proline dehydrogenase 1 Homo sapiens 81-86 32918543-1 2020 BACKGROUND/AIMS: Proline availability for proline dehydrogenase/proline oxidase (PRODH/POX) may represent switching mechanism between PRODH/POX-dependent apoptosis and autophagy. Proline 17-24 proline dehydrogenase 1 Homo sapiens 134-139 32918543-4 2020 In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE). Proline 22-29 proline dehydrogenase 1 Homo sapiens 34-39 32918543-4 2020 In order to targeting proline for PRODH/POX-dependent pathways substrate for prolidase, glycyl-proline (GP) was provided and proline utilization for collagen biosynthesis was blocked using 2-methoxyestradiol (MOE). Proline 95-102 proline dehydrogenase 1 Homo sapiens 34-39 32159324-1 2020 Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Delta1-pyrroline-5-carboxylate. Proline 58-65 proline dehydrogenase 1 Homo sapiens 0-21 32159324-1 2020 Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Delta1-pyrroline-5-carboxylate. Proline 58-65 proline dehydrogenase 1 Homo sapiens 23-28 32159324-1 2020 Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Delta1-pyrroline-5-carboxylate. Proline 120-129 proline dehydrogenase 1 Homo sapiens 0-21 32159324-1 2020 Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Delta1-pyrroline-5-carboxylate. Proline 120-129 proline dehydrogenase 1 Homo sapiens 23-28 32159324-3 2020 Here we show that the proline analogue thiazolidine-2-carboxylate (T2C) is a mechanism-based inactivator of PRODH. Proline 22-29 proline dehydrogenase 1 Homo sapiens 108-113 32159324-4 2020 Structures of the bifunctional proline catabolic enzyme proline utilization A (PutA) determined from crystals grown in the presence of T2C feature strong electron density for a 5-membered ring species resembling l-T2C covalently bound to the N5 of the FAD in the PRODH domain. Proline 31-38 proline dehydrogenase 1 Homo sapiens 263-268 32159324-4 2020 Structures of the bifunctional proline catabolic enzyme proline utilization A (PutA) determined from crystals grown in the presence of T2C feature strong electron density for a 5-membered ring species resembling l-T2C covalently bound to the N5 of the FAD in the PRODH domain. Proline 56-63 proline dehydrogenase 1 Homo sapiens 263-268 32159324-10 2020 These results may inform the design of new mechanism-based inactivators of PRODH for use as chemical probes to study the roles of proline metabolism in cancer. Proline 130-137 proline dehydrogenase 1 Homo sapiens 75-80 32213586-3 2020 PYCR converts the P5C intermediate to proline as a biosynthesis pathway, whereas proline dehydrogenase (PRODH) breaks down proline to P5C as a degradation pathway. Proline 81-88 proline dehydrogenase 1 Homo sapiens 104-109 32213586-4 2020 Intriguingly, expressions of proline biosynthesis PYCR gene and proline degradation PRODH gene are up-regulated directly by c-Myc oncoprotein and p53 tumor suppressor, respectively, suggesting that the proline-P5C metabolic axis is a key checkpoint for tumor cell growth. Proline 64-71 proline dehydrogenase 1 Homo sapiens 84-89 32213586-4 2020 Intriguingly, expressions of proline biosynthesis PYCR gene and proline degradation PRODH gene are up-regulated directly by c-Myc oncoprotein and p53 tumor suppressor, respectively, suggesting that the proline-P5C metabolic axis is a key checkpoint for tumor cell growth. Proline 64-71 proline dehydrogenase 1 Homo sapiens 84-89 31933109-3 2020 They are substrates for production of pyrroline-5-carboxylate which is the product of conversion of proline by proline dehydrogenase/ proline oxidase (PRODH/POX) to produce ATP for protective autophagy or reactive oxygen species for apoptosis. Proline 100-107 proline dehydrogenase 1 Homo sapiens 151-156 31933109-3 2020 They are substrates for production of pyrroline-5-carboxylate which is the product of conversion of proline by proline dehydrogenase/ proline oxidase (PRODH/POX) to produce ATP for protective autophagy or reactive oxygen species for apoptosis. Proline 100-107 proline dehydrogenase 1 Homo sapiens 157-160 31933109-4 2020 Interconversion of proline, ornithine, and glutamate may therefore regulate PRODH/POX-dependent apoptosis/autophagy. Proline 19-26 proline dehydrogenase 1 Homo sapiens 76-81 31933109-4 2020 Interconversion of proline, ornithine, and glutamate may therefore regulate PRODH/POX-dependent apoptosis/autophagy. Proline 19-26 proline dehydrogenase 1 Homo sapiens 82-85 31933109-9 2020 Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process). Proline 0-7 proline dehydrogenase 1 Homo sapiens 25-30 31933109-9 2020 Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process). Proline 0-7 proline dehydrogenase 1 Homo sapiens 31-34 31933109-9 2020 Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process). Proline 117-124 proline dehydrogenase 1 Homo sapiens 25-30 31933109-9 2020 Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process). Proline 117-124 proline dehydrogenase 1 Homo sapiens 31-34 31933109-9 2020 Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process). Proline 168-175 proline dehydrogenase 1 Homo sapiens 25-30 31933109-9 2020 Proline availability for PRODH/POX-dependent apoptosis/autophagy is regulated at the level of collagen biosynthesis (proline utilizing process) and prolidase activity (proline supporting process). Proline 168-175 proline dehydrogenase 1 Homo sapiens 31-34 31559416-3 2019 Proline oxidase, also known as proline dehydrogenase (POX/PRODH), is a key enzyme in the proline metabolism pathway and plays a vital role in tumorigenesis. Proline 31-38 proline dehydrogenase 1 Homo sapiens 54-57 31559416-3 2019 Proline oxidase, also known as proline dehydrogenase (POX/PRODH), is a key enzyme in the proline metabolism pathway and plays a vital role in tumorigenesis. Proline 31-38 proline dehydrogenase 1 Homo sapiens 58-63 31229682-2 2019 One of the genes located in the deleted region of 22q11DS is Proline Dehydrogenase (PRODH) which is important for conversion of proline to glutamate. Proline 128-135 proline dehydrogenase 1 Homo sapiens 61-82 31229682-2 2019 One of the genes located in the deleted region of 22q11DS is Proline Dehydrogenase (PRODH) which is important for conversion of proline to glutamate. Proline 128-135 proline dehydrogenase 1 Homo sapiens 84-89 28990412-1 2019 SIGNIFICANCE: Proline catabolism refers to the 4-electron oxidation of proline to glutamate catalyzed by the enzymes proline dehydrogenase (PRODH) and l-glutamate gamma-semialdehyde dehydrogenase (GSALDH, or ALDH4A1). Proline 14-21 proline dehydrogenase 1 Homo sapiens 117-138 28990412-1 2019 SIGNIFICANCE: Proline catabolism refers to the 4-electron oxidation of proline to glutamate catalyzed by the enzymes proline dehydrogenase (PRODH) and l-glutamate gamma-semialdehyde dehydrogenase (GSALDH, or ALDH4A1). Proline 14-21 proline dehydrogenase 1 Homo sapiens 140-145 28990412-1 2019 SIGNIFICANCE: Proline catabolism refers to the 4-electron oxidation of proline to glutamate catalyzed by the enzymes proline dehydrogenase (PRODH) and l-glutamate gamma-semialdehyde dehydrogenase (GSALDH, or ALDH4A1). Proline 71-78 proline dehydrogenase 1 Homo sapiens 117-138 28990412-1 2019 SIGNIFICANCE: Proline catabolism refers to the 4-electron oxidation of proline to glutamate catalyzed by the enzymes proline dehydrogenase (PRODH) and l-glutamate gamma-semialdehyde dehydrogenase (GSALDH, or ALDH4A1). Proline 71-78 proline dehydrogenase 1 Homo sapiens 140-145 28990412-3 2019 In some bacteria, PRODH and GSALDH are combined into a bifunctional enzyme known as proline utilization A (PutA). Proline 84-91 proline dehydrogenase 1 Homo sapiens 18-23 29648801-4 2018 The degradation of proline occurs in the mitochondrion and involves two oxidative steps catalyzed by proline dehydrogenase (PRODH) and GSAL dehydrogenase (GSALDH). Proline 19-26 proline dehydrogenase 1 Homo sapiens 101-122 29648801-4 2018 The degradation of proline occurs in the mitochondrion and involves two oxidative steps catalyzed by proline dehydrogenase (PRODH) and GSAL dehydrogenase (GSALDH). Proline 19-26 proline dehydrogenase 1 Homo sapiens 124-129 29648801-5 2018 PRODH is a flavin-dependent enzyme that couples proline oxidation with reduction of membrane-bound quinone, while GSALDH catalyzes the NAD+-dependent oxidation of GSAL to glutamate. Proline 48-55 proline dehydrogenase 1 Homo sapiens 0-5 29648801-6 2018 PRODH and PYCR form a metabolic relationship known as the proline-P5C cycle, a novel pathway that impacts cellular growth and death pathways. Proline 58-65 proline dehydrogenase 1 Homo sapiens 0-5 29648801-9 2018 A major challenge in the field is to discover inhibitors that specifically target PRODH and PYCR isoforms for use as tools for studying proline metabolism and the functions of the proline-P5C cycle in cancer. Proline 136-143 proline dehydrogenase 1 Homo sapiens 82-87 29648801-9 2018 A major challenge in the field is to discover inhibitors that specifically target PRODH and PYCR isoforms for use as tools for studying proline metabolism and the functions of the proline-P5C cycle in cancer. Proline 180-187 proline dehydrogenase 1 Homo sapiens 82-87 29681859-7 2018 These data suggest that polyphenols of propolis induce PRODH/POX-dependent apoptosis through up-regulation of mitochondrial proline degradation and down-regulation of proline utilization for collagen biosynthesis. Proline 124-131 proline dehydrogenase 1 Homo sapiens 55-60 29681859-7 2018 These data suggest that polyphenols of propolis induce PRODH/POX-dependent apoptosis through up-regulation of mitochondrial proline degradation and down-regulation of proline utilization for collagen biosynthesis. Proline 124-131 proline dehydrogenase 1 Homo sapiens 61-64 29681859-7 2018 These data suggest that polyphenols of propolis induce PRODH/POX-dependent apoptosis through up-regulation of mitochondrial proline degradation and down-regulation of proline utilization for collagen biosynthesis. Proline 167-174 proline dehydrogenase 1 Homo sapiens 55-60 29568391-1 2018 Proline degradation by proline dehydrogenase/proline oxidase (PRODH/POX) contributes to apoptosis or autophagy. Proline 0-7 proline dehydrogenase 1 Homo sapiens 62-71 28863383-2 2017 Previous studies suggested that this group of compounds affect prolidase activity (proline releasing enzyme from imidodipeptides) and collagen biosynthesis (proline utilizing process) providing substrate (proline) for proline oxidase (POX) dependent apoptosis. Proline 83-90 proline dehydrogenase 1 Homo sapiens 218-233 28863383-2 2017 Previous studies suggested that this group of compounds affect prolidase activity (proline releasing enzyme from imidodipeptides) and collagen biosynthesis (proline utilizing process) providing substrate (proline) for proline oxidase (POX) dependent apoptosis. Proline 157-164 proline dehydrogenase 1 Homo sapiens 218-233 28863383-2 2017 Previous studies suggested that this group of compounds affect prolidase activity (proline releasing enzyme from imidodipeptides) and collagen biosynthesis (proline utilizing process) providing substrate (proline) for proline oxidase (POX) dependent apoptosis. Proline 157-164 proline dehydrogenase 1 Homo sapiens 235-238 28863383-10 2017 The data suggest that massive production of proline by proBet-dependent activation of prolidase and inhibition of proline utilization for collagen biosynthesis may represent mechanism for POX-dependent apoptosis in EA cells. Proline 44-51 proline dehydrogenase 1 Homo sapiens 188-191 28712849-3 2017 FAD-dependent proline dehydrogenase (PRODH) and NAD+-dependent glutamate semialdehyde dehydrogenase (GSALDH) convert proline to glutamate in two sequential oxidative steps. Proline 14-21 proline dehydrogenase 1 Homo sapiens 37-42 28492237-5 2017 We discover that proline catabolism via proline dehydrogenase (Prodh) supports growth of breast cancer cells in 3D culture. Proline 17-24 proline dehydrogenase 1 Homo sapiens 40-61 28492237-5 2017 We discover that proline catabolism via proline dehydrogenase (Prodh) supports growth of breast cancer cells in 3D culture. Proline 17-24 proline dehydrogenase 1 Homo sapiens 63-68 28942439-0 2017 Functional Consequences of Intracellular Proline Levels Manipulation Affecting PRODH/POX-Dependent Pro-Apoptotic Pathways in a Novel in Vitro Cell Culture Model. Proline 41-48 proline dehydrogenase 1 Homo sapiens 79-84 28942439-0 2017 Functional Consequences of Intracellular Proline Levels Manipulation Affecting PRODH/POX-Dependent Pro-Apoptotic Pathways in a Novel in Vitro Cell Culture Model. Proline 41-48 proline dehydrogenase 1 Homo sapiens 85-88 28942439-1 2017 BACKGROUND/AIMS: The effect of impaired intracellular proline availability for proline dehydrogenase/proline oxidase (PRODH/POX)-dependent apoptosis was studied. Proline 54-61 proline dehydrogenase 1 Homo sapiens 118-127 28942439-9 2017 RESULTS: PRODH/POX knockdown decreased DNA and collagen biosynthesis, whereas increased prolidase activity and intracellular proline level in MCF-7shPRODH/POX cells. Proline 125-132 proline dehydrogenase 1 Homo sapiens 9-14 28942439-9 2017 RESULTS: PRODH/POX knockdown decreased DNA and collagen biosynthesis, whereas increased prolidase activity and intracellular proline level in MCF-7shPRODH/POX cells. Proline 125-132 proline dehydrogenase 1 Homo sapiens 15-18 28942439-9 2017 RESULTS: PRODH/POX knockdown decreased DNA and collagen biosynthesis, whereas increased prolidase activity and intracellular proline level in MCF-7shPRODH/POX cells. Proline 125-132 proline dehydrogenase 1 Homo sapiens 155-158 28942439-12 2017 All the compounds inhibited collagen biosynthesis, increased prolidase activity and cytoplasmic proline level in MCF-7shPRODH/POX cells and contributed to the induction of pro-survival mode only in MCF-7shPRODH/POX cells. Proline 96-103 proline dehydrogenase 1 Homo sapiens 126-129 28942439-14 2017 CONCLUSION: PRODH/POX was confirmed as a driver of apoptosis and proved the eligibility of MCF-7shPRODH/POX cell line as a highly effective model to elucidate the different mechanisms underlying proline utilization or generation in PRODH/POX-dependent pro-apoptotic pathways. Proline 195-202 proline dehydrogenase 1 Homo sapiens 12-17 28942439-14 2017 CONCLUSION: PRODH/POX was confirmed as a driver of apoptosis and proved the eligibility of MCF-7shPRODH/POX cell line as a highly effective model to elucidate the different mechanisms underlying proline utilization or generation in PRODH/POX-dependent pro-apoptotic pathways. Proline 195-202 proline dehydrogenase 1 Homo sapiens 18-21 28942439-14 2017 CONCLUSION: PRODH/POX was confirmed as a driver of apoptosis and proved the eligibility of MCF-7shPRODH/POX cell line as a highly effective model to elucidate the different mechanisms underlying proline utilization or generation in PRODH/POX-dependent pro-apoptotic pathways. Proline 195-202 proline dehydrogenase 1 Homo sapiens 98-103 27622935-2 2016 The proline dehydrogenase (PRODH) gene, which encodes the enzyme that catalyzes proline catabolism, maps to human chromosome 22q11.2, a region conferring risk of schizophrenia. Proline 4-11 proline dehydrogenase 1 Homo sapiens 27-32 27040799-12 2016 PRODH/POX expression is often down-regulated in various tumors, limiting mitochondrial proline utilization to P5C. Proline 87-94 proline dehydrogenase 1 Homo sapiens 0-9 27040799-14 2016 Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis. Proline 0-7 proline dehydrogenase 1 Homo sapiens 25-30 27040799-14 2016 Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis. Proline 0-7 proline dehydrogenase 1 Homo sapiens 31-34 27040799-14 2016 Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis. Proline 119-126 proline dehydrogenase 1 Homo sapiens 25-30 27040799-14 2016 Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis. Proline 119-126 proline dehydrogenase 1 Homo sapiens 31-34 25666758-3 2015 Genetic variants at chromosome 22q11.2, located in and near PRODH (proline dehydrogenase), were associated with L-proline in plasma (beta=0.29; P=6.38 x 10(-10)). Proline 112-121 proline dehydrogenase 1 Homo sapiens 60-65 25666758-3 2015 Genetic variants at chromosome 22q11.2, located in and near PRODH (proline dehydrogenase), were associated with L-proline in plasma (beta=0.29; P=6.38 x 10(-10)). Proline 112-121 proline dehydrogenase 1 Homo sapiens 67-88 26598224-6 2015 Importantly, the reversal effect of proline was blocked by concomitant proline dehydrogenase/oxidase (PRODH/POX) knockdown. Proline 36-43 proline dehydrogenase 1 Homo sapiens 102-107 26598224-6 2015 Importantly, the reversal effect of proline was blocked by concomitant proline dehydrogenase/oxidase (PRODH/POX) knockdown. Proline 36-43 proline dehydrogenase 1 Homo sapiens 108-111 26330555-1 2015 Proline oxidase (POX) catalytically converts proline to pyrroline-5-carboxylate. Proline 45-52 proline dehydrogenase 1 Homo sapiens 0-15 26330555-1 2015 Proline oxidase (POX) catalytically converts proline to pyrroline-5-carboxylate. Proline 45-52 proline dehydrogenase 1 Homo sapiens 17-20 26055684-3 2015 One gene of particular interest is the gene coding for proline dehydrogenase (PRODH), an enzyme responsible for the conversion of proline into glutamate. Proline 55-62 proline dehydrogenase 1 Homo sapiens 78-83 26161086-3 2015 Mutants of Delta (1)-Pyrroline-5-Carboxylate Synthetase1 (P5CS1) and Proline Dehydrogenase1 (PDH1), key enzymes in proline synthesis and catabolism respectively, both have similar reductions in growth during controlled soil drying. Proline 115-122 proline dehydrogenase 1 Homo sapiens 69-91 26161086-3 2015 Mutants of Delta (1)-Pyrroline-5-Carboxylate Synthetase1 (P5CS1) and Proline Dehydrogenase1 (PDH1), key enzymes in proline synthesis and catabolism respectively, both have similar reductions in growth during controlled soil drying. Proline 115-122 proline dehydrogenase 1 Homo sapiens 93-97 26161086-6 2015 An example of this is immunoblot detection of P5CS1 and PDH1 showing that the Highly ABA-induced (HAI) protein phosphatase 2Cs (PP2Cs) have different effects on P5CS1 and PDH1 protein levels despite having similar increases in proline accumulation. Proline 227-234 proline dehydrogenase 1 Homo sapiens 56-60 26161086-6 2015 An example of this is immunoblot detection of P5CS1 and PDH1 showing that the Highly ABA-induced (HAI) protein phosphatase 2Cs (PP2Cs) have different effects on P5CS1 and PDH1 protein levels despite having similar increases in proline accumulation. Proline 227-234 proline dehydrogenase 1 Homo sapiens 171-175 25569235-9 2015 GWAS replicated three known loci in the metabolome wide significance: CPS1 with glycine (P-value = 1.27x10-32), PRODH with proline (P-value = 1.11x10-19), SLC16A9 with carnitine level (P-value = 4.81x10-14) and uncovered a novel association between DMGDH and dimethyl-glycine (P-value = 1.65x10-19) level. Proline 124-131 proline dehydrogenase 1 Homo sapiens 113-118 26553010-1 2015 Proline dehydrogenase/proline oxidase (PRODH/POX) is an enzyme catalyzing the first step of proline degradation, during which ROS and/or ATP is generated. Proline 22-29 proline dehydrogenase 1 Homo sapiens 39-48 25184115-10 2014 Thus proline oxidation by proline dehydrogenase drives superoxide/H2O2 production, but it does so mainly or exclusively by providing anaplerotic carbon for other mitochondrial dehydrogenases and not by producing superoxide/H2O2 directly. Proline 5-12 proline dehydrogenase 1 Homo sapiens 26-47 24787057-3 2014 PRODH maps to chromosome 22q11, a region conferring the highest known genetic risk of schizophrenia, and encodes proline oxidase, which catalyzes proline catabolism. Proline 113-120 proline dehydrogenase 1 Homo sapiens 0-5 24787057-9 2014 This study presents a mechanism by which 25(OH)D insufficiency confers risk of schizophrenia; via proline elevation due to reduced PRODH expression, and a concomitant dysregulation of neurotransmission. Proline 98-105 proline dehydrogenase 1 Homo sapiens 131-136 23861960-1 2013 The tumor suppressor p53 was previously shown to markedly up-regulate the expression of the PRODH gene, encoding the proline dehydrogenase (PRODH) enzyme, which catalyzes the first step in proline degradation. Proline 117-124 proline dehydrogenase 1 Homo sapiens 92-97 23861960-1 2013 The tumor suppressor p53 was previously shown to markedly up-regulate the expression of the PRODH gene, encoding the proline dehydrogenase (PRODH) enzyme, which catalyzes the first step in proline degradation. Proline 117-124 proline dehydrogenase 1 Homo sapiens 140-145 23861960-11 2013 This supports a deeper link between proteins of the p53-family and metabolic pathways, as PRODH modulates the balance of proline and glutamate levels and those of their derivative alpha-keto-glutarate (alpha-KG) under normal and pathological (tumor) conditions. Proline 121-128 proline dehydrogenase 1 Homo sapiens 90-95