Pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase - Wikidata - awgldk - TriplyDB

Pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase

Pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase

http://www.wikidata.org/entity/Q28288793

about

The metabolic advantage of tumor cells Arginine Metabolism in Bacterial Pathogenesis and Cancer Therapy Amino acid deprivation using enzymes as a targeted therapy for cancer and viral infections Overexpression of arginine transporter CAT-1 is associated with accumulation of L-arginine and cell growth in human colorectal cancer tissue Single amino acid arginine deprivation triggers prosurvival autophagic response in ovarian carcinoma SKOV3 A randomised phase II study of pegylated arginine deiminase (ADI-PEG 20) in Asian advanced hepatocellular carcinoma patients.Arginine deiminase augments the chemosensitivity of argininosuccinate synthetase-deficient pancreatic cancer cells to gemcitabine via inhibition of NF-κB signaling Arginine starvation-associated atypical cellular death involves mitochondrial dysfunction, nuclear DNA leakage, and chromatin autophagy.Arginine starvation impairs mitochondrial respiratory function in ASS1-deficient breast cancer cells.Increased expression of argininosuccinate synthetase protein predicts poor prognosis in human gastric cancer Arginine deprivation affects glioblastoma cell adhesion, invasiveness and actin cytoskeleton organization by impairment of β-actin arginylation.RNA interference of argininosuccinate synthetase restores sensitivity to recombinant arginine deiminase (rADI) in resistant cancer cells Bioengineered human arginase I with enhanced activity and stability controls hepatocellular and pancreatic carcinoma xenografts.Down-regulation of argininosuccinate synthetase is associated with cisplatin resistance in hepatocellular carcinoma cell lines: implications for PEGylated arginine deiminase combination therapy.Blocking autophagy enhanced cytotoxicity induced by recombinant human arginase in triple-negative breast cancer cells.Arginine deiminase PEG20 inhibits growth of small cell lung cancers lacking expression of argininosuccinate synthetase Negative argininosuccinate synthetase expression in melanoma tumours may predict clinical benefit from arginine-depleting therapy with pegylated arginine deiminase.Reduced expression of argininosuccinate synthetase 1 has a negative prognostic impact in patients with pancreatic ductal adenocarcinoma The Emerging Hallmarks of Cancer Metabolism Epigenetic status of argininosuccinate synthetase and argininosuccinate lyase modulates autophagy and cell death in glioblastoma.Differential expression of argininosuccinate synthetase in serous and non-serous ovarian carcinomas.Arginine deiminase as a novel therapy for prostate cancer induces autophagy and caspase-independent apoptosis.Arginase: an emerging key player in the mammalian immune system.A metabolic synthetic lethal strategy with arginine deprivation and chloroquine leads to cell death in ASS1-deficient sarcomas.Co-application of canavanine and irradiation uncouples anticancer potential of arginine deprivation from citrulline availability Targeted cellular metabolism for cancer chemotherapy with recombinant arginine-degrading enzymes.Targeting arginine-dependent cancers with arginine-degrading enzymes: opportunities and challenges.The role of arginine and the modified arginine deiminase enzyme ADI-PEG 20 in cancer therapy with special emphasis on Phase I/II clinical trials.Metabolic rewiring of pancreatic ductal adenocarcinoma: New routes to follow within the maze.Drug-induced amino acid deprivation as strategy for cancer therapy.Phase 1 Dose-Escalation Study of Pegylated Arginine Deiminase, Cisplatin, and Pemetrexed in Patients With Argininosuccinate Synthetase 1-Deficient Thoracic Cancers.Arginine dependence of tumor cells: targeting a chink in cancer's armor.Purification, immobilization, and biochemical characterization of l-arginine deiminase from thermophilic Aspergillus fumigatus KJ434941: anticancer activity in vitro.Pegylated arginine deiminase synergistically increases the cytotoxicity of gemcitabine in human pancreatic cancer Arginine-Dual roles as an onconutrient and immunonutrient.Metabolic Interactions in the Tumor Microenvironment.Single amino acid arginine starvation efficiently sensitizes cancer cells to canavanine treatment and irradiation.Bioengineered arginase I increases caspase-3 expression of hepatocellular and pancreatic carcinoma cells despite induction of argininosuccinate synthetase-1.Recombinant human arginase inhibits the in vitro and in vivo proliferation of human melanoma by inducing cell cycle arrest and apoptosis.Genetic variation in SLC7A2 interacts with calcium and magnesium intakes in modulating the risk of colorectal polyps.

P2860

Q21245765-1373120B-AD69-4E65-B06C-4CBE6488B3D2 Q26765461-7C35733C-1ABE-4743-ADF9-08FFBC4FD7C1 Q30040775-FE37D542-D297-40F9-8515-BC2FEBEDEAE2 Q31139529-9826A014-008B-487D-A08C-D13C3B2CFAB7 Q33759388-3520B79C-73B6-43DB-A352-E04D6DEACF1E Q34250146-64EB54DF-4BC1-4FA7-A28C-E9BAE6C082FE Q34305783-C524004B-29ED-4989-858E-3779F1585BD4 Q34314481-2D428030-FBA0-4879-9FB6-65E685B8785C Q34497105-37C5CF45-A433-4EDB-8C2F-0127C76C9EE5 Q34626077-CE385928-2E34-4E6C-97D0-68E09B47ECB6 Q34807813-9539B2CD-6F89-49C8-95FF-7F5AE7D4292F Q34832425-11E27A9F-C944-4AE5-9FF8-124304E6A77B Q35015474-7D308FF8-B5B3-4140-B297-BA9871B7D339 Q35233239-7F78318E-80B4-4BC9-BDC5-B3CFA51D717C Q35679199-53B2A2F9-925B-485D-88EF-7DC3D27170AF Q35682009-AEB5B1EC-21DF-4385-9E48-FF8BE584A21B Q35927116-93675EBE-99A0-4526-8F54-BA9A03E3FA58 Q36277197-7FA6075D-3C6A-48C3-9F9F-7E7CAC7BAA0D Q36468964-94FF7092-55E8-4B3C-9EBF-195EC20E4DF0 Q36586507-A88097C6-FD15-453D-AFA6-B82251EE9395 Q36873800-DF8818ED-C4E8-4A86-9206-231A7BB9681C Q37068792-B39DA7DF-F8B9-4257-9846-EA231F9B912D Q37395887-CD05D547-03AB-4865-B4FF-A615BB77896D Q37465815-3C2CDE71-B0EA-4EE9-A5A1-2D423DCA0D62 Q37687381-B905AAB5-53EA-4145-9A44-B078B72748C1 Q37820202-D9DF39BC-28B0-45E0-83AD-C433648407DE Q38181070-B613A9D6-FCB3-457D-9EA9-B33BB14FE200 Q38223301-6F2F5EE2-AAD6-4D6F-B59C-21BD0CA8E5EC Q38366834-47B3AD62-6C2F-407D-826D-25BBA38895DE Q38657061-3B675571-1DB3-4E2D-A812-B0451B5AA404 Q38733577-408F5441-3757-49E3-A325-F014EF900658 Q38816145-5EBCB6F1-4193-46BC-B41D-6B5FAD0475C3 Q38920582-4DA6D978-64A9-4340-AC22-5384166F9186 Q38929570-E474353F-9E1C-4851-AFC3-06D4DA167608 Q39012828-8AAA75B8-39D5-438D-B750-CB13FD21B24D Q39452100-35D3687B-FD0A-4303-AF72-A5954832A57D Q39529376-AC63FCF2-D676-4AE3-96E2-45A6591949E6 Q39704277-4A635175-5CF8-411D-81CE-DE1F7C622DC2 Q39823199-68025404-6135-4FE1-8B42-A0BFE91B4962 Q40202441-D3E40C73-73FC-47FC-BFFB-A654D23161AA

P2860

Pancreatic cancer cell lines deficient in argininosuccinate synthetase are sensitive to arginine deprivation by arginine deiminase

http://www.wikidata.org/entity/Q28288793

description

2008 nî lūn-bûn

@nan

2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@ast

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@en

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@nl

type

label

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@ast

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@en

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@nl

prefLabel

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@ast

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@en

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@nl

P1433

Q28288793-0C6A5A9E-D2CE-4D6A-B82C-BCD748483A90

P1476

Q28288793-F82728B3-1AE1-4AD2-9857-3EEF1A1DB961

P2093

Q28288793-64C3F778-7528-4F17-9655-77281BAAAE81

Q28288793-83864039-52E6-4BC9-A78E-5A3ED4F5175C

Q28288793-8783F79A-A58E-4D5F-BBD5-B7F5CB588226

Q28288793-8FCEC24F-D7E8-42B8-B255-9ED95F7DBC7A

Q28288793-C8B25C24-054D-47D0-8818-84FE1C36DDFB

Q28288793-D7730E04-570F-4534-A58E-112426707228

Q28288793-F225ECB3-A4E8-4019-86A1-0F7B53EAF6B9

P2860

Q28288793-014BDC8C-927E-4DC2-A8B4-7B81B84B508A

Q28288793-068CEAB4-8A76-4C8D-BC3D-ED787AF52511

Q28288793-16F7F299-B33D-4F50-BBCA-F5C43A88180D

Q28288793-1C3F3262-FC8F-4CD3-9C98-1889C402E029

Q28288793-1E33AB4E-079D-4094-B986-F335BF51ECFF

Q28288793-2B9084EB-0302-45E1-AF18-A410B8EBFABB

Q28288793-2C41EBED-2B1B-4D0A-9A14-57FDEB8DA089

Q28288793-3371975A-FC44-41DA-A6E5-39A8143DC5D4

Q28288793-337993B1-18B9-4E7F-885E-2756CD95BC9C

Q28288793-42388140-2478-4D77-8674-D86B6BE69018

P304

Q28288793-B715E6FA-67AB-4866-8B71-BBB9504210BA

P31

Q28288793-2990E3A9-5037-4DFA-9761-C99D86522CA7

P3181

Q28288793-396EA4C3-DC22-46B8-883B-2648A2FE065A

P356

Q28288793-BFBA4E8E-2B60-43EE-8FCD-5D09202C55F7

P407

Q28288793-8CC774C3-706E-4638-A4CB-DAA19BB7B9B2

P433

Q28288793-17266C05-F2A6-418A-A987-BAE0AA6CAE93

P478

Q28288793-8986B2F3-B85A-446C-9657-8DD9EFB9EF52

P577

Q28288793-43FD0176-BB27-48CA-8DF5-5D74B9A6B596

P5875

Q28288793-30D7A17B-E159-47C0-B153-BA539A53B773

P698

Q28288793-99E81EDD-B83D-4F80-B2F2-DEE5296DEDB3

P932

Q28288793-F89638F6-4422-4107-AE5F-72FADF9FA5E8

P3181

P356

P1433

International Journal of Cancer

P1476

Pancreatic cancer cell lines d ...... rivation by arginine deiminase

@en

P2093

Colin M Parsons

http://www.w3.org/2001/XMLSchema#string

Hsing-Jien Kung

http://www.w3.org/2001/XMLSchema#string

Joseph Galante

http://www.w3.org/2001/XMLSchema#string

Randie Kim

http://www.w3.org/2001/XMLSchema#string

Richard J Bold

http://www.w3.org/2001/XMLSchema#string

Subbulakshmi Virudachalam

http://www.w3.org/2001/XMLSchema#string

Tawnya L Bowles

http://www.w3.org/2001/XMLSchema#string

P2860

Argininosuccinate synthetase from the urea cycle to the citrulline-NO cycle

Coinduction of nitric oxide synthase, argininosuccinate synthetase, and argininosuccinate lyase in lipopolysaccharide-treated rats. RNA blot, immunoblot, and immunohistochemical analyses

Isolation and characterization of argininosuccinate synthetase from human liver

Autophagy as a regulated pathway of cellular degradation

Autophagy: from phenomenology to molecular understanding in less than a decade

Almost all about citrulline in mammals.

Enzymes of arginine metabolism.

Another way to die: autophagic programmed cell death.

The best way to use asparaginase in childhood acute lymphatic leukaemia--still to be defined?

Autophagy as a cell death and tumor suppressor mechanism.

P304

1950-5

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

3023170

http://www.w3.org/2001/XMLSchema#string

P356

10.1002/IJC.23723

http://www.w3.org/2001/XMLSchema#string

P407

P433

8

http://www.w3.org/2001/XMLSchema#string

P478

123

http://www.w3.org/2001/XMLSchema#string

P577

2008-10-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

51432328

http://www.w3.org/2001/XMLSchema#string

P698

18661517

http://www.w3.org/2001/XMLSchema#string

P932

4294549

http://www.w3.org/2001/XMLSchema#string