Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome. - Wikidata - wikimedia - TriplyDB

Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome.

Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome.

http://www.wikidata.org/entity/Q39813739

about

New Insights into the Function of the Immunoproteasome in Immune and Nonimmune Cells New molecular targets in mantle cell lymphoma Elucidation of the α-keto-aldehyde binding mechanism: a lead structure motif for proteasome inhibition The immunoproteasome and viral infection: a complex regulator of inflammation Selective inhibition of the immunoproteasome by ligand-induced crosslinking of the active site Indolo-phakellins as β5-specific noncovalent proteasome inhibitors Selective Inhibition of the Immunoproteasome by Structure-Based Targeting of a Non-catalytic Cysteine A clinical update on the role of carfilzomib in the treatment of relapsed or refractory multiple myeloma Trial Watch: Proteasomal inhibitors for anticancer therapy Molecular mechanisms of bortezomib resistant adenocarcinoma cells Nitric oxide-dependent CYP2B degradation is potentiated by a cytokine-regulated pathway and utilizes the immunoproteasome subunit LMP2 Carfilzomib: a novel second-generation proteasome inhibitor Carfilzomib: A new proteasome inhibitor for relapsed or refractory multiple myeloma.A phase 2 single-center study of carfilzomib 56 mg/m2 with or without low-dose dexamethasone in relapsed multiple myeloma.Carfilzomib Triple Combination Therapy: A Review in Relapsed Multiple Myeloma.Antileukemic activity and mechanism of drug resistance to the marine Salinispora tropica proteasome inhibitor salinosporamide A (Marizomib).The pan-HDAC inhibitor vorinostat potentiates the activity of the proteasome inhibitor carfilzomib in human DLBCL cells in vitro and in vivo An open-label, single-arm, phase 2 (PX-171-004) study of single-agent carfilzomib in bortezomib-naive patients with relapsed and/or refractory multiple myeloma Assessing subunit dependency of the Plasmodium proteasome using small molecule inhibitors and active site probes A novel orally active proteasome inhibitor ONX 0912 triggers in vitro and in vivo cytotoxicity in multiple myeloma.An open-label, single-arm, phase 2 study of single-agent carfilzomib in patients with relapsed and/or refractory multiple myeloma who have been previously treated with bortezomib.Nature of pharmacophore influences active site specificity of proteasome inhibitors.Apigenin manipulates the ubiquitin-proteasome system to rescue estrogen receptor-β from degradation and induce apoptosis in prostate cancer cells.New insights, recent advances, and current challenges in the biological treatment of multiple myeloma.Combined inhibition of p97 and the proteasome causes lethal disruption of the secretory apparatus in multiple myeloma cells.Carfilzomib demonstrates broad anti-tumor activity in pre-clinical non-small cell and small cell lung cancer models.Emerging role of carfilzomib in treatment of relapsed and refractory lymphoid neoplasms and multiple myeloma.Molecular targeted approaches in mantle cell lymphoma.Elucidating the catalytic subunit composition of distinct proteasome subtypes: a crosslinking approach employing bifunctional activity-based probes.Oral proteasome inhibitor with strong preclinical efficacy in myeloma models.Subunit specific inhibitors of proteasomes and their potential for immunomodulation A selective inhibitor of the immunoproteasome subunit LMP2 induces apoptosis in PC-3 cells and suppresses tumour growth in nude mice.Paradoxical resistance of multiple myeloma to proteasome inhibitors by decreased levels of 19S proteasomal subunits.Selective depletion of tumour suppressors Deleted in Colorectal Cancer (DCC) and neogenin by environmental and endogenous serine proteases: linking diet and cancer Activity-based near-infrared fluorescent probe for LMP7: a chemical proteomics tool for the immunoproteasome in living cells.Discovery of Highly Selective Inhibitors of the Immunoproteasome Low Molecular Mass Polypeptide 2 (LMP2) Subunit.Mismatch in epitope specificities between IFNγ inflamed and uninflamed conditions leads to escape from T lymphocyte killing in melanoma.A phase 1/2 study of carfilzomib in Japanese patients with relapsed and/or refractory multiple myeloma The 39th David A. Karnofsky Lecture: bench-to-bedside translation of targeted therapies in multiple myeloma.The proteasome inhibitor carfilzomib functions independently of p53 to induce cytotoxicity and an atypical NF-κB response in chronic lymphocytic leukemia cells.

P2860

Q26774372-117F77E0-FAC4-4B17-9B54-D26E03C46BA0 Q26821766-A4160957-9EE5-4928-A513-12A7836E7C31 Q27666372-81C965D1-EBFC-4E01-BE06-F5D5DB677E0F Q27694656-02A1AAF3-AF31-4ACB-9EE0-9DB6438DDB1D Q27695633-465548E7-4AF2-4FDA-BB80-E1A5515D2F63 Q27697335-44164553-C342-469A-91BB-CD24137F20FE Q27702605-D444D347-C1A8-46A2-8AC1-639562D206AD Q28067148-8ACE2EA4-C852-4AE0-B5AD-2FF30A2FE69E Q28082910-EC5FCF31-0D47-4F4A-A7AB-EF5B34EF7702 Q28478538-4D05E070-0270-479B-92B4-C1E1E60D154F Q28584243-46756E2B-CD80-4448-B52D-A50A12364C7B Q33395298-931C4811-B84E-4E58-AE36-D52FC23D07FD Q33405119-69CAB2AB-053C-4554-96C6-DBE825645C19 Q33416105-B7E8A358-A856-4593-8595-6D2BB4A4E626 Q33430690-336E2DEB-DCE9-40B4-AD37-92A471F7E13D Q33742779-BC0CC66F-A2DB-468A-BDD3-48755BA4152C Q33896749-0353DC57-F97A-4D11-8498-6B49B5BFCD7B Q34008600-3E61A703-F548-4D44-988F-EA476F0E7760 Q34061291-BD324201-8ACB-4182-9462-CF960E24671D Q34134986-FBD85D23-4CAA-49DF-B93F-04A531DD543E Q34291281-CF3810A2-1C91-42BE-BE31-A1C517A157D2 Q34401062-CFFD542B-FB8A-428B-92CD-FBCF66536FB1 Q34448480-D459C14B-2C15-45B6-8087-FB07D3CC0A5B Q34773850-722FC87F-9D89-4586-B195-971058BB519E Q34999190-398A4EA5-954C-4D5E-B0F2-0AE2AFC40D1F Q35005087-FA860EB2-5F51-4F81-8844-A8BDA89A2693 Q35009005-6E35A7A7-E08A-463C-8892-0784F3D8E97C Q35127368-69EEEBB9-0C70-463E-9850-B27FB9BFF07D Q35555565-3908EC8D-D9CA-4268-A739-B2AC16A41F0B Q35969785-BC85DC04-5E6A-4FDF-9ACF-34E5CA26EDA1 Q36042649-EF088D06-4B44-4AA4-858F-20A8F2119258 Q36075303-34C557F8-47FD-451A-8C07-5DEAB56AED68 Q36150369-C9584DFE-0E25-4367-B55E-A11913FF1455 Q36156772-60F43B39-9398-4705-9A68-4DCE650C082E Q36201624-48718083-E692-407F-8258-C622E9A79BEE Q36354644-7A26897F-E10C-40FC-ADA4-A21244B0500A Q36583731-5E8CEB55-9276-4195-A189-C62CCDE06766 Q36671445-FF06AA29-77C2-40D9-A895-10772D8EDF75 Q36709283-E0053C48-3020-40D9-BC05-A38AE4E7AECF Q36815262-447E39F7-5A91-4B3A-B121-1A4D8655F6C5

P2860

Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome.

http://www.wikidata.org/entity/Q39813739

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

Carfilzomib can induce tumor c ...... ke activity of the proteasome.

@en

Carfilzomib can induce tumor c ...... ke activity of the proteasome.

@nl

type

label

Carfilzomib can induce tumor c ...... ke activity of the proteasome.

@en

Carfilzomib can induce tumor c ...... ke activity of the proteasome.

@nl

prefLabel

Carfilzomib can induce tumor c ...... ke activity of the proteasome.

@en

Carfilzomib can induce tumor c ...... ke activity of the proteasome.

@nl

P1433

Q39813739-AF645A87-1712-4303-BC5D-15B9474CDCE8

P1476

Q39813739-EFA85B89-9234-44C7-B040-11645F3A662C

P2093

Q39813739-097A9863-2BEE-4A1D-8769-FA606C218A23

Q39813739-15C34B77-33BD-45B2-929A-B2611B1023C1

Q39813739-4C79E4C2-8954-466F-A23A-1F597B3B0DB1

Q39813739-59918652-C1AC-45D6-B866-8BC5A31A3F09

Q39813739-79911A13-9F45-4D6E-A9BE-4F9D2EEB1E85

Q39813739-7EFCF1B2-BDE8-432D-A375-51A4A7122DCD

Q39813739-957E8FE0-137D-4085-9B86-86104B74A3F5

Q39813739-97B75276-DFAB-40B0-BB92-02726D0AAD23

Q39813739-A331F4EC-94BC-47C4-9C13-DE91B2307E8E

Q39813739-A5A7EB86-5A30-4B42-AFC2-AE7EDFF44C29

P304

Q39813739-F424682E-DC0E-4F80-B95D-23ECE27840E2

P31

Q39813739-9F23D8AE-14B5-4B3B-8C63-79F42A71CC6A

P356

Q39813739-F045E30D-94B3-47BA-8ED5-E01EE0B78B84

P407

Q39813739-E95B6A1C-A243-4150-BEBA-F5117963335E

P433

Q39813739-279453E2-F324-4DA6-BB7E-0A7BAB0E9D35

P478

Q39813739-1B0F71FF-21FA-406A-A2E0-4F8886184B8D

P50

Q39813739-43D5781E-639F-4F68-B3F7-2BEC259DE1CE

P577

Q39813739-BA41F1DB-E5DE-4D3F-88D6-F3674F763AB5

P5875

Q39813739-72761EFA-A047-47A7-B645-49EEC8395AAD

P698

Q39813739-41B22EF8-6570-4DCC-930B-FD8BFEE61AD5

P356

BLOOD-2009-05-223677

P1433

P1476

Carfilzomib can induce tumor c ...... ke activity of the proteasome.

@en

P2093

Catherine Sylvain

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

Erika Suzuki

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

Francesco Parlati

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

James B Lorens

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

Kevin D Shenk

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

Konstantin Levitsky

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

Mark K Bennett

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

Monette Aujay

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

Paulina Ruurs

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

Susan J Lee

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

P304

3439-3447

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

P31

scholarly article

P356

10.1182/BLOOD-2009-05-223677

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

P407

P433

16

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

P478

114

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

P50

David R Micklem

P577

2009-08-11T00:00:00Z

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

P5875

26733424

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

P698

19671918

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