An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract. - Wikidata - wikimedia - TriplyDB

An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract.

An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract.

http://www.wikidata.org/entity/Q37695132

about

The Ribonuclease A Superfamily in Humans: Canonical RNases as the Buttress of Innate Immunity A Review of Ribonuclease 7's Structure, Regulation, and Contributions to Host Defense RNase 7 in Cutaneous Defense Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles Ribonucleases 6 and 7 have antimicrobial function in the human and murine urinary tract.Human antimicrobial peptides and proteins α-Intercalated cells defend the urinary system from bacterial infection Renal intercalated cells sense and mediate inflammation via the P2Y14 receptor.Distinct α-intercalated cell morphology and its modification by acidosis define regions of the collecting duct.Amplifying renal immunity: the role of antimicrobial peptides in pyelonephritis.Insulin and the phosphatidylinositol 3-kinase signaling pathway regulate Ribonuclease 7 expression in the human urinary tract.Exploring the mechanisms of action of human secretory RNase 3 and RNase 7 against Candida albicans The potential of circulating cell-free RNA as a cancer biomarker: challenges and opportunities.Polyvinylsulfonic acid: A Low-cost RNase inhibitor for enhanced RNA preservation and cell-free protein translation.Immune Modulation by Human Secreted RNases at the Extracellular Space.

P2860

Q26741426-308DF248-CFBB-40A2-AE6C-BC46BADCD8C3 Q26752202-AEA49489-0A3B-46AE-B6CC-63511655437D Q26752767-3FFD52C0-12A8-4064-B7E4-EC1FE2ED9C18 Q27684378-C17B4306-1581-49DE-95A7-4A297C1502AD Q30032297-A3AEBC17-3B2A-43AA-92CD-D12AB05508C6 Q33673156-107224FF-11E9-4F0F-8482-41F0F1427632 Q33808284-5B3ACBEC-5CDC-454A-B153-CBA0DED71013 Q35208204-5D20B5BF-6F7C-4309-A3D5-41F55B58CA61 Q36017594-27D34B06-B736-4C4D-8413-5C0BDC30302A Q38543398-FCB630F7-1806-400E-A722-BAE3FA8948D3 Q39612821-C63CEF4D-4C56-4603-B5A2-AE78A371AA87 Q39699474-98C028A8-C5E6-4967-9C68-6B33195BFB68 Q47201290-DA5366DD-6C52-4B58-94FE-2FDA235F978F Q47974213-E0C981F2-3500-4C89-8666-55690C7E1E6A Q55255353-97A48707-4A63-4E9B-B23C-5CB7FA11B9F1

P2860

An endogenous ribonuclease inhibitor regulates the antimicrobial activity of ribonuclease 7 in the human urinary tract.

http://www.wikidata.org/entity/Q37695132

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 09 October 2013

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

An endogenous ribonuclease inh ...... 7 in the human urinary tract.

@en

An endogenous ribonuclease inh ...... 7 in the human urinary tract.

@nl

type

label

An endogenous ribonuclease inh ...... 7 in the human urinary tract.

@en

An endogenous ribonuclease inh ...... 7 in the human urinary tract.

@nl

prefLabel

An endogenous ribonuclease inh ...... 7 in the human urinary tract.

@en

An endogenous ribonuclease inh ...... 7 in the human urinary tract.

@nl

P1433

Q37695132-3FE1588B-F5F2-489B-A8AA-CE4039330E9F

P1476

Q37695132-0770D777-3C50-4C65-A690-4110796DCC26

P2093

Q37695132-2E6E20FE-17D2-437B-B5DD-2D7C88A27F79

Q37695132-49B37E42-0254-459F-B550-FD5692FEBB6C

Q37695132-58184BF0-68DA-46D0-B880-4A3394956581

Q37695132-650422D5-2776-4676-A469-160F6D7793EB

Q37695132-6716E14B-4AA5-4D22-AFD4-7EA1B8147C56

Q37695132-846C24DF-F7E1-4886-9AF9-DEF4685A3E4C

P2860

Q37695132-0BD456CC-4BC8-4401-8404-740220E8574B

Q37695132-0D0068FC-BC6B-4B2C-A808-C15F6E90B767

Q37695132-14559A20-BDDE-46F2-B74A-876E3ADB2BD8

Q37695132-18F13AA1-2598-48B0-A395-73825263F251

Q37695132-1F2EC501-313C-40F5-A39C-046F0088155B

Q37695132-1F561F0F-59B6-45C3-8AA4-E2CA98F9D2CB

Q37695132-27842859-5D33-47F2-AB86-59CB2A894362

Q37695132-2A3A8AB8-9A17-4929-B1FA-7D5B6D7D8CB1

Q37695132-2AE45B8B-E905-4036-968F-2665119630A8

Q37695132-32A23D37-CCF4-434F-A52D-0C7C431EDD83

P2888

Q37695132-BF2C90FB-3454-483E-BE0F-B890ED2EF62A

P304

Q37695132-C10E8822-005B-4A95-9093-F6B3C330AA62

P31

Q37695132-E8428B80-AF4E-43BF-83BA-C49EA0014321

P356

Q37695132-6F3475DA-5D70-4F85-BDF9-9570150F1BE4

P407

Q37695132-68FD975C-E341-476D-BCC4-E61CC3E40562

P433

Q37695132-00E75A01-F7CB-44EC-9CAE-76CEE14AF64A

P478

Q37695132-1C864B6B-BB1C-4843-8BCD-546BA5B8C586

P50

Q37695132-152DCC1F-1AA1-400C-A03E-3F0FF111A58B

Q37695132-B4CE02CA-98E7-4D73-9868-43D27F7F2E70

P577

Q37695132-0CD38CA4-E24D-4F3A-9260-E2AD2107E807

P5875

Q37695132-53700B2D-D23B-4E5B-8B8E-66E88E20F236

P6179

Q37695132-D33A72E7-BE20-449A-8A3E-2974874F699D

P698

Q37695132-DF02E019-5589-4EED-A418-B31419D39AE8

P932

Q37695132-D2DF85F6-D139-4098-8704-B3F7A2994B9A

P356

P1433

Kidney International

P1476

An endogenous ribonuclease inh ...... 7 in the human urinary tract.

@en

P2093

Andrew L Schwaderer

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

Daniel M Cohen

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

Jennifer Kline

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

John D Spencer

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

Sheryl S Justice

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

Tad Eichler

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

P2860

RNase 7 contributes to the cutaneous defense against Enterococcus faecium

Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein

Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall

Kallikrein-mediated proteolysis regulates the antimicrobial effects of cathelicidins in skin

RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin

Ribonuclease 7, an antimicrobial peptide upregulated during infection, contributes to microbial defense of the human urinary tract

The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity

Crystal structure of RNase A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor

Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats

Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans

P2888

P304

1179-1191

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

P31

scholarly article

P356

10.1038/KI.2013.395

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

P407

P433

5

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

P478

85

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

P50

P577

2013-10-09T00:00:00Z

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

P5875

257598817

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

P6179

1020376197

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

P698

24107847

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

P932

3981961

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