Competition for zinc binding in the host-pathogen interaction - Test2 - elhamkhani - TriplyDB

Competition for zinc binding in the host-pathogen interaction

Competition for zinc binding in the host-pathogen interaction

http://www.wikidata.org/entity/Q27001616

about

The Zinc Transport Systems and Their Regulation in Pathogenic Fungi Iron and zinc exploitation during bacterial pathogenesis ZnuA and zinc homeostasis in Pseudomonas aeruginosa The Hexahistidine Motif of Host-Defense Protein Human Calprotectin Contributes to Zinc Withholding and Its Functional Versatility The Yersinia pestis siderophore, yersiniabactin, and the ZnuABC system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice.The ins and outs of bacterial iron metabolism.Type VI Secretion System Transports Zn2+ to Combat Multiple Stresses and Host Immunity.Dual Zinc Transporter Systems in Vibrio cholerae Promote Competitive Advantages over Gut Microbiome.The capability of Pseudomonas aeruginosa to recruit zinc under conditions of limited metal availability is affected by inactivation of the ZnuABC transporter.The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD.Attenuated mutant strain of Salmonella Typhimurium lacking the ZnuABC transporter contrasts tumor growth promoting anti-cancer immune response.The extracellular proteome of two Bifidobacterium species reveals different adaptation strategies to low iron conditions Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase Bacterial Metabolism Shapes the Host-Pathogen Interface Epidemiology and risk factors for IBD.Zinc transporters YbtX and ZnuABC are required for the virulence of Yersinia pestis in bubonic and pneumonic plague in mice.Zinc Homeostasis at the Bacteria/Host Interface-From Coordination Chemistry to Nutritional Immunity.The ZIP family zinc transporters support the virulence of Cryptococcus neoformans.Growth of Pseudomonas aeruginosa in zinc poor environments is promoted by a nicotianamine-related metallophore.Salmonella utilizes zinc to subvert anti-microbial host defense of macrophages via modulation of NF-κB signaling.Nickel Sequestration by the Host-Defense Protein Human Calprotectin.Role of Metal-Dependent Regulation of ESX-3 Secretion in Intracellular Survival of Mycobacterium tuberculosis.Interplay between copper and zinc homeostasis through the transcriptional regulator Zur in Enterococcus faecalis.Metal economy in host-microbe interactions.The Metallophore Staphylopine Enables Staphylococcus aureus To Compete with the Host for Zinc and Overcome Nutritional Immunity.Differential Effects of Iron, Zinc, and Copper on Dictyostelium discoideum Cell Growth and Resistance to Legionella pneumophila.Clinical Evolution of New Delhi Metallo-β-Lactamase (NDM) Optimizes Resistance under Zn(II) Deprivation.Mechanisms of zinc binding to the solute-binding protein AztC and transfer from the metallochaperone AztD.Fine control of metal concentrations is necessary for cells to discern zinc from cobalt.Zinc is required to ensure the expression of flagella and the ability to form biofilms in Salmonella enterica sv Typhimurium.Just When We Thought We Knew Everything We Needed To Know about Zn Acquisition and Bacterial Pathogenesis.Pseudomonas aeruginosa transcriptome during human infection.

P2860

Q26779734-741A68A0-0FD8-40EA-AEEC-B7EB31EA13C6 Q28082191-2B5BD24A-3AE4-4A60-85ED-E72FE7458230 Q28493182-AE6AD03B-CF74-4D0C-8613-3B1F3321CA41 Q28828870-D32C9BB3-30D4-46FC-A8AD-60EFFFA9032D Q34044097-282A698D-71FD-415D-A65B-1B0E659AEC15 Q34055559-9837AF9A-7A76-43E9-A264-053585232476 Q35680668-2ADBDF21-DD5D-4AC9-A886-23F34D2D6982 Q35701593-3113A4F1-85DB-4082-8548-5DF864131925 Q35732371-F89C3344-A7FD-4266-AB00-E7B0092DE2AB Q36018510-980D759A-2A72-4422-AD77-2CB30B3D5056 Q36232119-C4C47147-922A-4179-B135-A33251DD6B99 Q36243198-71FCE44E-92BC-4089-B34F-3C31B035514B Q37017171-30A661D0-4E30-4680-AE38-8A78075B04A4 Q37041802-6E00A7E3-CBC2-4ACD-A24B-341193F0224A Q38366954-1D5A8C74-EBAB-4B5C-AE4D-4B8E96C32BFE Q38765764-ED38F109-BD55-4390-AD5F-B28140961775 Q38935738-54865E67-D987-4CA4-B0BE-DD5582C59865 Q39818401-A9838787-52A5-46BE-B865-12442E6493E8 Q40051274-289B6333-FA03-4552-97AA-7ED273DFDC53 Q40065845-54B5EF5F-434E-46C6-97B6-B73D37FC0E0F Q40188001-EF129147-7CBC-4FF5-87BB-E11D97A5CCC7 Q40651569-592D3620-59A5-434C-A2C0-75C3860D5FD1 Q41022681-C7EBC959-0AFD-4FBC-AB4C-151CD700C27E Q43104111-CB9BD83E-D82E-46FA-AC52-E5452A3D3646 Q47098548-6903ECBB-71BE-4B68-8784-49B9CB07BC11 Q47551972-6E0C00E1-74AB-45AE-AB74-5CA6A74493E2 Q47737111-41B6B8CC-7041-4F68-863D-A2091FBAC04F Q47831694-5ED8ABD6-80D1-476F-9343-6468B8A7FD56 Q48206690-349F6ED0-EF67-486A-A929-B40CDA4505DA Q48307444-7751E114-C083-41EB-B742-5418F85AAA2C Q49588269-1DDC0FC2-F9B4-434F-A992-6F0F757A6B0C Q54212212-169FE039-819D-4D8F-B406-699554341D5E

P2860

Competition for zinc binding in the host-pathogen interaction

http://www.wikidata.org/entity/Q27001616

description

2013 nî lūn-bûn

@nan

2013 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Competition for zinc binding in the host-pathogen interaction

@ast

Competition for zinc binding in the host-pathogen interaction

@en

Competition for zinc binding in the host-pathogen interaction

@nl

type

label

Competition for zinc binding in the host-pathogen interaction

@ast

Competition for zinc binding in the host-pathogen interaction

@en

Competition for zinc binding in the host-pathogen interaction

@nl

prefLabel

Competition for zinc binding in the host-pathogen interaction

@ast

Competition for zinc binding in the host-pathogen interaction

@en

Competition for zinc binding in the host-pathogen interaction

@nl

P1433

Q27001616-4A8CF68A-6A27-4C52-930D-D8795F0EEC46

P1476

Q27001616-4E22FB46-4EE9-458A-9183-E08B3044BE4F

P2093

Q27001616-6677457F-C5BB-4177-8029-59F7CCC79274

Q27001616-B2F3DB7A-84B9-4539-9F64-400380E0C93B

P275

Q27001616-B43AFF36-8FAA-4A50-846C-623BE8DBA5E8

P2860

Q27001616-00357246-5BD9-4741-98EA-EA423C620EF0

Q27001616-0883CEEF-5BCB-4319-962D-AC6469C744B2

Q27001616-09289D2F-FEF7-404F-BA7A-5EA761DAEDC3

Q27001616-09C74A9B-39BB-45C3-B560-DB8511801854

Q27001616-09E3AA8B-0ECD-4F85-B27E-2BC58B05EA5F

Q27001616-09FCB416-3E83-4D5E-8F67-EF3A48C650ED

Q27001616-0E1FA0CC-1CC4-45B9-967E-56509C2BF561

Q27001616-0FA90D23-C76A-4CE2-AE8D-DB43B08C7930

Q27001616-135426C6-CE51-48D7-BD58-9E76E6D21513

Q27001616-156CBD98-0341-45F9-8A94-FDFFC48A43A6

P304

Q27001616-45D1BC71-71E3-48DE-B3C4-10FDB8B9A1DB

P31

Q27001616-B02B4FD4-621A-4D71-BE70-35EA55204AF9

Q27001616-D844E8BF-C237-435C-8B5F-BDA9C7C5852E

P3181

Q27001616-6B7E0E58-7332-4163-8BFD-4B1F4775A18A

P356

Q27001616-FF5E4C52-B8DC-4830-B3C1-9357626673E9

P407

Q27001616-5BB0229A-547B-420F-9E65-786085C181D4

P478

Q27001616-A0098836-2F44-42BC-A3B1-C995EC5B8D93

P50

Q27001616-C1EEB739-A29D-4693-BAA5-61C970F7212F

P577

Q27001616-092D11CD-31B6-4158-B518-F4B28C558661

Q27001616-3C94BEAC-F54C-4AD2-A385-96461A3D1A84

P5875

Q27001616-A14D6237-A8B8-4DD1-B551-0782861BE96E

P698

Q27001616-D646C90B-19D0-4E81-A26C-36E6859F75F5

P921

Q27001616-73FFFAB7-0FBC-48E0-9F76-0857FEF926AD

Q27001616-82494BF2-3728-4AAC-9CBB-D3E678A508A2

P932

Q27001616-78D72BF4-8CF7-4902-B562-364780DFADD5

P3181

P356

FCIMB.2013.00108

P1433

Frontiers in cellular and infection microbiology

P1476

Competition for zinc binding in the host-pathogen interaction

@en

P2093

Mauro Cerasi

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

Serena Ammendola

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

P275

Creative Commons Attribution 3.0 Unported

P2860

Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection

Granulocyte macrophage-colony stimulating factor induced Zn sequestration enhances macrophage superoxide and limits intracellular pathogen survival

The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase

Identification of an Acinetobacter baumannii zinc acquisition system that facilitates resistance to calprotectin-mediated zinc sequestration

Structural determinants of metal specificity in the zinc transport protein ZnuA from synechocystis 6803

Crystal structure and function of the zinc uptake regulator FurB from Mycobacterium tuberculosis

Structural Analysis of ABC-family Periplasmic Zinc Binding Protein Provides New Insights Into Mechanism of Ligand Uptake and Release

Possible regulatory role for the histidine-rich loop in the zinc transport protein, ZnuA

A Conserved Structural Module Regulates Transcriptional Responses to Diverse Stress Signals in Bacteria

Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli

P304

108

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

P31

scholarly article

P3181

4836722

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

P356

10.3389/FCIMB.2013.00108

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

P407

P478

3

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

P50

Andrea Battistoni

P577

2013-01-01T00:00:00Z

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

2013-12-24T00:00:00Z

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

P5875

259628536

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

P698

24400228

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

P921

inorganic compound

P932

3872050

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