Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

about

Nickel Sequestration by the Host-Defense Protein Human Calprotectin.The role of calprotectin in withholding zinc and copper from Candida albicans.Human calprotectin affects the redox speciation of iron.Magnetic circular dichroism of UCl6- in the ligand-to-metal charge-transfer spectral region.

P2860

Q40188001-12505FDD-3C9D-4ACA-A172-E7D88A8D94EE Q47407305-D8F186A3-72F8-4C18-A2F5-DB1A10CA4E6B Q50611121-28E24E12-A801-405E-931F-36215A159A9C Q53201468-64307F3A-BF7B-44C0-9A73-9A41BCB2E9BE

P2860

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

Item

http://www.wikidata.org/entity/Q42314747

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Magnetic circular dichroism studies of iron

@nl

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

@en

type

Item

label

Magnetic circular dichroism studies of iron

@nl

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

@en

prefLabel

Magnetic circular dichroism studies of iron

@nl

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

@en

P1476

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

@en

P2093

Elizabeth M Nolan

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

Toshiki G Nakashige

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

P2860

The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting alpha-helices can determine specific association of two EF-hand proteins

Molecular basis for manganese sequestration by calprotectin and roles in the innate immune response to invading bacterial pathogens

Spectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activation

The Hexahistidine Motif of Host-Defense Protein Human Calprotectin Contributes to Zinc Withholding and Its Functional Versatility

The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes.

Biophysical characterization of S100A8 and S100A9 in the absence and presence of bivalent cations.

Near-IR MCD of the nonheme ferrous active site in naphthalene 1,2-dioxygenase: correlation to crystallography and structural insight into the mechanism of Rieske dioxygenases.

MCD C-Term Signs, Saturation Behavior, and Determination of Band Polarizations in Randomly Oriented Systems with Spin S >/= (1)/(2). Applications to S = (1)/(2) and S = (5)/(2).

Nutritional immunity: transition metals at the pathogen-host interface.

Reaction mechanisms of mononuclear non-heme iron oxygenases.

P304

1369-1377

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

P31

scholarly article

P356

10.1039/C6SC03487J

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

P433

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

P478

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

P50

Tessa M Baker

Michael L Neidig

P577

2016-10-11T00:00:00Z

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

P698

28451278

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

P932

5361872

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

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

about

P2860

P2860

Magnetic circular dichroism studies of iron(ii) binding to human calprotectin.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P932