Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop (Q24306580)

GOA release 2020-03-11

ferric iron binding

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GOA release 2020-03-11

1

Norbert Sträter

Norbert

Sträter

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9 December 2023

9

Hans C Freeman

Hans C

Freeman

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9 December 2023

6

David B Langley

David B

Langley

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9 December 2023

10

J Mitchell Guss

J Mitchell

Guss

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9 December 2023

4

Bernt

Krebs

Bernt Krebs

1 reference

9 December 2023

Beate Jasper

2

Beate

Jasper

1 reference

9 December 2023

Marcel Scholte

3

Marcel

Scholte

1 reference

9 December 2023

Anthony P Duff

5

Anthony P

Duff

1 reference

9 December 2023

Runlin Han

7

Runlin

Han

1 reference

9 December 2023

Bruce A Averill

8

Bruce A

Averill

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Journal of Molecular Biology

9 December 2023

language of work or name

English

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publication date

5 August 2005

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published in

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volume

351

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issue

1

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page(s)

233-46

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cites work

The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity

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Conserved sequence pattern in a wide variety of phosphoesterases

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Structure validation by Calpha geometry: phi,psi and Cbeta deviation

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Recombinant human and mouse purple acid phosphatases: expression and characterization

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Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structures

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Crystal structure of a mammalian purple acid phosphatase

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Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a mu-(hydr)oxo bridged di-iron center

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Iron-containing acid phosphatases: comparison of the enzymes from beef spleen and pig allantoic fluid

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WHAT IF: a molecular modeling and drug design program

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Processing of X-ray diffraction data collected in oscillation mode

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Crystal structure of mammalian purple acid phosphatase

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Purification and properties of the native form of the purple acid phosphatase from bovine spleen

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Mutational analysis of the interaction between active site residues and the loop region in mammalian purple acid phosphatases

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Binuclear Metallohydrolases

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Electro-nuclear double resonance spectroscopic evidence for a hydroxo-bridge nucleophile involved in catalysis by a dinuclear hydrolase

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Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases

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Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas

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Comparative studies of rat recombinant purple acid phosphatase and bone tartrate-resistant acid phosphatase

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Mice lacking tartrate-resistant acid phosphatase (Acp 5) have disordered macrophage inflammatory responses and reduced clearance of the pathogen, Staphylococcus aureus

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Osteopontin--a possible anchor of osteoclasts to bone

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Role of Uteroferrin in Iron Transport and Macromolecular Uptake by Allantoic Epithelium of the Porcine Conceptus1, 2

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An enzyme with a double identity: purple acid phosphatase and tartrate-resistant acid phosphatase.

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Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site

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Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) open reading frame 4 protein (kaposica) is a functional homolog of complement control proteins

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Identifiers

DOI

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Fatcat ID

release_j47s3idszrcbvci6vv7vjxfdce

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