Intrinsically disordered proteins and biomineralization. - Wikidata - wikimedia - TriplyDB

Intrinsically disordered proteins and biomineralization.

Intrinsically disordered proteins and biomineralization.

http://www.wikidata.org/entity/Q34045958

about

Bone Alkaline Phosphatase and Tartrate-Resistant Acid Phosphatase: Potential Co-regulators of Bone Mineralization Reactivity of U-associated osteopontin with lactoferrin: a one-to-many complex.Anatomically-specific intratubular and interstitial biominerals in the human renal medullo-papillary complex.Phosphorylation regulates the secondary structure and function of dentin phosphoprotein peptides.Protein disorder-order interplay to guide the growth of hierarchical mineralized structures.In-depth proteomic analyses of Haliotis laevigata (greenlip abalone) nacre and prismatic organic shell matrix.Calcium-Binding Proteins with Disordered Structure and Their Role in Secretion, Storage, and Cellular Signaling.Understanding the Biomineralization Role of Magnetite-Interacting Components (MICs) From Magnetotactic Bacteria

P2860

Q33841897-4FA43F3F-0148-4CC7-92F1-0898FE879815 Q38754422-66BA0341-A9F1-4FC3-A6F4-9672EA987E5E Q45393759-A05E8004-7B87-487D-8484-020EEBA5A834 Q46276371-408A1456-F499-4594-8E04-6273CEF428EE Q55301538-67E56C43-B362-43A7-88F1-F70836BC5D1D Q55465356-7AACEE6C-63DD-453C-A004-A4DDEBAE35F1 Q55514345-6E013E3F-84BB-406F-B18C-6CB8D8474361 Q58573021-FB6779AA-E348-44A9-BE97-92BAE51D36CD

P2860

Intrinsically disordered proteins and biomineralization.

http://www.wikidata.org/entity/Q34045958

description

2016 nî lūn-bûn

@nan

2016 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի հունվարին հրատարակված գիտական հոդված

@hy

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

name

Intrinsically disordered proteins and biomineralization.

@ast

Intrinsically disordered proteins and biomineralization.

@en

Intrinsically disordered proteins and biomineralization.

@nl

type

label

Intrinsically disordered proteins and biomineralization.

@ast

Intrinsically disordered proteins and biomineralization.

@en

Intrinsically disordered proteins and biomineralization.

@nl

prefLabel

Intrinsically disordered proteins and biomineralization.

@ast

Intrinsically disordered proteins and biomineralization.

@en

Intrinsically disordered proteins and biomineralization.

@nl

P1433

Q34045958-79F8E1FD-C537-404E-B71C-919D8F905345

P1476

Q34045958-51941E14-DF2B-4C3F-B040-85D61B1AE210

P2093

Q34045958-95BC366D-4642-46D9-A907-CBD7304C9769

P2860

Q34045958-006746AE-36AD-4743-8159-D40A5C08545E

Q34045958-00AD259E-3BBA-42DE-B456-768F14F02E81

Q34045958-00EB9156-05C1-4690-921D-BE09E9329A0D

Q34045958-0322A0D3-02E9-4FA6-9DD9-4AB9C7671D74

Q34045958-07C68CFA-55B9-41F3-8AA2-932E5E316090

Q34045958-0813E609-7E43-4B6A-8D8D-F01CBA8A5332

Q34045958-09E41279-D100-489A-AC71-29C99CEA2090

Q34045958-0ED2D65F-A380-44A8-94FA-7CD403731665

Q34045958-0FA69A09-B0B4-48AF-A0A7-46A1C3972FBC

Q34045958-1055E87C-4F15-4866-87D2-EC4ADBBA52E3

P304

Q34045958-7542FFAA-42B0-4372-85B4-63A353E064BA

P31

Q34045958-79EA56F5-EFA0-4AAC-B553-2CD0A8E97D36

P356

Q34045958-5677DBBB-A19E-4D8E-A6DD-E2113D93731B

P478

Q34045958-D1A10399-9820-4103-8CFC-4862C0892654

P50

Q34045958-14180D19-A391-4D24-8119-AEE4F08D2200

P577

Q34045958-3ADB0145-06FF-4323-A45E-D5BE2F47041B

P5875

Q34045958-2090893F-C792-49C7-B22D-1E1979B73AA2

P698

Q34045958-6FF3AFFB-5F8C-4B5C-8F83-9EBF0D167986

P921

Q34045958-F7CE0033-53EC-40BA-95B9-7B619EA40DF1

P932

Q34045958-52A60453-9A6F-49AA-AAAA-80EE9E2C95E7

P356

J.MATBIO.2016.01.007

P1433

P1476

Intrinsically disordered proteins and biomineralization

@en

P2093

Adele L Boskey

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

P2860

Roles of electrostatics and conformation in protein-crystal interactions

Classification of intrinsically disordered regions and proteins

Secreted kinase phosphorylates extracellular proteins that regulate biomineralization

A Single Kinase Generates the Majority of the Secreted Phosphoproteome

Modulation of crystal formation by bone phosphoproteins: role of glutamic acid-rich sequences in the nucleation of hydroxyapatite by bone sialoprotein

Microfibrillar structure of type I collagen in situ

Candidate cell and matrix interaction domains on the collagen fibril, the predominant protein of vertebrates

Osteopontin inhibits mineral deposition and promotes regression of ectopic calcification

Silaffins in Silica Biomineralization and Biomimetic Silica Precipitation

Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)

P304

43-59

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

P31

scholarly article

P356

10.1016/J.MATBIO.2016.01.007

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

P478

52-54

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

P50

Eduardo Villarreal

P577

2016-01-22T00:00:00Z

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

P5875

291558071

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

P698

26807759

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

P921

biomineralization

P932

4875856

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