ライフサイエンスコーパス: Tamm

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1 Tamm states can exist with zero in-plane wavevector comp

2 Tamm-Horsfall protein (THP) is a glycoprotein uniquely e

3 Tamm-Horsfall protein (THP), also known as uromodulin, i

4 ge band structure and can be classified as a Tamm-like state lacking any surface defect.

5 Here, we implement a Tamm-plasmon-polariton structure and study the coupling

6 teractions between urinary proteins, such as Tamm-Horsfall protein, and TLR-4 add to the complexity o

7 Tamm state under the metal film and display Tamm state-coupled emission (TSCE).

8 ules tested inhibited aggregation, including Tamm-Horsfall protein, which did not inhibit growth.

9 xpress COX-2, bNOS, NKCC2, and ROMK, but not Tamm-Horsfall protein, and showed rapid (86)Rb(+) uptake

10 Here we show that elimination of Tamm-Horsfall protein (THP) expression from mouse kidney

11 stably expressing human-relevant mutants of Tamm-Horsfall protein in polarized Madin-Darby canine ki

12 thod to understand the optical properties of Tamm states and localization of the modes or electric fi

13 t prevent adhesion of bacteria by release of Tamm-Horsfall protein, lactoferrin, lipocalin, and const

14 ive to wavelength, which suggests the use of Tamm structures to provide both directional emission and

15 ltered light chains bind to a common site on Tamm-Horsfall protein (THP), which is produced by cells

16 inant glutathione-S-transferase-OPN (G-OPN), Tamm-Horsfall protein, chondroitin sulfate, human serum

17 Our structure is designed to support optical Tamm states, which are trapped electromagnetic modes bet

18 This removed Tamm-Horsfall protein, the major contaminant, and subfra

19 gene under the direction of the TAL-specific Tamm-Horsfall protein promoter was generated.

20 Here we show that Tamm-Horsfall protein (THP) is the principal urinary pro

21 In contrast to SPCE, the Tamm states can display either S or P polarization.

22 top of the metal film can interact with the Tamm state under the metal film and display Tamm state-c

23 to specifically bind and trap the wild-type Tamm-Horsfall protein (THP) and prevent it from exiting

24 Uromodulin (UMOD)/Tamm-Horsfall protein, the most abundant human urinary p

25 odes the most common protein in human urine, Tamm-Horsfall protein, and rare mutations in UMOD cause

26 of the UMOD gene, which encodes uromodulin (Tamm-Horsfall protein), associate with chronic kidney di

27 revalent soluble urinary protein uromodulin (Tamm-Horsfall protein), potently inhibited growth of pat

28 ar, because the encoded protein, uromodulin (Tamm-Horsfall protein), is exclusively produced by the k

29 Uromodulin/Tamm-Horsfall protein is not immunostimulatory in the tu

30 t that pathologic accumulation of uromodulin/Tamm-Horsfall glycoprotein (THP) occurs in the endoplasm

31 s well as an assessment of the commonly used Tamm-Dancoff approximation to the GW-BSE approach.

32 s to demonstrate the utility of the in vitro Tamm-Horsfall protein (THP)-1 human monocyte cell cultur

33 The gene neither codistributed with Tamm-Horsfall protein nor aquaporin-2.

34 ight chains (FLCs), which coprecipitate with Tamm-Horsfall glycoprotein (THP) in the lumen of the dis

35 immunoglobulin free light chains (FLCs) with Tamm-Horsfall glycoprotein (THP).

36 f filtered monoclonal light chains (LC) with Tamm-Horsfall glycoprotein (THP) triggers heterotypic ag

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