Determination of type I receptor specificity by the type II receptors for TGF-beta or activin

Science ◽  
1993 ◽  
Vol 262 (5135) ◽  
pp. 900-902 ◽  
Author(s):  
R Ebner ◽  
R. Chen ◽  
S Lawler ◽  
T Zioncheck ◽  
R Derynck
Keyword(s):  
Type I ◽  
Type Ii ◽  
Tgf Beta ◽  
Receptor Specificity

scholarly journals DETERMINATION OF CROSS SECTIONS FOR GRAVITY TYPE QUAY WALLS

2017 ◽  
pp. 5
Author(s):  
Tugce Yuksel ◽  
Yalcin Yuksel ◽  
Busra Basaran ◽  
Esin Cevik
Keyword(s):  
Cross Sections ◽  
Vertical Wall ◽  
Block Size ◽  
Seismic Loading ◽  
Block Type ◽  
Type I ◽  
Type Ii ◽  
Seismic Loadings ◽  
Port Structures

Block type quay walls are widely used as port structures in the world. In this study three types of vertical block type quay walls with different block size exposed to seismic loading were investigated experimentally. The block ratios of Type I, Type II and III vertical wall models are B/h=2, 1.5 and 1.5 & H/h=6, 6 and 3, respectively. The tests were conducted in the shaking tank with different harmonic seismic loadings and the behaviors of these walls were investigated comparatively.

The Determination of Macrostresses (Type-I Stresses) and Microstresses (Type-Ii Stresses) by Neutron Diffraction

1994 ◽  
Vol 376 ◽  
Author(s):  
T.M. Holden
Keyword(s):  
Neutron Diffraction ◽  
Experimental Methods ◽  
Stress Fields ◽  
Type I ◽  
Type Ii ◽  
Sources Of Error ◽  
Precision And Accuracy

ABSTRACTNeutron diffraction has been used as tool for measuring stress fields (type-I stresses) and intergranular or microstresses (type-II stresses) for a decade. The experimental methods for measuring the two types of stresses are outlined. Emphasis is placed on maximizing the precision and accuracy of the measurements. Some serious sources of error in measurements near surfaces and some subtle wavelength effects are considered.

X-ray structure determination of the monoclinic (121 K) and orthorhombic (85 K) phases of langbeinite-type dithallium dicadmium sulfate

2000 ◽  
Vol 56 (6) ◽  
pp. 921-935 ◽  
Author(s):  
A. Guelylah ◽  
G. Madariaga ◽  
W. Morgenroth ◽  
M. I. Aroyo ◽  
T. Breczewski ◽  
...  
Keyword(s):  
Orthorhombic Symmetry ◽  
Type I ◽  
Type Ii ◽  
Monoclinic Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
Distortion Analysis ◽  
Precise Analysis ◽  
Monoclinic Distortion

The structures of the monoclinic and the orthorhombic phases of type I langbeinite Tl2Cd2(SO4)3 have been determined at 121 and 85 K, respectively, by X-ray diffraction. A precise analysis of these structures shows the existence of some differences compared to langbeinites of type II. The monoclinic structure differs very little from the high-temperature cubic structure and the distortion relating the monoclinic structure to the cubic one is very small. SO4 tetrahedra seem to rotate under orthorhombic symmetry in the monoclinic phase. A symmetry distortion analysis of the ferroelectric monoclinic distortion discloses the importance of the secondary modes with orthorhombic symmetry, especially for the O atoms of the SO4 groups.

Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor

Science ◽  
1993 ◽  
Vol 260 (5112) ◽  
pp. 1344-1348 ◽  
Author(s):  
R Ebner ◽  
R. Chen ◽  
L Shum ◽  
S Lawler ◽  
T. Zioncheck ◽  
...  
Keyword(s):  
Type I ◽  
Type Ii ◽  
Tgf Beta ◽  
Beta Receptor

Determination of Preferred Morphology of Self-Accommodating Martensite in Ti-Nb-Al Shape Memory Alloy Using Optical Microscopy

2014 ◽  
Vol 922 ◽  
pp. 260-263 ◽  
Author(s):  
Masatoshi Ii ◽  
Masaki Tahara ◽  
Hideki Hosoda ◽  
Shuichi Miyazaki ◽  
Tomonari Inamura
Keyword(s):  
Shape Memory Alloy ◽  
Shape Memory ◽  
Optical Microscopy ◽  
Early Stage ◽  
Type I ◽  
Type Ii ◽  
Different Types ◽  
Forward Transformation

The preferred morphology of self-accommodation (SA) microstructure in a Ti-Nb-Al shape memory alloy was investigated by the evaluation of the frequency distribution of the habit plane variant (HPV) clusters using in-situ optical microscopy. The observed HPV clusters were classified into two different types; one is the cluster connected by the {111}o type I twin (Type I) and the other is connected by the <211>o type II twin (Type II). The total fractions of the Type I and Type II clusters were 52% and 48%, respectively. The incompatibility at junction planes (JPs) of the two clusters was almost the same among these clusters. However, most of the larger martensite plates (> 50μm) formed Type I cluster at the later stage of the reverse martensitic transformation, i.e., at the early stage of the forward transformation upon cooling. The ratio of the fraction of Type I and II is almost 2:1 at the early stage of the forward transformation.

scholarly journals Two distinct transmembrane serine/threonine kinases from Drosophila melanogaster form an activin receptor complex.

1994 ◽  
Vol 14 (2) ◽  
pp. 944-950 ◽  
Author(s):  
J L Wrana ◽  
H Tran ◽  
L Attisano ◽  
K Arora ◽  
S R Childs ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Transmembrane Protein ◽  
Bone Morphogenetic Protein 2 ◽  
Type I ◽  
Type Ii ◽  
Tgf Beta ◽  
Activin Receptor ◽  
Domain Of Unknown Function

A transmembrane protein serine/threonine kinase, Atr-I, that is structurally related to receptors for members of the transforming growth factor-beta (TGF-beta) family has been cloned from Drosophila melanogaster. The spacing of extracellular cysteines and the cytoplasmic domain of Atr-I resemble most closely those of the recently described mammalian type I receptors for TGF-beta and activin. When expressed alone in test cells, Atr-I is unable to bind TGF-beta, activin, or bone morphogenetic protein 2. However, Atr-I binds activin efficiently when coexpressed with the distantly related Drosophila activin receptor Atr-II, with which it forms a heteromeric complex. Atr-I can also bind activin in concert with mammalian activin type II receptors. Two alternative forms of Atr-I have been identified that differ in an ectodomain region encompassing the cysteine box motif characteristic of receptors in this family. Comparison of Atr-I with other type I receptors reveals the presence of a characteristic 30-amino-acid domain immediately upstream of the kinase region in all these receptors. This domain, of unknown function, contains a repeated Gly-Ser sequence and is therefore referred to as the GS domain. Maternal Atr-I transcripts are abundant in the oocyte and widespread during embryo development and in the imaginal discs of the larva. The structural properties, binding specificity, and dependence on type II receptors define Atr-I as an activin type I receptor from D. melanogaster. These results indicate that the heteromeric kinase structure is a general feature of this receptor family.

Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor beta and activin

1994 ◽  
Vol 14 (6) ◽  
pp. 3810-3821
Author(s):  
J Cárcamo ◽  
F M Weis ◽  
F Ventura ◽  
R Wieser ◽  
J L Wrana ◽  
...  
Keyword(s):  
Transforming Growth Factor Beta ◽  
Amino Acid Sequence Identity ◽  
Transforming Growth Factor ◽  
Type I ◽  
Type Ii ◽  
Tgf Beta ◽  
Transcriptional Responses ◽  
Receptor Complexes ◽  
Growth Inhibitory ◽  
Growth Factor Beta

Transforming growth factor beta (TGF-beta) and activin bind to receptor complexes that contain two distantly related transmembrane serine/threonine kinases known as receptor types I and II. The type II receptors determine ligand binding specificity, and each interacts with a distinct repertoire of type I receptors. Here we identify a new type I receptor for activin, ActR-IB, whose kinase domain is nearly identical to that of the recently cloned TGF-beta type I receptor, T beta R-I. ActR-IB has the structural and binding properties of a type I receptor: it binds activin only in the presence of an activin type II receptor and forms a heteromeric noncovalent complex with activin type II receptors. In Mv1Lu lung epithelial cells, ActR-IB and T beta R-I signal a common set of growth-inhibitory and transcriptional responses in association with their corresponding ligands and type II receptors. The transcriptional responses include elevated expression of fibronectin and plasminogen activator inhibitor 1. Although T beta R-I and ActR-IB are nearly identical in their kinase domains (90% amino acid sequence identity), their corresponding type II receptor kinase domains are very different from each other (42% amino acid sequence identity). Therefore, signaling of a specific set of responses by TGF-beta and activin correlates with the presence of similar type I kinases in their complex. Indeed, other TGF-beta and activin type I receptors (TSR-I and ActR-I) whose kinase domains significantly diverge from those of T beta R-I and ActR-IB do not substitute as mediators of these growth-inhibitory and extracellular matrix transcriptional responses. Hence, we conclude that the type I receptor subunits are primary specifiers of signals sent by TGF-beta and activin receptor complexes.

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