Stable association wollastonite-anorthite, and other cale-silicate assemblages in amphibolite-facies crystalline schists of Nanga Parbat, Northwest Himalayas

1964 ◽  
Vol 10 (3) ◽  
pp. 315-356 ◽  
Author(s):  
Peter Misch
Keyword(s):  
Amphibolite Facies ◽  
Nanga Parbat ◽  
Stable Association ◽  
Northwest Himalayas

Neotectonics of the Nanga Parbat Syntaxis, Pakistan, and crustal stacking in the northwest Himalayas

1989 ◽  
Vol 94 (3-4) ◽  
pp. 329-343 ◽  
Author(s):  
Robert W.H. Butler ◽  
David J. Prior ◽  
Robert J. Knipe
Keyword(s):  
Nanga Parbat ◽  
Northwest Himalayas

DIVING DEEPER INTO THE PICURIS OROGEN: UPPER AMPHIBOLITE FACIES METAMORPHISM AND BRITTLE DEFORMATION ALONG THE PLOMO SHEAR ZONE

2020 ◽  
Author(s):  
Adrian E. Castro ◽  
◽  
Chloe Bonamici ◽  
Christopher G. Daniel ◽  
Danielle Shannon Sulthaus
Keyword(s):  
Shear Zone ◽  
Amphibolite Facies ◽  
Brittle Deformation ◽  
Facies Metamorphism

Timanide (Ediacaran-Early Cambrian) Metamorphism at the Transition from Eclogite to Amphibolite Facies in the Beloretsk Complex, SW-Urals, Russia

2019 ◽  
Vol 30 (6) ◽  
pp. 1144-1165 ◽  
Author(s):  
Arne P. Willner ◽  
Michael Gopon ◽  
Johannes Glodny ◽  
Victor N. Puchkov ◽  
Hans-Peter Schertl
Keyword(s):  
Amphibolite Facies ◽  
Early Cambrian

scholarly journals Stable association of RNAi machinery is conserved between the cytoplasm and nucleus of human cells

RNA ◽  
2016 ◽  
Vol 22 (7) ◽  
pp. 1085-1098 ◽  
Author(s):  
Roya Kalantari ◽  
Jessica A. Hicks ◽  
Liande Li ◽  
Keith T. Gagnon ◽  
Viswanadham Sridhara ◽  
...  
Keyword(s):  
Human Cells ◽  
Rnai Machinery ◽  
Stable Association

scholarly journals Characterization of Receptor Interaction and Transcriptional Repression by the Corepressor SMRT

1997 ◽  
Vol 11 (13) ◽  
pp. 2025-2037 ◽  
Author(s):  
Hui Li ◽  
Christopher Leo ◽  
Daniel J. Schroen ◽  
J. Don Chen
Keyword(s):  
Nuclear Receptors ◽  
Nuclear Receptor ◽  
Transcriptional Repression ◽  
Thyroid Hormone Receptor ◽  
Receptor Interaction ◽  
Basal Transcription ◽  
Protein Protein Interaction ◽  
Stable Association ◽  
Interacting Surfaces ◽  
Transcriptional Corepressors

Abstract SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) and N-CoR (nuclear receptor corepressor) are two related transcriptional corepressors that contain separable domains capable of interacting with unliganded nuclear receptors and repressing basal transcription. To decipher the mechanisms of receptor interaction and transcriptional repression by SMRT/N-CoR, we have characterized protein-protein interacting surfaces between SMRT and nuclear receptors and defined transcriptional repression domains of both SMRT and N-CoR. Deletional analysis reveals two individual nuclear receptor domains necessary for stable association with SMRT and a C-terminal helix essential for corepressor dissociation. Coordinately, two SMRT domains are found to interact independently with the receptors. Functional analysis reveals that SMRT contains two distinct repression domains, and the corresponding regions in N-CoR also repress basal transcription. Both repression domains in SMRT and N-CoR interact weakly with mSin3A, which in turn associates with a histone deacetylase HDAC1 in a mammalian two-hybrid assay. Far-Western analysis demonstrates a direct protein-protein interaction between two N-CoR repression domains with mSin3A. Finally we demonstrate that overexpression of full-length SMRT further represses basal transcription from natural promoters. Together, these results support a role of SMRT/N-CoR in corepression through the utilization of multiple mechanisms for receptor interactions and transcriptional repression.

scholarly journals Detection of gp91-phox precursor protein in B-cell lines from patients with X-linked chronic granulomatous disease as an indicator for mutations impairing cytochrome b558 biosynthesis

1996 ◽  
Vol 315 (2) ◽  
pp. 571-575 ◽  
Author(s):  
Colin D. PORTER ◽  
KURIBAYASHI KURIBAYASHI ◽  
Mohamed H. PARKAR ◽  
Dirk ROOS ◽  
Christine KINNON
Keyword(s):  
Nadph Oxidase ◽  
B Cell ◽  
Chronic Granulomatous Disease ◽  
Cell Lines ◽  
Binding Domain ◽  
Granulomatous Disease ◽  
Cytochrome B558 ◽  
Stable Association ◽  
P22 Phox ◽  
Fad Binding

NADPH oxidase cytochrome b558 consists of two subunits, gp91-phox and p22-phox, defects of which result in chronic granulomatous disease (CGD). The nature of the interaction between these subunits has yet to be determined. Absence of p22-phox in autosomal CGD patient-derived B-cell lines results in detectable levels of an incompletely glycosylated gp91-phox precursor. We have detected this same precursor species in four cell lines from patients with the X-linked form of the disease due to mutations in gp91-phox. Such mutations should delineate regions of gp91-phox important for its biosynthesis, including stable association with p22-phox. One mutation mapped to the putative FAD-binding domain, one mapped to a potential haem-binding domain, and two involved the region encoded by exon 3.

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