Phonon dynamics and anharmonicity in phase segregated structural domains of MgZnO film

2014 ◽  
Vol 104 (3) ◽  
pp. 031908 ◽  
Author(s):  
Jesse Huso ◽  
Hui Che ◽  
Dinesh Thapa ◽  
John L. Morrison ◽  
M. Grant Norton ◽  
...  
Keyword(s):  
Structural Domains ◽  
Mgzno Film ◽  
Phonon Dynamics

scholarly journals Structural Domains of Human Apolipoprotein B-100

1989 ◽  
Vol 264 (24) ◽  
pp. 14369-14375 ◽  
Author(s):  
G C Chen ◽  
S Zhu ◽  
D A Hardman ◽  
J W Schilling ◽  
K Lau ◽  
...  
Keyword(s):  
Apolipoprotein B ◽  
Structural Domains ◽  
Human Apolipoprotein

scholarly journals Functional Roles of Bromodomain Proteins in Cancer

Cancers ◽  
2021 ◽  
Vol 13 (14) ◽  
pp. 3606
Author(s):  
Samuel P. Boyson ◽  
Cong Gao ◽  
Kathleen Quinn ◽  
Joseph Boyd ◽  
Hana Paculova ◽  
...  
Keyword(s):  
Open Chromatin ◽  
Structural Domains ◽  
Pharmacological Agents ◽  
Functional Roles ◽  
Cellular Processes ◽  
Protein Interactome ◽  
Interaction Partners ◽  
Recent Developments ◽  
Bromodomain Proteins ◽  
Chromatin Configuration

Histone acetylation is generally associated with an open chromatin configuration that facilitates many cellular processes including gene transcription, DNA repair, and DNA replication. Aberrant levels of histone lysine acetylation are associated with the development of cancer. Bromodomains represent a family of structurally well-characterized effector domains that recognize acetylated lysines in chromatin. As part of their fundamental reader activity, bromodomain-containing proteins play versatile roles in epigenetic regulation, and additional functional modules are often present in the same protein, or through the assembly of larger enzymatic complexes. Dysregulated gene expression, chromosomal translocations, and/or mutations in bromodomain-containing proteins have been correlated with poor patient outcomes in cancer. Thus, bromodomains have emerged as a highly tractable class of epigenetic targets due to their well-defined structural domains, and the increasing ease of designing or screening for molecules that modulate the reading process. Recent developments in pharmacological agents that target specific bromodomains has helped to understand the diverse mechanisms that bromodomains play with their interaction partners in a variety of chromatin processes, and provide the promise of applying bromodomain inhibitors into the clinical field of cancer treatment. In this review, we explore the expression and protein interactome profiles of bromodomain-containing proteins and discuss them in terms of functional groups. Furthermore, we highlight our current understanding of the roles of bromodomain-containing proteins in cancer, as well as emerging strategies to specifically target bromodomains, including combination therapies using bromodomain inhibitors alongside traditional therapeutic approaches designed to re-program tumorigenesis and metastasis.

scholarly journals Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains.

1986 ◽  
Vol 261 (28) ◽  
pp. 13333-13341 ◽  
Author(s):  
H K Simmerman ◽  
J H Collins ◽  
J L Theibert ◽  
A D Wegener ◽  
L R Jones
Keyword(s):  
Sequence Analysis ◽  
Phosphorylation Sites ◽  
Structural Domains
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