Jenny Yang

Dr. Jenny Yang

orcid

Research Focus & Metrics

Academic Career Length

21Years (2006-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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6 May 2016 in Science Advances
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CZChen Zhang
Chen Zhang
TZTuo Zhang
Tuo Zhang
JZJuan Zou
Juan Zou
CMCassandra Lynn Miller
Cassandra Lynn Miller
RGRakshya Gorkhali
Rakshya Gorkhali
JYJenny Yang
Jenny Yang
Structural and functional characterization of the extracellular domain of the human CaSR with bound Mg 2+ and a tryptophan derivative.

Verified
Journal Article
Open access
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JYJenny Yang
Jenny Yang
YXYiting Xu
Yiting Xu
MKMichael Kirberger
Michael Kirberger
JYJenny Yang
Jenny Yang
Calmodulin (CaM) is an important intracellular protein that binds Ca2+ and functions as a critical second messenger involved in numerous biological activities through extensive interactions with proteins and peptides. CaM’s ability to adapt to binding targets with different structures is related to the flexible central helix separating the N- and C-terminal lobes, which allows for conformational changes between extended and collapsed forms of the protein. CaM-binding targets are most often identified using prediction algorithms that utilize sequence and structural data to predict regions of peptides and proteins that can interact with CaM. In this review, we provide an overview of different CaM-binding proteins, the motifs through which they interact with CaM, and shared properties that make them good binding partners for CaM. Additionally, we discuss the historical and current methods for predicting CaM binding, and the similarities and differences between these methods and their relative success at prediction. As new CaM-binding proteins are identified and classified, we will gain a broader understanding of the biological processes regulated through changes in Ca2+ concentration through interactions with CaM.

29 October 2019 in Nature Communications
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MSMani Salarian
Mani Salarian
RTRavi Chakra Turaga
Ravi Chakra Turaga
SXShenghui Xue
Shenghui Xue
MNMaysam Nezafati
Maysam Nezafati
KHKhan Hekmatyar
Khan Hekmatyar
JYJenny Yang
Jenny Yang
Early diagnosis and noninvasive detection of liver fibrosis and its heterogeneity remain as major unmet medical needs for stopping further disease progression toward severe clinical consequences. Here we report a collagen type I targeting protein-based contrast agent (ProCA32.collagen1) with strong collagen I affinity. ProCA32.collagen1 possesses high relaxivities per particle (r1 and r2) at both 1.4 and 7.0 T, which enables the robust detection of early-stage (Ishak stage 3 of 6) liver fibrosis and nonalcoholic steatohepatitis (Ishak stage 1 of 6 or 1 A Mild) in animal models via dual contrast modes. ProCA32.collagen1 also demonstrates vasculature changes associated with intrahepatic angiogenesis and portal hypertension during late-stage fibrosis, and heterogeneity via serial molecular imaging. ProCA32.collagen1 mitigates metal toxicity due to lower dosage and strong resistance to transmetallation and unprecedented metal selectivity for Gd3+ over physiological metal ions with strong translational potential in facilitating effective treatment to halt further chronic liver disease progression.

26 November 2012 in Metallomics
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YZYubin Zhou
Yubin Zhou
SXShenghui Xue
Shenghui Xue
JYJenny Yang
Jenny Yang
Calcium ion (Ca2+), the fifth most common chemical element in the earth's crust, represents the most abundant mineral in the human body. By binding to a myriad of proteins distributed in different cellular organelles, Ca2+ impacts nearly every aspect of cellular life. In prokaryotes, Ca2+ plays an important role in bacterial movement, chemotaxis, survival reactions and sporulation. In eukaryotes, Ca2+ has been chosen through evolution to function as a universal and versatile intracellular signal. Viruses, as obligate intracellular parasites, also develop smart strategies to manipulate the host Ca2+ signaling machinery to benefit their own life cycles. This review focuses on recent advances in applying both bioinformatic and experimental approaches to predict and validate Ca2+-binding proteins and their interactomes in biological systems on a genome-wide scale (termed “calciomics”). Calmodulin is used as an example of Ca2+-binding protein (CaBP) to demonstrate the role of CaBPs on the regulation of biological functions. This review is anticipated to rekindle interest in investigating Ca2+-binding proteins and Ca2+-modulated functions at the systems level in the post-genomic era.

13 May 2015 in Proceedings of the National Academy of Sciences
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SXShenghui Xue
Shenghui Xue
HYHua Yang
Hua Yang
JQJingjuan Qiao
Jingjuan Qiao
FPFan Pu
Fan Pu
JJJie Jiang
Jie Jiang
JYJenny Yang
Jenny Yang
Significance: Primary and metastatic liver cancers that are associated with high mortality rates and poor treatment responses are only diagnosed at late stages, due to the lack of highly sensitive contrast agents and robust imaging methodologies. We have developed a protein MRI contrast agent (ProCA32) by engineering high-affinity Gd 3+ -binding pockets in rat and human α-parvalbumin. ProCA32 can function as both a T 1 - and T 2 -weighted contrast agent, which enables noninvasive detection of early-stage micrometastatic liver tumors with sizes as small as 0.24 mm using T 1 - and T 2 -weighted or T 2 /T 1 ratio MRI. Our protein-based MRI contrast agents and imaging methodology are expected to provide robust results for the early detection of liver cancer as well as other liver diseases.

1 August 2013 in Journal of Inorganic Biochemistry
Verified
Journal Article
Closed access
MKMichael Kirberger
Michael Kirberger
HWHing C. Wong
Hing C. Wong
JJJie Jiang
Jie Jiang
JYJenny Yang
Jenny Yang