scispace - formally typeset
J

Jenny Yi-Chun Liu

Researcher at National Tsing Hua University

Publications -  51
Citations -  761

Jenny Yi-Chun Liu is an academic researcher from National Tsing Hua University. The author has contributed to research in topics: CMOS & Amplifier. The author has an hindex of 13, co-authored 47 publications receiving 689 citations. Previous affiliations of Jenny Yi-Chun Liu include University of California, Los Angeles.

Papers
More filters
Journal ArticleDOI

ICAP-1, a Novel β1 Integrin Cytoplasmic Domain–associated Protein, Binds to a Conserved and Functionally Important NPXY Sequence Motif of β1 Integrin

TL;DR: The identification of a novel protein, ICAP-1 (integrin cytoplasmic domain– associated protein-1), which binds to the β 1 integrin cytopsized domain is reported, which suggests an important role of IC AP-1 during integrin-dependent cell adhesion.
Journal ArticleDOI

60 GHz CMOS Amplifiers Using Transformer-Coupling and Artificial Dielectric Differential Transmission Lines for Compact Design

TL;DR: On-chip transformers combine bias, stability and input/interstage matching networks to enable compact designs and achieved a peak gain of 25 dB with 8 dB of gain variation in the variable-gain amplifier.
Journal ArticleDOI

Millimeter-Wave Self-Healing Power Amplifier With Adaptive Amplitude and Phase Linearization in 65-nm CMOS

TL;DR: In this article, a self-healing two-stage millimeter-wave broadband power amplifier (PA) with on-chip amplitude/phase compensation is realized in 65-nm CMOS.
Journal ArticleDOI

A Wideband Inductorless Single-to-Differential LNA in $0.18 \mu{\rm m}$ CMOS Technology for Digital TV Receivers

TL;DR: In this paper, an inverter-based inductorless single-to-differential (S2D) wideband low-noise amplifier (LNA) was proposed.
Journal ArticleDOI

Molecular Basis for Interaction between Icap1α PTB Domain and β1 Integrin

TL;DR: Findings indicate that Icap1α is a PTB domain protein, which recognizes the NPXY motif of β1 integrin, and suggest that an interaction between Val787 and the hydrophobic pocket created by Leu82 and Tyr144 of I cap1α forms the basis for the specificity of Icap 1α for the β1 Integrin subunit.