Results 31 to 40 of about 707,163 (239)

The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids. [PDF]

, 2015
Telomerase is an enzyme that adds repetitive DNA sequences to the ends of chromosomes and consists of two main subunits: the telomerase reverse transcriptase (TERT) protein and an associated telomerase RNA (TER). The telomerase essential N-terminal (TEN)
Akiyama, Benjamin M, Parks, Joseph W, Stone, Michael D   +2 more
core   +2 more sources

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

FEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho, Shin Morioka, Junko Sasaki, Takehiko Sasaki   +3 more
wiley   +1 more source

Ramachandran mapping of peptide conformation using a large database of computed Raman and Raman optical activity spectra [PDF]

, 2016
In the past few decades, Raman optical activity (ROA) spectroscopy has been shown to be very sensitive to the solution structure of peptides and proteins.
Barron, Laurence D., Johannessen, Christian, Mensch, Carl   +2 more
core   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

FEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source

Molecular modeling of an antigenic complex between a viral peptide and a class I major histocompatibility glycoprotein [PDF]

, 1992
Computer simulation of the conformations of short antigenic peptides (&lo residues) either free or bound to their receptor, the major histocompatibility complex (MHC)- encoded glycoprotein H-2 Ld, was employed to explain experimentally determined ...
Allen, Babbit, Bjorkman, Buus, Chen, Cramer, Del Val, DeLisi, Falk, Fauchère, Garrett, Jorgensen, Kidera, Kourilsky, Krug, Lambert, Lambert, Lambert, Margalit, Maryanski, Owen, Reddehase, Reddehase, Reddehase, Rötzschke, Saper, Schwartz, Serrano, Sette, Tirado-Rives, Townsend, Townsend, Townsend, Unanue, Van Bleek, Weiner, Wendoloski, Wold, Zinkernagel   +38 more
core   +1 more source

In situ molecular organization and heterogeneity of the Legionella Dot/Icm T4SS

FEBS Letters, EarlyView.
We present a nearly complete in situ model of the Legionella Dot/Icm type IV secretion system, revealing its central secretion channel and identifying new components. Using cryo‐electron tomography with AI‐based modeling, our work highlights the structure, variability, and mechanism of this complex nanomachine, advancing understanding of bacterial ...
Przemysław Dutka, Yuxi Liu, Stefano Maggi, Debnath Ghosal, Jue Wang, Prashant P. Damke, Stephen D. Carter, Wei Zhao, Sukhithasri Vijayrajratnam, Joseph P. Vogel, Carrie L. Shaffer, Grant J. Jensen   +11 more
wiley   +1 more source

Is Heteropolymer Freezing Well Described by the Random Energy Model?

, 1996
It is widely held that the Random Energy Model (REM) describes the freezing transition of a variety of types of heteropolymers. We demonstrate that the hallmark property of REM, statistical independence of the energies of states over disorder, is ...
A. M. Gutin, A. Yu. Grosberg, Alexander Yu. Grosberg, B. Derrida, Chris Joerg, E. I. Shakhnovich, E. I. Shakhnovich, E. Shakhnovich, E. Shakhnovich, J. D. Bryngelson, J. D. Bryngelson, J. D. Bryngelson, J. D. Bryngelson, K. Yue, K. Yue, M. H. Hecht, N. D. Socci, P. G. Wolynes, S. Miyazawa, Toyoichi Tanaka, V. S. Pande, V. S. Pande, V. S. Pande, Vijay S. Pande   +23 more
core   +1 more source

Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [PDF]

, 2010
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. These diseases can be hereditary in humans and four of the many disease-associated missense mutants of PrP are in the ...
Daggett, Valerie, van der Kamp, Marc W
core   +2 more sources

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

FEBS Letters, EarlyView.
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li, Pedro A. Sánchez‐Murcia, Bernd Nidetzky   +2 more
wiley   +1 more source

Reading the three-dimensional structure of a protein from its amino acid sequence

, 2000
While all the information required for the folding of a protein is contained in its amino acid sequence, one has not yet learnt how to extract this information so as to predict the detailed, biological active, three-dimensional structure of a protein ...
Broglia, R. A., Tiana, G.
core   +1 more source