Nature Search

Yeast genes and human disease

Douglas E. Bassett
Mark S. Boguski
Philip Hieter
Research15 Feb 1996
Nature

Volume: 379, P: 589-590
Tubular Transport by Human Kidney stored at 4°C

STANTON SEGAL
INEZ SMITH
PHILIP HOLTZAPPLE
Research26 Apr 1969
Nature

Volume: 222, P: 387-389
Safer and efficient base editing and prime editing via ribonucleoproteins delivered through optimized lipid-nanoparticle formulations

The safety and efficacy of ribonucleoproteins for genome editing can be enhanced by formulations of lipid nanoparticles optimized for enhanced stability, delivery efficiency and editing potency of the protein complexes.

Rafał Hołubowicz
Samuel W. Du
Krzysztof Palczewski
ResearchOpen Access28 Nov 2024
Nature Biomedical Engineering

Volume: 9, P: 57-78
A combination treatment based on drug repurposing demonstrates mutation-agnostic efficacy in pre-clinical retinopathy models

This preclinical study demonstrates the potential of a drug repurposing strategy using the coadministration of tamsulosin, metoprolol, and bromocriptine to provide a mutation-agnostic therapy for inherited retinal degeneration.

Henri Leinonen
Jianye Zhang
Krzysztof Palczewski
ResearchOpen Access15 Jul 2024
Nature Communications

Volume: 15, P: 1-22
Publisher Correction: Restoration of visual function in adult mice with an inherited retinal disease via adenine base editing

Susie Suh
Elliot H. Choi
Krzysztof Palczewski
Amendments and Corrections29 Oct 2020
Nature Biomedical Engineering

Volume: 4, P: 1119
The yeast genome — a common currency

Philip Hieter
Douglas E. Bassett Jr.
David Valle
News & Views01 Jul 1996
Nature Genetics

Volume: 13, P: 253-255
Carotenoid cleavage enzymes evolved convergently to generate the visual chromophore

NinaB is an isomerooxygenase that generates visual chromophore (11-cis-retinal) from carotenoid substrates. Here Solano et al. reveal the structural basis for NinaB isomerase activity, providing new insights into the evolution of visual chromophore synthesis by carotenoid cleavage enzymes.

Yasmeen J. Solano
Michael P. Everett
Philip D. Kiser
ResearchOpen Access14 Feb 2024
Nature Chemical Biology

Volume: 20, P: 779-788
Structural basis for the allosteric modulation of rhodopsin by nanobody binding to its extracellular domain

G protein-coupled receptors (GPCRs) are involved in many physiological processes and are targets of intense drug discovery research. Here, the authors describe llama-derived nanobodies that allosterically modulate rhodopsin, a prototypical GPCR.

Arum Wu
David Salom
Krzysztof Palczewski
ResearchOpen Access25 Aug 2023
Nature Communications

Volume: 14, P: 1-17
Restoration of visual function in adult mice with an inherited retinal disease via adenine base editing

Subretinal viral delivery, in mice, of an adenine base editor and a single-guide RNA targeting a nonsense mutation in the Rpe65 gene restores near-normal levels of retinal and visual functions.

Susie Suh
Elliot H. Choi
Krzysztof Palczewski
Research19 Oct 2020
Nature Biomedical Engineering

Volume: 5, P: 169-178
Catalytic mechanism of a retinoid isomerase essential for vertebrate vision

Retinoid isomerase is a critical enzyme in the conversion of retinyl esters to 11-cis-retinol, a key step in the regeneration of visual pigments that mediate light perception. Structural, biochemical and modeling data using substrate analogs explain how this unusual reaction proceeds.

Philip D Kiser
Jianye Zhang
Krzysztof Palczewski
Research20 Apr 2015
Nature Chemical Biology

Volume: 11, P: 409-415
Targeting G protein-coupled receptor signaling at the G protein level with a selective nanobody inhibitor

G protein-coupled receptors (GPCRs) activate and dissociate the G protein heterotrimer into Gα-GTP and Gβγ dimer, which facilitate distinct signalling events. Here authors develop a nanobody, Nb5 that modulates Gβγ-mediated signaling without affecting GTP-bound Gαq and Gαs-mediated signaling events.

Sahil Gulati
Hui Jin
Krzysztof Palczewski
ResearchOpen Access18 May 2018
Nature Communications

Volume: 9, P: 1-15
LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3

A crystal structure of a chimera composed of lipid-metabolizing transmembrane enzymes HRASLS3 and LRAT (which catalyzes esterification of vitamin A) identifies a quaternary structural rearrangement that coincides with formation of a three-dimensionally swapped dimer.

Marcin Golczak
Avery E Sears
Krzysztof Palczewski
Research10 Nov 2014
Nature Chemical Biology

Volume: 11, P: 26-32

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