Results 161 to 170 of about 33,782 (294)

Evidence for base-pairing between mammalian U2 and U6 small nuclear ribonucleoprotein particles. [PDF]

, 1990
T P Hausner, L. Giglio, Alan M. Weiner
openalex   +1 more source

Protein tandem repeats that produce frameshifts can generate new structural states and functions

The FEBS Journal, EarlyView.
We explored an alternative protein structure landscape by analyzing amino acid sequences from frameshifted tandem repeats—regions prone to frameshifts. These frameshifts, especially in short repeats, lead to more drastic changes than in non‐repetitive regions, often altering structure, function, localization, and potentially contributing to disease ...
Zarifa Osmanli, Gudrun Aldrian, Jeremy Leclercq, Theo Falgarone, Santiago M. Gómez Bergna, Denis N. Prada Gori, Andrew V. Oleinikov, Ilham Shahmuradov, Andrey V. Kajava   +8 more
wiley   +1 more source

In vitro properties of the first ORF protein from mouse LINE-1 support its role in ribonucleoprotein particle formation during retrotransposition

, 1997
Vladimir O. Kolosha, Sandra L. Martin
openalex   +2 more sources

Structural investigation of human U6 snRNA recognition by spliceosomal recycling factor SART3 RNA recognition motifs

The FEBS Journal, EarlyView.
Human SART3 has two RRM domains to engage with U6 snRNA for spliceosome recycling. This study reports solution structures of SART3 RRM domains and investigates the interaction between RRM and U6 snRNA. SART3 binds to the asymmetric bulge of U6 snRNA as a dimer via conserved positively charged surfaces.
Iktae Kim, Kyeong‐Mi Bang, So Young An, Changkon Park, Ji‐Yeon Shin, Youngim Kim, Hyun Kyu Song, Jeong‐Yong Suh, Nak‐Kyoon Kim   +8 more
wiley   +1 more source

Binding of Bacillus subtilis dynamin‐like protein DynA to the bacterial membrane is essential for effective phage defense

The FEBS Journal, EarlyView.
The bacterial dynamin‐like protein DynA from Bacillus subtilis plays a key role in phage defense. It binds the plasma membrane through a unique paddle domain in its D1 subunit. This membrane association is essential for its protective function, likely preventing explosive membrane rupture following phage infection.
Samia Shafqat, Urska Repnik, Marc Bramkamp   +2 more
wiley   +1 more source

Amino Acid Incorporation in Vitro by Ribonucleoprotein Particles Detached from Guinea Pig Liver Microsomes

, 1960
Jack F. Kirsch, Philip Siekevitz, George E. Palade   +2 more
openalex   +1 more source

LABELLING OF IMMUNOLOGICALLY SPECIFIC PROTEINS BY RIBONUCLEOPROTEIN PARTICLES FROM RAT-LIVER AND CHICK-LIVER CELL SAP [PDF]

, 1963
ALEXANDRA VON DER DECKENA
openalex   +1 more source

Investigating the molecular mechanisms underlying the anti‐CRISPR function of AcrIIA13b protein

The FEBS Journal, EarlyView.
Anti‐CRISPR protein AcrIIA13b inhibits CRISPR–Cas9 function by preventing target DNA engagement. The Cas9–sgRNA ribonucleoprotein (RNP) normally recognizes the protospacer adjacent motif (PAM) duplex to initiate DNA cleavage. AcrIIA13b binding to the PAM‐interacting WED–PI domain blocks this recognition, leaving the target DNA intact.
So Yeon Lee, Hyun Ho Park
wiley   +1 more source

Zebrafish as a model for Catel–Manzke syndrome—identification and characterization of the zebrafish TGDS ortholog

The FEBS Journal, EarlyView.
Zebrafish Tgds, when expressed as a recombinant protein, catalyzes the dehydration of UDP‐D‐glucose, the initial step in the formation of 6‐deoxyhexoses. Corresponding Tgds mutations found in Catel–Manzke syndrome patients lead to reduced enzymatic activity and stability.
Maria Rosaria Coppola, Deianira Bellitto, Erfan Asgari, Virginia Bazzurro, Giorgia Casucci, Francesco Piacente, Matteo Bozzo, Davide Ceresa, Costantino Parisi, Cecilia Winata, Simona Candiani, Michela Tonetti   +11 more
wiley   +1 more source

METABOLISM AND MORPHOLOGY OF RIBONUCLEOPROTEIN PARTICLES FROM THE CELL NUCLEUS OF LYMPHOCYTES

, 1960
John H. Frenster, Vincent G. Allfrey, A. E. Mirsky   +2 more
openalex   +2 more sources