Results 61 to 70 of about 2,757,435 (387)

Amino Acid Sequence of Endothiapepsin [PDF]

European Journal of Biochemistry, 1987
The amino acid sequence of endothiapepsin, the aspartic protease from Endothia parasitica has been determined. The enzyme consists of 330 residues. The sequence determination was performed exclusively at the protein level. The homology of this fungal milk-clotting enzyme with aspartic proteases is demonstrated by alignment with pepsin, chymosin ...
openaire   +2 more sources

Variable major proteins of Borrelia hermsii. Epitope mapping and partial sequence analysis of CNBr peptides. [PDF]

, 1985
The variable major proteins (VMP) of serotypes 7 and 21 of the relapsing fever agent Borrelia hermsii were isolated by detergent extraction and high performance liquid chromatography.
Barbour, AG, Barstad, PA, Coligan, JE, Raum, MG   +3 more
core  

Different domains cooperate to target the human ribosomal L7a protein to the nucleus and to the nucleoli. [PDF]

, 1997
The human ribosomal protein L7a is a component of the major ribosomal subunit. We transiently expressed in HeLa cells L7a-β-galactosidase fusion proteins and studied their subcellular localization by indirect immunofluorescence staining with anti-β ...
Giulia RUSSO, PIETROPAOLO C., RICCIARDELLI G.   +2 more
core   +1 more source

Single cis‐elements in brassinosteroid‐induced upregulated genes are insufficient to recruit both redox states of the BIL1/BZR1 DNA‐binding domain

FEBS Letters, EarlyView.
Phytohormone brassinosteroid‐induced gene regulation by the transcription factor BIL1/BZR1 involves redox‐dependent DNA‐binding alternation and interaction with the transcription factor PIF4. The reduced BIL1/BZR1 dimer binds preferred cis‐elements, while oxidation alters its oligomerization state and disrupts DNA‐binding ability.
Shohei Nosaki, Masae Ohtsuka, Takeshi Nakano, Masaru Tanokura, Takuya Miyakawa   +4 more
wiley   +1 more source

Predicting DNA-binding sites of proteins from amino acid sequence

BMC Bioinformatics, 2006
Background Understanding the molecular details of protein-DNA interactions is critical for deciphering the mechanisms of gene regulation. We present a machine learning approach for the identification of amino acid residues involved in protein-DNA ...
Wu Feihong, Terribilini Michael, Yan Changhui, Jernigan Robert L, Dobbs Drena, Honavar Vasant   +5 more
doaj   +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

A working model for cytoplasmic assembly of H/ACA snoRNPs

FEBS Letters, EarlyView.
Dyskerin is the component of nuclear H/ACA ribonucleoproteins (RNPs) endowed with pseudouridine synthase catalytic activity. Two isoforms of human dyskerin have been characterized: the abundant Iso1, mainly nuclear, and the shorter Iso3, mainly cytoplasmic but occasionally imported into nuclei.
Alberto Angrisani, Maria Furia
wiley   +1 more source

Protein sequence alignment with family-specific amino acid similarity matrices

BMC Research Notes, 2011
Background Alignment of amino acid sequences by means of dynamic programming is a cornerstone sequence comparison method. The quality of alignments produced by dynamic programming critically depends on the choice of the alignment scoring function ...
Kuznetsov Igor B
doaj   +1 more source

The Calbindin-D28k binding site on inositol monophosphatase may allow inhibition independent of the lithium site of action [PDF]

, 2011
Among numerous reported biochemical effects the lithium-inhibitable enzyme inositol-monophosphatase (IMPase) remains a viable target for lithium's therapeutic mechanism of action.
Amnon Hoffman, Chaim Gilon, Galila Agam, Itshak Levi, Joseph Fanous, Miriam Eisenstein, Orna Almog, Yael Askira, Yftah Talgan   +8 more
core   +1 more source

Mechanistic basis for inhibition of the extended‐spectrum β‐lactamase GES‐1 by enmetazobactam and tazobactam

FEBS Letters, EarlyView.
Antimicrobial resistance (AMR) is of huge importance, resulting in over 1 million deaths each year. Here, we describe how a new drug, enmetazobactam, designed to help fight resistant bacterial diseases, inhibits a key enzyme (GES‐1) responsible for AMR. Our data show it is a more potent inhibitor than the related tazobactam, with high‐level computation
Michael Beer, Philip Hinchliffe, Marko Hanževački, Christopher R. Bethel, Catherine L. Tooke, Marc W. Van der Kamp, Krisztina M. Papp‐Wallace, Robert A. Bonomo, Stuart Shapiro, Adrian J. Mulholland, James Spencer   +10 more
wiley   +1 more source