| + |
MRPL50 | form complex 
binding
|
39S mitochondrial large ribosomal subunit |
0.697 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262338 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL19 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.727 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262375 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL36 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.731 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262361 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL23 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262370 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL43 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.707 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262353 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL27 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.715 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262368 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL4 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.749 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262357 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL48 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262348 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL40 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.733 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262356 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL17 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262340 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL54 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.67 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262336 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL35 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262362 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL49 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.709 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262347 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL38 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.699 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262359 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL28 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.707 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262367 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL58 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262344 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL20 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.743 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262373 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPS18A | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262334 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL51 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262337 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL42 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262354 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL12 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262381 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL2 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262374 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL52 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262346 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL45 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.727 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262351 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL10 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262383 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL33 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.705 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262364 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL24 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262369 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL46 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262350 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL11 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262382 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPS30 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262342 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL55 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262335 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL41 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.719 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262355 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL57 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.645 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262341 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
GADD45GIP1 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.65 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262385 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL39 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.674 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262358 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL37 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.706 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262360 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL44 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262352 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL21 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262372 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL1 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262384 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL9 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262343 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL14 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.663 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262379 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL22 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.701 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262371 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL53 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.672 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262345 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL32 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.718 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262339 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL16 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.739 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262377 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
rRNA_transcription | up-regulates 
|
39S mitochondrial large ribosomal subunit |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262600 |
|
|
|
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by means of single-particle electron cryogenic microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three ribosomal RNA molecules. |
|
| Publications: |
1 |
| + |
MRPL15 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.708 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262378 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL34 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.676 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262363 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL3 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.719 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262366 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL30 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.683 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262365 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL18 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.653 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262376 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL13 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.758 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262380 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MRPL47 | form complex
binding
|
39S mitochondrial large ribosomal subunit |
0.734 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262349 |
|
|
in vitro |
|
| pmid |
sentence |
| 25838379 |
We have determined the structure of the intact mitoribosome to 3.5 angstrom resolution by single-particle electron cryo-microscopy. It reveals 80 extensively interconnected proteins, 36 of which are specific to mitochondria, and three rRNA molecules |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
39S mitochondrial large ribosomal subunit | up-regulates
|
Protein_synthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262333 |
|
|
|
|
| pmid |
sentence |
| 25838379 |
The highly divergent ribosomes of human mitochondria (mitoribosomes) synthesize 13 essential proteins of oxidative phosphorylation complexes. |
|
| Publications: |
1 |
4.0
39S mitochondrial large ribosomal subunit
CPX-5226