| Hepatitis B virus X protein promotes MAN1B1 expression by enhancing stability of GRP78 via TRIM25 to facilitate hepatocarcinogenesis. | Hepatitis B virus X protein promotes MAN1B1 expression by enhancing stability of GRP78 via TRIM25 to facilitate hepatocarcinogenesis.
You H, Zhang N, Yu T, Ma L, Li Q, Wang X, Yuan D, Kong D, Liu X, Hu W, Liu D, Kong F, Zheng K, Tang R., Free PMC Article | 03/15/2023 |
| MAN1B1-CDG: novel patients and novel variant. | MAN1B1-CDG: novel patients and novel variant.
Kasapkara CS, Olgac A, Kilic M, Keldermans L, Matthijs G, Jaeken J. | 01/22/2022 |
| The cytoplasmic tail of human mannosidase Man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin. | The cytoplasmic tail of human mannosidase Man1b1 contributes to catalysis-independent quality control of misfolded alpha1-antitrypsin.
Sun AH, Collette JR, Sifers RN., Free PMC Article | 12/12/2020 |
| Novel MAN1B1 variants were identified in patients with facial dysmorphism, hypotonia, truncal obesity and in some, behavioural problems. | MAN1B-CDG: Novel variants with a distinct phenotype and review of literature.
Balasubramanian M, Johnson DS, DDD Study. | 03/9/2019 |
| Results show that MAN1B1 expression was higher in bladder cancer (BC) tissues than those in normal tissues. Its overexpression was associated with poor prognosis. Furthermore, MAN1B1 seems to act as an oncogene in BC, which improved the likelihood of MAN1B1 taking on a promising prognostic biomarker. | MAN1B1 is associated with poor prognosis and modulates proliferation and apoptosis in bladder cancer.
Wang HF, Wu JH, Gai JW, Yang SQ, Ma QT, Ma HS, Feng Q. | 10/27/2018 |
| The two genetic associations with severe liver disease that had been suspected previously (one SNP for SERPINA1 and another for MAN1B1) were not confirmed in our cohort. For MAN1B1, four major haplotypes were identified but the prevalence of PHT did not significantly differ between them. | SERPINA1 and MAN1B1 polymorphisms are not linked to severe liver disease in a French cohort of alpha-1 antitrypsin deficiency children.
Joly P, Lachaux A, Ruiz M, Restier L, Belmalih A, Chapuis-Cellier C, Francina A, Renoux C, Bouchecareilh M. | 07/7/2018 |
| in the bound substrate complex, hydrophobic stacking interactions between Trp residues and the glycan core anchor the base of the glycan structure to the enzyme cleft | Substrate recognition and catalysis by GH47 α-mannosidases involved in Asn-linked glycan maturation in the mammalian secretory pathway.
Xiang Y, Karaveg K, Moremen KW., Free PMC Article | 04/7/2018 |
| MAN1B1 defective congenital disorder of glycosylation is reviewed. | Clinical utility gene card for: MAN1B1 defective congenital disorder of glycosylation.
Jaeken J, Lefeber DJ, Matthijs G., Free PMC Article | 02/3/2018 |
| Data show that HIV-1 env protein interacts with alpha-mannosidases ERManI (MAN1B1) and initiates endoplasmic reticulum (ER)-associated protein degradation (ERAD) pathway degradation process. | ERManI (Endoplasmic Reticulum Class I α-Mannosidase) Is Required for HIV-1 Envelope Glycoprotein Degradation via Endoplasmic Reticulum-associated Protein Degradation Pathway.
Zhou T, Frabutt DA, Moremen KW, Zheng YH., Free PMC Article | 02/6/2016 |
| Results suggest that endoplasmic reticulum mannosidase I (ERManI) is turned over by an active autophagic process. | Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates.
Benyair R, Ogen-Shtern N, Mazkereth N, Shai B, Ehrlich M, Lederkremer GZ., Free PMC Article | 10/3/2015 |
| The properties of ERMAN1 enable rapid selection of endoplasmic reticulum-associated degradation substrates in the endoplasmic reticulum.ERMAN1 digests mono-, di- and tri-glucosylated N-glycans. | Trimming of glucosylated N-glycans by human ER α1,2-mannosidase I.
Aikawa J, Takeda Y, Matsuo I, Ito Y. | 05/16/2015 |
| we linked mutations in MAN1B1 to a Golgi glycosylation disorder. Additionally, our results support the recent findings on MAN1B1 localization | MAN1B1 deficiency: an unexpected CDG-II.
Rymen D, Peanne R, Millón MB, Race V, Sturiale L, Garozzo D, Mills P, Clayton P, Asteggiano CG, Quelhas D, Cansu A, Martins E, Nassogne MC, Gonçalves-Rocha M, Topaloglu H, Jaeken J, Foulquier F, Matthijs G., Free PMC Article | 08/23/2014 |
| MAN1B1 deficiency appeared to be a frequent cause in our cohort of patients with unsolved congenital disorder of glycosylation type II. | Diagnostic serum glycosylation profile in patients with intellectual disability as a result of MAN1B1 deficiency.
Van Scherpenzeel M, Timal S, Rymen D, Hoischen A, Wuhrer M, Hipgrave-Ederveen A, Grunewald S, Peanne R, Saada A, Edvardson S, Grønborg S, Ruijter G, Kattentidt-Mouravieva A, Brum JM, Freckmann ML, Tomkins S, Jalan A, Prochazkova D, Ondruskova N, Hansikova H, Willemsen MA, Hensbergen PJ, Matthijs G, Wevers RA, Veltman JA, Morava E, Lefeber DJ. | 05/24/2014 |
| A novel post-transcriptional regulatory mechanism for ERManI via miR-125b and this molecule contributes to the regulation of carcinogenesis in hepatocellular carcinoma. | ERManI is a target of miR-125b and promotes transformation phenotypes in hepatocellular carcinoma (HCC).
Pan S, Cheng X, Chen H, Castro PD, Ittmann MM, Hutson AW, Zapata SK, Sifers RN., Free PMC Article | 04/19/2014 |
| ERManI and gamma-COP contribute to a golgi-based quality control module that facilitates the retrieval of captured ERAD substrates back to the endoplasmic reticulum. | Golgi-situated endoplasmic reticulum α-1, 2-mannosidase contributes to the retrieval of ERAD substrates through a direct interaction with γ-COP.
Pan S, Cheng X, Sifers RN., Free PMC Article | 11/2/2013 |
| Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system | Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system.
Pan S, Wang S, Utama B, Huang L, Blok N, Estes MK, Moremen KW, Sifers RN., Free PMC Article | 12/10/2011 |
| A homozygous nonsense mutation in MAN1B1 segregated with nonsyndromic autosomal-recessive intellectual disability and additional dysmorphic features. | Mutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-recessive intellectual disability.
Rafiq MA, Kuss AW, Puettmann L, Noor A, Ramiah A, Ali G, Hu H, Kerio NA, Xiang Y, Garshasbi M, Khan MA, Ishak GE, Weksberg R, Ullmann R, Tzschach A, Kahrizi K, Mahmood K, Naeem F, Ayub M, Moremen KW, Vincent JB, Ropers HH, Ansar M, Najmabadi H., Free PMC Article | 09/24/2011 |
| Observational study of gene-disease association. (HuGE Navigator) | Polymorphism in the endoplasmic reticulum mannosidase I (MAN1B1) gene is not associated with liver disease in individuals homozygous for the Z variant of the alpha1-antitrypsin protease inhibitor (PiZZ individuals).
Chappell S, Guetta-Baranés T, Hadzic N, Stockley R, Kalsheker N. | 04/7/2010 |
| the identified single-nucleotide polymorphism can accelerate the onset of the end-stage liver disease associated with alpha1-antitrypsin deficiency and underscore the contribution of biosynthetic quality control as a modifier of genetic disease | Single nucleotide polymorphism-mediated translational suppression of endoplasmic reticulum mannosidase I modifies the onset of end-stage liver disease in alpha1-antitrypsin deficiency.
Pan S, Huang L, McPherson J, Muzny D, Rouhani F, Brantly M, Gibbs R, Sifers RN., Free PMC Article | 01/21/2010 |
| ERManI is required for trimming to Man(5-6)GlcNAc(2) and for endoplasmic reticulum associated degradation in cells in vivo. | Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation.
Avezov E, Frenkel Z, Ehrlich M, Herscovics A, Lederkremer GZ., Free PMC Article | 01/21/2010 |
| the true catalytic proton donor is Asp463 in the human endoplasmic reticulum alpha-(1-->2)-mannosidase I | Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1-->2)-mannosidase I.
Cantú D, Nerinckx W, Reilly PJ. | 01/21/2010 |
| overexpression of Golgi alpha1,2-mannosidase IA, IB, and IC also accelerates ERAD of terminally misfolded human alpha1-antitrypsin variant null (Hong Kong) (NHK), and mannose trimming from the N-glycans on NHK in 293 cells | Stimulation of ERAD of misfolded null Hong Kong alpha1-antitrypsin by Golgi alpha1,2-mannosidases.
Hosokawa N, You Z, Tremblay LO, Nagata K, Herscovics A. | 01/21/2010 |
| ER processing alpha1,2-mannosidase (ER ManI) has a role in ER-associated degradation of misfolded proteins | Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I.
Hosokawa N, Tremblay LO, You Z, Herscovics A, Wada I, Nagata K. | 01/21/2010 |
| glycoside bond cleavage proceeds through a least motion conformational twist of a properly predisposed substrate | Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control.
Karaveg K, Siriwardena A, Tempel W, Liu ZJ, Glushka J, Wang BC, Moremen KW. | 01/21/2010 |
| Increased activity of alpha-mannosidase in the peritoneal fluid is associated with gynecologic cancers and pelvic inflammatory disease | Increased activity of lysosomal enzymes in the peritoneal fluid of patients with gynecologic cancers and pelvic inflammatory disease.
Beratis NG, Kaperonis A, Eliopoulou MI, Kourounis G, Tzingounis VA. | 01/21/2010 |